ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
O35386 | MNLTRAGARLQVLLGHLGRPSAPTIVAQPVSGLASPASFQPEQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVSDDDIQRFRAEFERICREEVKPPGIVIMRDVALAKQDYMPSDRMVSKIQDFQEDEELFRYCLLPEILKYVECFTGPNIMALHGMLINKPPDVGKKTSRHPLHQDLHYFPFRPSNLIVCAWTAMEHIDRNNGCLVVLPGTHKGTLKPHDYPKWEGGVNKMYHGIQDYDPNSPRVHLVMEKGDTVFFHPLLIHGSGRNKTQGFRKAISCHFGSSDCQCIDVSGTSQENIAREVVEMAEKKYGFQGVMDFKDTWIFRSRLVKGERINI | Function: Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms) (By similarity). Does not hydroxylate long and very long straight chain acyl-CoAs or 2-methyl-and 4-methyl-branched acyl-CoAs (By similarity).
Catalytic Activity: 2-oxoglutarate + O2 + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA + CO2 + succinate
Sequence Mass (Da): 38607
Sequence Length: 338
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Peroxisome
EC: 1.14.11.18
|
P0DJQ3 | MERIDSHVSPRYAQIPTFMRLPHDPQPRGYDVVVIGAPYDGGTSYRPGARFGPQAIRSESGLIHGVGIDRGPGTFDLINCVDAGDINLTPFDMNIAIDTAQSHLSGLLKANAAFLMIGGDHSLTVAALRAVAEQHGPLAVVHLDAHSDTNPAFYGGRYHHGTPFRHGIDEKLIDPAAMVQIGIRGHNPKPDSLDYARGHGVRVVTADEFGELGVGGTADLIREKVGQRPVYVSVDIDVVDPAFAPGTGTPAPGGLLSREVLALLRCVGDLKPVGFDVMEVSPLYDHGGITSILATEIGAELLYQYARAHRTQL | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: amidinoproclavaminate + H2O = proclavaminate + urea
Sequence Mass (Da): 33401
Sequence Length: 313
Pathway: Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate from D-glyceraldehyde 3-phosphate and L-arginine: step 4/8.
EC: 3.5.3.22
|
Q42440 | MSTGISTDLHVHFGALNFSKTYKSGLSNRTVSFSRVGYAQNRKLSCSVSNTENVAPKDDERGKDRPLVKMCGITSARDAAMAVEAGADFIGMIIWPHSKRSISLSVAKDISKVAREGGAKPVGVFVEDDENTILRAADSSDLELVQLHGNGSRAAFSRLVRKRRVIYVLNANQDGKLLNEVPEEDCHLADWILVDSATGGSGHGFNWAQFKLPSVRSRNGWLLAGGINPTNVSEALSILQPDGIDVSSGICGTDGIQKDKSKISSFITAVRSVHY | Function: Catalyzes the conversion of 5-phosphoribosylanthranilate to l-(O-carboxyphenylamino)-l-deoxyribulose-5-phosphate, which is the third step of the tryptophan biosynthetic pathway.
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 29633
Sequence Length: 275
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
Subcellular Location: Plastid
EC: 5.3.1.24
|
P05121 | MQMSPALTCLVLGLALVFGEGSAVHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP | Function: Serine protease inhibitor. Inhibits TMPRSS7 . Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots . As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading . Acts as a regulator of cell migration, independently of its role as protease inhibitor . It is required for stimulation of keratinocyte migration during cutaneous injury repair . It is involved in cellular and replicative senescence . Plays a role in alveolar type 2 cells senescence in the lung (By similarity). Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis .
PTM: Inactivated by proteolytic attack of the urokinase-type (u-PA) and the tissue-type (TPA), cleaving the 369-Arg-|-Met-370 bond.
Sequence Mass (Da): 45060
Sequence Length: 402
Subcellular Location: Secreted
|
P05120 | MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAVTPMTPENFTSCGFMQQIQKGSYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITNCILFFGRFSSP | Function: Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1.
PTM: The signal sequence is not cleaved.
Sequence Mass (Da): 46596
Sequence Length: 415
Subcellular Location: Cytoplasm
|
P12388 | MEELSMANTMFALNLLKQIEKSNSTQNIFISPWSISSTLAIVLLGAGGNTEQQMAKVLQFNEIGSYGITTRNPENFSGCDFAQQIQKENYPSAILQAQAGDKIHSAFSSLSSTINTPQGDYLLESANKLFGEKSARFKEEYIQLSKKYYSTEPEAVDFLECAEEAREKINSWVKTQTKGEIPNLLPEGSVDEDTKMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSHESIPVQMMFLHAKLNIGYIKDLKTQILELPHTGNISMLLLLPDEIEDASTGLELLESEINFANFNKWISKDTLDEDDVVVYIPKFKLAQSYELKSILQSMGMEDAFNKGKANFSGMSERNDLFLSEVFHQASVDVTEEGTVAAGGTGAVMTGRTGHGGPQFVADHPFLFFIMDKITHTILFVGRFSSP | Function: Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1. Not required for normal murine development or survival.
PTM: The signal sequence is not cleaved.
Sequence Mass (Da): 46292
Sequence Length: 415
Subcellular Location: Cytoplasm
|
P29524 | MEELSMANTMFALNLLKQIEQSNSTQNIFISPWSISSTLAIVFLGAQANTEEQMAKVLNFDKIGSYDLTPGNPENFHGCDFAQHIQRDNYPVAILQAQARDKIHSAFSSLSSTINTPRLGDYLLESANKLFGEKSARFKEEYIQRCKKYYSTEPEAVDFLECANEARKKINSWVKTQTKGEIPNLLPEGSVDEDTKMVLVNTIYFKGRWKTPFQKRLNGLYPFRVNLNESKPVQMMYLREKLNIGYIKDLKTQILELPYIGNISMFLLLPDEIEDSSTGLEMLEREINFDNFNKWISKETLDEDDVLVYIPKFKLAQNYELKPILQRMGMEDAFNKGKADFSGMSESNDLFLSEVFHQATVDVNEEGTVAAGGTGAVMTGRTGHGGPQFVADHPFLFFIMNNITRTILFVGRFSSP | Function: Inhibits urokinase-type plasminogen activator.
PTM: The signal sequence is not cleaved.
Sequence Mass (Da): 47248
Sequence Length: 416
Subcellular Location: Cytoplasm
|
Q8LPI9 | MSTGISSDLHLHPRALNFSKTSKSGLSNRKVSFSSVGYAQNRKLSCSVSSTENVAPKDDDRGKDRPLVKMCGITSARDAAMAVEAGADFIGMIIWPHSKRSISLSVAKDISQVAREGGAKPVGVFVEDDENTILRAADSSDLELVQLHGNSSRAAFSRLVRERKVIYVLNANEDGKLLNVVPEEDGHLADWILVDSATGGRYLDQLLSFFALSHCNVFLRGTSYTITLVHETVCLSQVTEISRV | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 26525
Sequence Length: 244
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
Subcellular Location: Plastid
EC: 5.3.1.24
|
Q6G5H3 | MTIHKAVKRITASEIRSRKGQEPIVSLTAYQAYSARIADPYCDLLLVGDSVGMVVHGFETTLPVSLDMMILHGQAVMRGSKRALVVVDMPFGSYEESPEQAFSNASRILAETGCSAVKLEGGVYIAETIDFLCKRGIPVMSHVGLTPQAVNRFGGFKTQGRNESNWQQIEADAAAIEKAGAFAVVVEGVVEPLAVKLTQMLSIPTIGIGASSQCDGQILVMEDMLGYGTWVPKFVRRYGVLEQEMEKAIKSYADDVKSRTFPSDEEIYKLKQKSG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 29976
Sequence Length: 275
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
Q6MHI3 | MKTILDFHDKKSKKQKISMITCYDYSFARIVADSDIDCILVGDSLAMVMLGHSTTLDVSASVMAHHTAAVVRGAGDKFVIADLPFMSYRKGLTANMTAVEKVMKAGAHAVKLEGAAGNLKLVRHLVDSGVPVMGHLGLTPQSVNQLGGFKVQGRDEKAQKKILEAALQLQDAGAFSVVLECVPSKLAKEITAALEIPTIGIGAGVDCDGQVLVLQDMLGMNQGFKPKFVKTYLDGFNTIKGALNQYHQEVSTEIFPSEKESYS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28276
Sequence Length: 263
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
Q9JZW6 | MITVNTLQKMKAAGEKIAMLTAYESSFAALMDDAGVEMLLVGDSLGMAVQGRKSTLPVSLRDMCYHTECVARGAKNAMIVSDLPFGAYQQSKEQAFAAAAELMAAGAHMVKLEGGVWMAETTEFLQMRGIPVCAHIGLTPQSVFAFGGYKVQGRGGKAQALLNDAKAHDDAGAAVVLMECVLAELAKKVTETVSCPTIGIGAGADCDGQVLVMHDMLGIFPGKTAKFVKNFMQGHDSVQAAVRAYVAEVKAKTFPAAEHIFAD | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 27739
Sequence Length: 263
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
Q82Y18 | MDQSAAKRMTITTLQNACEQGEKIAVLTCYDATFAAVLEEAGVDILLVGDSLGNVVQGKSSTLPVTLDEMIYHVRCVERGTHRVFIMADMPFGTFQVSPQEAFGNAVRLMAAGAQMVKIEGGQHMAETVEFLSCRGIPVCAHIGLMPQFVHQLGGYRVQGKTPNDARQLREDALLLQEAGAAMLLMELIPAVLGEEITRLLSIPTIGIGAGAACSGQVLVLHDMLGISSGTLPRFVRNFMMDADSIQTAVSNYVEAVKLGAFPAYEHTF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28903
Sequence Length: 269
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
A9A2T9 | MHKSVQDIVNMKKGKKKVSVITGYDYTLASLCDKAGIDVLLVGDSAGMVMLGYENTIPVTMDQMCMFTEAVSRARNNALLVADLPFMSYQASIEDAINNSGKLIKAGADAVKLEGGSIMAETISAIVDVGIPVMGHIGLQPQTTMLSQGYKVQGRTKDSAMQLIQDAKELEEAGVFSIALEMVSHEVAQIISETVSAPTIGIGSGVNCDGQVLVVQDLLGMYDKIKPKFAKRYMNLSEDIVKSLEDYKNDVESNTFPAEENWFSMDPEELKKLREQIGS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 30315
Sequence Length: 279
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
Q3JCP9 | MGRLTLTKLQKMKRQGEKITMLTAYDASFAALLEAAGVEVLLVGDSLGMVIQGQESTLSVTMDDMVYHCRNVSRGSQCTFILSDMPFMSYATPNQAMDNAARLMREGGAQMVKLEGGRLLGEIVEHLTARGIPVCAHLGLLPQSVHRIGGYRVQGREEISARRIQEDAMILQEAGADMLILECVPARLGSKITDALKIPVISCGAGPYCDGQVLVLYDMLGISPGKSPSFSRNFLEGTSNIPNAIQAYVSAVKKNEFPLLELSY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28630
Sequence Length: 264
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
A6Q1X8 | MKKRHTVNTIKSAKNSNKLVMITAYDALFAKLFEPIVDMILVGDSLNMVFAGRSDTLSATLDQMIYHANAVCSGAPSAFVVLDMPYGTYINEKEALQNAIRIYKETDVDAVKLEGGKEKADLIKTLCQNGIAVMGHIGLLPQHVRGQGGYKVVREADRLMEDAKALEEAGVFSIIIEGVKPEVAAKVTDAVQVPVIGIGAGKETDGQVLVWSDMLGFFEDFKPKFVKQYLNGAKLVKEAVSQYAKEVKEGSFPSQEFSY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28316
Sequence Length: 259
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
Q72LM0 | MRRTVKDFRNAKGQRLVYLTAYDYPTARLAEAAGVDAILVGDSLGMVVLGYPSTVPVTLEEMLHHTKAARRGAPETFLVADLPYLAYATLDRALLAAERLLKEGGADAVKLEGGEEVAEIVRGLVRAGVPVLGHVGLTPQTASQLGGYKLQGRRPEEAERILKGALALEEAGAYGVVLEMVPARLAKEVTERLSVHTVGIGAGPHTDAQVLVFHDVVGLYGDFKPRFVKRYLEAGRLIQEALSRYAQEVREGVFPGEEHSF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28270
Sequence Length: 261
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
Q8DM44 | MVRRSVTLPQLQAKKALGEPITMLTAWDYLWARLLDAAGVDVILVGDSLGMVALGYPTTLPVTLDQMIHHAQAVRRGVSHSFLVCDLPFLSYQESPEQALRSAGRLIKEAEVQAVKMEGASPVVQAATRRLVEAGIPVLGHVGLLPQRVHQLGGWRQQGNTPQDAAAILAGALALAEAGVFAVILEHIPAALAQQITAQLKIPTIGIGAGPHCDGQVLVTADVLGLSPQVPPFAKVYADLGTQAIAAIENYCQAVKSRQFP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 27660
Sequence Length: 261
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
Q10WG3 | MAVTTKQLIQWKQKGRPIVALTAYDYTIAQLLDNAGVDLILVGDSLGMVTLGYETTLPVTLEEMIHHAKAVRRAVKQALMVVDLPFLTYQESPQQAIHSAGRILKETGAQAVKLESGNEAIAQTVKKLTSIGIPVMGHIGLIPQSVHQFGGYPQQGNAPDASARILTEALALAEAGAFALVLEHIKADLAKEITEKVSIPTIGIGAGAYCDGQILVINDVLGLSHWQPPFAKPYVNLRETITQAVKEYSLEVKKRKFPQPPSP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28403
Sequence Length: 263
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
B3E5K9 | MRKKITIPEILLMKQEGRKVTVLTAYDYPTARLVDAGGVDAILVGDSAGVVFSGHENTLPVTMDEMLYHVKAVVRARPKALVVADMPFMACQSGEIEALKNCGRMLQEGGAEAVKIEGGSNMAPIIRAVTEMDIPVMGHVGLTPQSVHRMGGYKVQGRKDQAERILEDAHAVQEAGAFAVVLEGIPAKLAARITEMLEIPTIGIGAGPACDGQVLVIHDILGLCEKYSPKFVKRYADLAPLITEAARQYVSEVKDGTFPTEEHSFS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28639
Sequence Length: 266
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
Q83GK7 | MICMSRKPSPTRRTRIHRFHKGSCGRKLVGLTCYDFSTARVLSDCELDFLLVGDSASGVIYGYENTGSVCLDEIIYLAAGVVRGAPNSFIIVDLPFGTYEKSDELAVETAIEVIKRTGASAVKLEGGARMACRISAIVRAGVPVMGHIGFTPQTINALGGYKIQGRDNADLIYLDAQAVEQAGAFAVVMEMVTEDLAKTITSEIKITTIGVGAGRYTDGQLLVINDLIGLSEKKITFAPRYASIDNTVASCVKLWRKDVLEGNFPQKDHIPA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 29356
Sequence Length: 272
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
A5CX20 | MNIEALKVFKESGEKITCLTAYDASFASVFDACGIDIILVGDSLGNVIQGDKNTLDVSMSDMIYHMQAVAKGTQNALRIADMPYQSYTYAEQTLTNAKRLIMAGAQMVKLEGGCEHEASFRILQGNDISVCGHLGLQPQSVVEIDGYRVQGRGKQGANKIIKNALALASWGVKVIVLECVPAELAKQVSQSVSIPIIGIGAGLDCDGQVLVSYDMLGVHVRHVPRFVKNFLTDNGDVKSAVNAFIKAVKDKSFPSKKYSY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28082
Sequence Length: 260
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
|
Q2T095 | MKVISSIQELRDQLRGQNRTAFVPTMGNLHEGHLSLMRLARQHGDPVVASIFVNRLQFGPNEDFDKYPRTLQEDIEKLQKENVYVLFAPTERDMYPEPQEYRVQPPHDLGDILEGEFRPGFFTGVCTVVTKLMACVQPRVAVFGKKDYQQLMIVRRMCQQLALPVEIVAAETVRDADGLALSSRNRYLSEAERAEAPELAKTLARVRDAVLDGERDLAAIERRAVAHLSARGWQPDYVSIRRRENLVAPSAAQIEAGDPLVVLTAAKLGATRLIDNLEI | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31400
Sequence Length: 279
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q1DAN8 | MAPAVLKTVADVKDWTAGLRREGHRLALVPTMGFLHEGHLSLIREGRRRADVVAVSIFVNPTQFGPKEDLSRYPRDFEGDVAKCISAGAQAIFAPAGPEVMYPQGYQTYVEVTDVSQGLCGARRPGHFRGVATVVTKLLTLFRPEVALFGEKDYQQLQVIRALNQDLHLGADIVGMPTVREPDGLAMSSRNAYLSPEERQRALALSRGLKAAQALLREGTRESEPLVAAVRRELEAAGLREDYVELVDAERLTPLASVAPGQPARLLVAAFSGTTRLIDNMQLGGEENAGRV | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31778
Sequence Length: 292
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q82Y17 | MEIITDIAPLRARLRHEASVAFVPTMGNLHAGHLSLVRIAQKHASCSVVSIFVNRLQFAPHEDFDRYPRTWSDDCRLLEEQGADIVFMPDEKTLYPVPQEFQLLLPPVADTLEGACRPGFFRGVTTVVLKLFNIVQPHIAVFGEKDYQQLQVVHRMVDQLNLPVEIIAGETVRDEDGLALSSRNNYLDATQRQEAGELAHHLKQIRDSIASGERDFPLLEQLAAEKLSKRGWVVDYVAVRQQHTLLPVAASDSSLVILGAAWLNQTRLIDNFLLTLP | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31131
Sequence Length: 277
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
A6Q581 | MQIVHTPRELKEARIALKGSVGFVPTMGALHQGHLSLIEKSKEHNDYTIVSVFVNPTQFLPGEDFEKYPRRYEADKKICELAGVDILFMPQPDTIYSEDEVLVKAPHQKGYVLEGHFRPGHFDGVLQVVNKLFHIVLPTRAYFGKKDAQQLYLIQKMVQDFFMDIEIVPCEIVRDNDGLALSSRNVYLSDAERKKALLISKSLKRAAKMVQSGILDIQEIQKEMQNILQDLKVEYIAFVDRDFRPLQKIQIGKTIILVAAYVGSTRLIDNIWL | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31241
Sequence Length: 273
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q5Z2U3 | MIDPTLRGAYRPGQLTVHHDPAVLGSVAKALRGVGRTVALVPTMGALHQGHLQIVRQAKRTNQVVIVSIFVNPLQFGAGEDLDKYPRTLDADVELLRAEGVELVFAPNAEQMYPDGPRTTVHPGPLGAELEGASRPTHFAGMLTVVAKLLQIARPHQAFFGEKDYQQLTLIRQMVRDLNFDVRIVAVPTVRESDGLALSSRNRYLDAAQRETALALSAALSAGAHAGGLGAEGVLAAARAVLDATPGLDLDYLELRSSTLGPAPASGNARLLVAAKVGTTRLIDNIAVTLGAPIDGHPNLDSQPEPAGTDPALLPPAR | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 33561
Sequence Length: 318
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
A1SDW7 | MSSAPVLAHTREELATLLAAARARGEQVGLVPTMGALHEGHASLVRAARERVTDDGRMGPVVVSVFVNPLQFGANEDLDRYPRTLEADLEVCAREGADIVFAPSVDEVYPGGPPQVTVRPGPLGKILEGKVRPGHFRGVLTVVAKLFGLVRPDVAVFGQKDYQQLALIRRMVLDLALGVEIVAAETVREDDGLALSSRNRYLEPEQREQAVALSRALLAAQENAGYGAEVALDEARAELRAAPGVDLDYLVITDPDLDELPAVVPPGTPARILVAARVGGTRLIDNLPLMLGTRGPAGEASPPNRERSEPGSAEQNKSPGEARTTPSGTSEASE | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 35428
Sequence Length: 334
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
P40459 | MKIFHTVEEVVQWRTQELRETRFRETIGFVPTMGCLHSGHASLISQSVKENTYTVVSIFVNPSQFAPTEDLDNYPRTLPDDIKLLESLKVDVLFAPNAHVMYPQGIPLDIEEQKGPFVSVLGLSEKLEGKTRPNFFRGVATVVTKLFNIVMADVAYFGQKDIQQFIVLQCMVDELFVNTRLQMMPIVRNNNGLALSSRNKYLCPESLKISENLYRGLKAAENAIRRLAPGGRLSRSEIIDTVTQIWAPYVDSHDFKIDYVSLADFKTLDELSDVENTSEQQPIVISCAVYVTDREKPDTVVRLIDNIVI | Function: Required for pantothenic acid biosynthesis.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 35032
Sequence Length: 309
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q9EYU1 | MRKLVAGKLHGIHVTEANLNYHGSITLDPDHCEAAGILPMEFVEIWNKNSGARISTYVILGERGSRCCILNGAAARTCQPDDPIIVCNSIYLDEAHITSLKPRIVTFDQDNHILDRLSYSVDIDTDGRYSFAILDEADEPLVIPALVSGA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 16449
Sequence Length: 150
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
Q7NDK7 | MLRTVLLGKIHRATVTGACLEYVGSISVDSRLLAAAGILPHEQVHVVNLNNGARLVTYAIEASEGSGAVVLNGAAARLAAAGDQVIVLAYGQGTAVELEHHQPQVVYVDAQNRIVSVHRSVEHAG | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 13053
Sequence Length: 125
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
B7K6Z1 | MGKIRLMHAKLHRVRVTEANVGYIGSITIDPQLLDRVGILPLEEVDIVNLNNGKRFSTYVFPGEAGTGEVCPNGGAALLCQPGDLLIIYAYEERDRSEVLQQGHHARVIVADENNQIKQFFHQTLIPTEEGKGVSFHSDEIILNGQPKNNPILSEN | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 17283
Sequence Length: 156
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
A1WUU3 | MQLNMLKGKLHQARVTQTELEYEGSCAIDLDLLEAVGIHEYEQIHVYNIENGERFVTYAIIGERGSRMISMNGAAAHKCNEGDRVIICAYAGVPESELGEFQPRLAYLDADNRITQRRGSIPLQVA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 14095
Sequence Length: 126
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
Q18HQ3 | MRRWLLKSKLHRARVTGTEKDYEGSISIDAALLSEADIAVGEQVQVVNVTNGERFETYTIEGESRQMELNGAAARLAETGDVIIVISYGLYVKDEQPEPTVLLLDEENRISERE | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 12796
Sequence Length: 114
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
Q7VJB2 | MQFEMLYSKIHRAKVSDANLNYVGSITIDKTLAQSANLLAGMKVEIVNINNGERFSTYVIYGDKKGEICLNGAAARKVQIGDIIIIIAYATYTHNELEHYKPTIVQVNESNQILSITNEV | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 13378
Sequence Length: 120
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
P56065 | MTFEMLYSKIHRATITDANLNYIGSITIDEDLAKLAKLREGMKVEIVDVNNGERFSTYVILGKKRGEICVNGAAARKVAIGDVVIILAYASMNEDEINAHKPSIVLVDEKNEILEKG | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 12939
Sequence Length: 117
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
Q118E6 | MTTIKLMHAKLHRVRVTDAKPDYVGSVTIDSDLLEKVGILPLEEVQIVNLNNGQRWLTYVLPGQAGSGMVCPNGGAALLCKKDDILIIWANEQCDRAEVLENGHKAKIFVADENNHCREFLYQILNPNQGSVEFHSLPVIPEGKTSEYLQQMIETNKI | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 17668
Sequence Length: 158
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
A5CW02 | MKRIFLSAKLHKVTTTAVELNYEGSCEIDGVLLDAAGIGAFEQIQIYNINNGNRFTTYTILGKDNSGIISVNGAAARKVNVGDVLIIAAYALYSEEELEGYAPRLCYVNNKNILTKISTGSKKSSLY | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 13815
Sequence Length: 127
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
Q8PLK9 | MHLSLLKAKIHRATVTHSELNYEGSIAIDGLLLEATGIREFEQVHIWDVTNGARFSTYAIRAEDGSGIMSLNGGAARHVQVGDLIIVAAFASMSEDEAKTFKPNLVYVNAHNAISHTNHSIPTQAA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 13623
Sequence Length: 126
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
Q9PGR7 | MQLSLLKAKIHRATVSHSELNYEGSIAIDGLLLEAAGLYEFEKVHIWNVTNGARFTTYAIRAEHGSGIISVNGGAARYVQVGDLVIVAAFAQMSEDEAAVFSPNLVYVDAANAMTHTNHSIPTQVA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 13528
Sequence Length: 126
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
A1JJN6 | MIRTMLQGKLHRVKVTQADLHYEGSCAIDQDFLEAAGILEYEAIDIYNVDNGQRFSTYAIAAERGSRIISVNGAAARCACVGDKLIICSYVQMSDADARLHHPKVAYFEGENQLQRKAKAVPVQVA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 13902
Sequence Length: 126
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
P53632 | MGAKSVTASSSKKIKNRHNGKVKKSKKIKKVRKPQKSISLNDENEVEILPSRNEQETNKLPKDHVTADGILVLEHKSDDDEGFDVYDGHFDNPTDIPSTTEESKTPSLAVHGDEKDLANNDDFISLSASSEDEQAEQEEEREKQELEIKKEKQKEILNTDYPWILNHDHSKQKEISDWLTFEIKDFVAYISPSREEIEIRNQTISTIREAVKQLWPDADLHVFGSYSTDLYLPGSDIDCVVTSELGGKESRNNLYSLASHLKKKNLATEVEVVAKARVPIIKFVEPHSGIHIDVSFERTNGIEAAKLIREWLDDTPGLRELVLIVKQFLHARRLNNVHTGGLGGFSIICLVFSFLHMHPRIITNEIDPKDNLGVLLIEFFELYGKNFGYDDVALGSSDGYPVYFPKSTWSAIQPIKNPFSLAIQDPGDESNNISRGSFNIRDIKKAFAGAFDLLTNRCFELHSATFKDRLGKSILGNVIKYRGKARDFKDERGLVLNKAIIENENYHKKRSRIIHDEDFAEDTVTSTATATTTDDDYEITNPPAKKAKIEEKPESEPAKRNSGETYITVSSEDDDEDGYNPYTL | Function: Catalytic subunit of the TRAMP complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Polyadenylates RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. TRF4 is also required for proper nuclear division in mitosis, DNA damage repair and sister chromatid cohesion. Involved in the regulation of histone mRNA levels. May mediate mitotic chromosome condensation.
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 66031
Sequence Length: 584
Subcellular Location: Nucleus
EC: 2.7.7.19
|
Q9LW57 | MATSSTFSSLLPSPPALLSDHRSPPPSIRYSFSPLTTPKSSRLGFTVPEKRNLAANSSLVEVSIGGESDPPPSSSGSGGDDKQIALLKLKLLSVVSGLNRGLVASVDDLERAEVAAKELETAGGPVDLTDDLDKLQGKWRLLYSSAFSSRSLGGSRPGLPTGRLIPVTLGQVFQRIDVFSKDFDNIAEVELGAPWPFPPLEATATLAHKFELLGTCKIKITFEKTTVKTSGNLSQIPPFDIPRLPDSFRPSSNPGTGDFEVTYVDDTMRITRGDRGELRVFVIA | Function: Required for plastoglobule development and resistance to multiple stresses. Regulates plastoglobule osmiophilic content. May be involved in the transport of lipophilic antioxidants in and out of the plastoglobule.
PTM: Phosphorylated as part of a basal defense response.
Sequence Mass (Da): 30455
Sequence Length: 284
Subcellular Location: Plastid
|
P00784 | MAMIPSISKLLFVAICLFVYMGLSFGDFSIVGYSQNDLTSTERLIQLFESWMLKHNKIYKNIDEKIYRFEIFKDNLKYIDETNKKNNSYWLGLNVFADMSNDEFKEKYTGSIAGNYTTTELSYEEVLNDGDVNIPEYVDWRQKGAVTPVKNQGSCGSCWAFSAVVTIEGIIKIRTGNLNEYSEQELLDCDRRSYGCNGGYPWSALQLVAQYGIHYRNTYPYEGVQRYCRSREKGPYAAKTDGVRQVQPYNEGALLYSIANQPVSVVLEAAGKDFQLYRGGIFVGPCGNKVDHAVAAVGYGPNYILIKNSWGTGWGENGYIRIKRGTGNSYGVCGLYTSSFYPVKN | Function: Cysteine proteinase with a high level of diversity in substrate specificity, an amino acid bearing a large hydrophobic side chain at the P2 position is preferred.
Catalytic Activity: Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'.
Sequence Mass (Da): 38922
Sequence Length: 345
EC: 3.4.22.2
|
Q45066 | MSQPELFHDLPLEEVIGDRFGRYSKYIIQDRALPDARDGLKPVQRRILYAMHTDGNTFDKNFRKAAKTVGNVIGNYHPHGDSSVYEAMVRMSQDWKVRNVLIEMHGNNGSIDGDPPAAMRYTEARLSPIASELLRDIDKNTVEFVPNFDDTSKEPVVLPAMFPNLLVNGSTGISAGYATDIPPHHLGEVIDAVIKRIQMPSCSVDELMEVIKGPDFPTGGIIQGVDGIRKAYETGKGKIIIRGKAEIETIRGGREQIVITEIPFEVNKANLVKKMDEFRIDKKVEGISEVRDETDRTGLRVVIELKKEADAKGILNFLYKNTDLQITYNFNMVAIHNRRPMLMSLPSILDAYIGHQKEVVTNRSVYELQKAKDRHHIVEGLMKALSILDEVIATIRSSSDKRDAKNNLIAKYEFTEPQAEAIVSLQLYRLTNTDITALKEEAEELGKKIEELESILSNDKKLLKVITNSLKALKKKYADTRRSVIEEKIEEIKINLEVMVASEDVYVTVTKDGYLKRTSQRSFAASNGQDFGMKDTDRMLHQFEMNTTDVLLLFTNKGSYIYCPVHQLPDIRWKDMGQHFSNLITIDRDETIVKAIPIKEFDPSAYLLFFTKNGMVKKTELTHYKAQRYSKALVALNLKGEDELIDVHVTNGESQIFMATHLGYGLWFGEDEVNVVGARAAGVKGINLKEDDFVVSGEILQQSDSIVLFTQRGAVKRMSLSEFEKTSRAKRGVVMLRELKKNPHRVVALFACGLEQRLMAETEKGDRKELQTKELRTNDRYSNGSFFFDEEESGKVTAVWRLHTEQ | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 91321
Sequence Length: 806
Subcellular Location: Cell membrane
EC: 5.6.2.2
|
O51066 | MDIRTVLKDNFLQYSSYVIKDRAIASVVDGFKPVQRRIIHSLFEMHDGNFHKVANVVGNTMKYHPHGDTSIYEALVNIANKDLFIEKQGNFGNLFTGDPASASRYIECRLTPLAFDVLYSKEITIYESSYDGRNNEPLLYPAKIPVILIQGSEGIAVGMAAKILPHNFNEILNAVKSELLGESYDIYPDFPTGGIVDVNEYADGNGKVLVRAKIETIDEKTIVIRELPFGETTESLISSIEKAIRKNYIKVSSINDFTAENVAIELSLPRGVYASEVIEKLYHYTNCQISISVNLLLLSERYPVVYTIKDLIKFHAAHLQKILKMELELQKSKILEKIFYKTLEQIFIEKKIYKLLETISKEENILSIILSEVLRHKESFSREVLKEDVENLLKIPIRKISLFDIDKNSKDIKILNKELKSINSNISSIRGYSINFIDLLLAKYSKEHQRKTKISLIKSKNVKEIATKNMKVYLNLAEGFAGTSLFDGEFIGNASYYDKILVFRENSYVLKNIEDKTFIDKKNVCALVYDINNSKEQIFSIIYFNRLDNFYYVKRFKIDKFITDKVYEFLGENDEFVDFSLNPEFVEFSTNKDIVKRIEIDNFMVKSRSSIGKRISSNNLKKVKFK | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule (By similarity).
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 72042
Sequence Length: 626
Subcellular Location: Cell membrane
EC: 5.6.2.2
|
O54478 | MNKPVLPPPGGPDDGDRILDEPLTEALSRRYLAYALSTIGSRALPDVRDGLKPVHRRVLYAMSNMRLNPDAAARKCAKVVGEVMGNFHPHGDASIYDALVRLAQEFSQRIPLVEGQGNFGNIDGDSAAAMRYTECKMTEAAMLLLDGIDEDAVDFRPTYDGQDEEPVVLPSGFPNLLANGSSGIAVGMATSIPPHNAAELIDACQLLLANPDATTADLLEKVPGPDFPTGGVIVESRASLLETYETGRGGVRMRAKWEKEDTGRGTYQIVVTEIPYQVKKSDLVEQLADLIDSKKAALLGDVRDESAEDIRLVLEPKSKNVEPEVLMESLFKLSALESRFPVNINVLDARGTPGVMGIKQALMAFLAHRREVLTRRARHRLAKIEARLHILDGLLIAYLNLDEVIRIVRYEDKPKEKLIETFGLTDIQADAILNTRLRQLAKLEEMEIRREHAELVEERDGILAMLASEAKQWKLVGVGLSEVRAALLKIKHPLDKPRPTGVTGRSVFGEAPQVDADAAIEAMIVREPITIILSERGWIRAAKGKIDDPSELKFKEGDKLGFLVPAETTDKLLIFSSDGRFFTLGCDKLPSARGHGEPVRMMIELDDKVKIIDVFPFKAGRKRILASKGGYGFLMPEEEALANRKAGKQVLNVGNEGAAFCLEAVGDQLAVIGDNGKILIFPLEELPEMPRGKGVKLQAYREGGLRDGLSFNAETGAYWIDTAGRRRDWAEWKEWVGRRAGAGKLVPKGFATNKRFRPK | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 83521
Sequence Length: 759
Subcellular Location: Cell membrane
EC: 5.6.2.2
|
P47446 | MDQKNNNLFQKAIEEVFAVSFSKYAKYIIQDRALPDLRDGLKPVQRRILYGMFQMGLKPTTPYKKSARAVGEIMGKYHPHGDSSIYDAIIRMSQSWKNNWTTVSIHGNNGSVDGDNAAAMRYTETRLSLYGFELLKDIDKKLVSFINNFDDSEKEPTVLPTLLPNLFINGASGIAAGYATNIAPHNTNELLDSLCLRIDQPNCELKQILKIVKGPDFPTGGNVYFEKSLSDIYQAGKGKFIIQAKYEVNKNLNQIEITQIPYETLKANIVKQIEEIIFDNKLSAIESVIDSSDRNGIRIIIKHKDFLPAEKIMAFLFKHTQLQVNFNLNNTVIANRFPIQIGLLSYLDHFLKFCHELIINKAKYELELASKRLEIILGLIKAISIIDKIIKLIRSAVDKSDAREKLIDNFKFTFNQAEAIVSLRLYQLTNTDIFELNQEQNELEKTVISSEQLIASEKARNKLLKKQFEGYKKQFHQQRRSQICGFINQKKVEESELIENKTYGVLITKAGNYHKFESNQLLKSTTDFKSESDTIIFAQTIANTDQIFIVTSLGNIINIPVYKLAFNSKNKLASLVSKKPILLEYETIVFVGTMNSVNQPILVLTSKLGMVKRIDLTKLNIKPLKATLCISLRDKDHLVSAFLQQDDKLICLVSDHNYYTVFHTNEIPLISSKGMGVKGMKLKLEDQIKFVVAFEANEPLVMICSDGSVINLKQTELVVVSRMATAKKLPVKKAINYCFSDATNTQLINFQGKNGSKLITTSELNQMSKTAISQTRFNKLN | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 88513
Sequence Length: 781
Subcellular Location: Cell membrane
EC: 5.6.2.2
|
P48374 | MNTQPHASHTDSNTLMLGRYAERAYLEYAMSVVKGRALPEVSDGQKPVQRRILFAMRDMGLTAGAKPVKSARVVGEILGKYHPHGDSSAYEAMVRMAQDFTLRYPLIDGIGNFGSRDGDGAAAMRYTEARLTPIAELLLSEINQGTVDFMPNYDGAFDEPLHLPARLPMVLLNGASGIAVGMATEIPSHNLNEVTQAAIALLKKPTLETADLMQYIPAPDFAGGGQIITPADELRRIYETGKGSVRVRARYEIEKLARGQWRVIVTELPPNANSAKILAEIEEQTNPKPKAGKKQLNQDRLNTKKLMLDLIDRVRDESDGEHPVRLVFEPKSSRIDTDTFINTLMAQTSLEGNVSMNLVMMGLDNRPAQKNLKTILQEWLDFRIVTVTRRLKFRLNQVEKRLHILEGRLKVFLHIDEVIKVIRESDDPKADLMAVFGLTEIQAEDILEIRLRQLARLEGFKLEKELNELREEQGRLNIFLGDENEKRKLIIKEMQADMKQFGDARRTLVEEAGRAVLTQTAADEPITLILSEKGWIRSRAGHNLDLSQTAFKEGDRLKQTLEGPHCFTRRHPRFIRGRTYSIDAAEIPGGRGDGVPVSSLIELQNGAKPVAMLTGLPEQHYLLSSSGGYGFIAKLGDMVGRVKAGKVVMTADSGETVLPPVAVYASSFINPDCKIIAATSQNRALAFPIGELKIMAKGKGLQIIGLNAGESMTHTAVSSEPEILIESEGRRGAAHKDRLPVALIEAKRGKKGRLLPISGSLKQLSSPK | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 84896
Sequence Length: 768
Subcellular Location: Cell membrane
EC: 5.6.2.2
|
Q9HUK1 | MSESLDLSLEGVERRSLAEFTEQAYLNYSMYVIMDRALPHIGDGLKPVQRRIVYAMSELGLDADSKHKKSARTVGDVLGKFHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTEARLSRYSEVLLSELGQGTVDWVPNFDGTLDEPAVLPARLPNLLLNGTTGIAVGMATDVPPHNLREVASACVRLLDQPGATVAELCEHVPGPDFPTEAEIITPRADLQKVYETGRGSVRMRAVYRVEDGDIVIHALPHQVSGSKVLEQIAGQMQAKKLPMVADLRDESDHENPTRIVIIPRSNRVDVEELMTHLFATTDLETSYRVNLNIIGLDGKPQVKDLRQLLSEWLQFRIGTVRRRLQFRLDKVERRLHLLDGLLIAFLNLDEVIHIIRTEDQPKAVLMERFELSEVQADYILDTRLRQLARLEEMKIRGEQEELLKEQKRLQTLLGSEAKLKKLVREELIKDAETYGDDRRSPIVARAEARALSETELMPTEPVTVVLSEKGWVRCAKGHDIDAAGLSYKAGDGFKAAAPGRSNQYAVFIDSTGRSYSLPAHSLPSARGQGEPLSGRLTPPPGASFECVLLPDDDALFVIASDAGYGFVVKGEDLQAKNKAGKALLSLPNGSAVVAPRPVRDVEQDWLAAVTTEGRLLLFKVSDLPQLGKGKGNKIIGIPGERVASREEYLTDLAVLPAGATLVLQAGKRTLSLKGDDLEHYKGERGRRGNKLPRGFQRVDSLLVDIPPQD | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 83365
Sequence Length: 754
Subcellular Location: Cell membrane
EC: 5.6.2.2
|
Q59749 | MGQSLLPPSGGDDNIQPVDLKAALEERYLAYALSTIMHRALPDVRDGLKPVHRRIIHAMSEMGLRPNSSFKKCARIVGDVIGKFHPHGDQSVYDALVRLAQDFSQRYPVVDGQGNFGNIDGDNAAAYRYTEAKMTEVAALLLEGIDQDAVDFRPTYNEEDQEPTVLPGAFPNLLANGASGIAVGMATSIPPHNAHELCDAALHLIKHPDATVEDLLFDPANPQRGGIEGPDFPTGGVIVESRASMAESYRTGRGGFRVRARWAVEDLGRGGFQIVVTEIPYQVQKSRLIEKIAELLIARKLPLLEDIRDESAEDVRVVLVPKSRSVDANILMESLFKLTELESRIPLNMNVLSMGRVPRVMALNEVLSEWLAHRREVLQRRSRHRLAAIDRRLEILGGYLIAYLNIDEVIRIIREEDEPKAVMIERFGLTDVQAEAILNMRLRSLRKLEEFEIRTEFDSLSKEKAEIEALLASGDKQWQAVAWEIGEVKKKFAKATELGKRRSTFSDAPDADVEAIQQAMIEKEPITVVISEKGWIRALKGHIADTSSLQFKDGDGLKVSFPAQTTDKILIFTTGGKAYTLGGDKLPGGRGHGEPLRIMVDMENDQDVLTAFVHDPARKLIVSSTAGNGFVVTESDIVANTRKGKQVMNVTMPDEAKLVVPVKGDHLAVVGENRKMLVFPLVQVPEMARGKGVRLQRYKDGGVSDIRSFAIAEGLTWEDSAGRVFTKTRDELIEWMGDRAGAGRVVPKGFPRSGKFSG | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 83754
Sequence Length: 758
Subcellular Location: Cell membrane
EC: 5.6.2.2
|
Q9ZE79 | MKEAKIENIDFGNALSERYLAYALSTIMSRSLPDVRDGLKPVHRRLLYAMLQLRLEPNSGYKKCARVVGDVIGKYHPHGDVAVYDTLVRLAQHFSLRYPLIDGQGNFGSIDGDNAAAMRYTESRMTEICMLLMEDIDKDTVDFRSTYDDSDLEPVIMPASFPNLLANGSEGIAVGMATNIPPHNLHELCDALLYLIDNPQAGINDIMNFIKGPDFPTGGIIIDKAEVINAAYTTGRGSFRVRSRWEKEELSYGTYQIVVTEIPYQIQKSKLIEQIAILLKDKKIPLISSIRDESTDIIRVVIEPRDRSCDPQIVMESLFKLTNLESRIQLNMNVIGSNNVPRVMNILEILQEFLVHRKNIIIRRSTYLLNKIKQRLEILKVLRIVYLNLDEIIEIIREEDEPKTIIMERFKISAIQVEVILNTRLRSLQKLEEHAIIDEHSNLQKQQAILEKILKNHKELWQIVKKEIKAVQTKFGLNTIIGARRTSFEEVDLTNQVVDITAFITKEPITIICSKMGWVRSLKGHNTDLSTIKYKEGDTEKFIIEAYTTDKILIISSKGRFFTLLADNISKGKGTGGVSIKLLVDIGNNDITNILVYKPNQLLLLASSIGKGFLVNSNEVIAQTKTGKQIMNIPEGYSCIACLPVNGDSIACIGESRRLLVFNIDEIPEMKKGQGVVLQRFKNAKLLDIKIFNKQDGLSWNDGTKIQLEKNIVAFLGKRGGFGTFPPIGFPKNNRFSP | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 83348
Sequence Length: 738
Subcellular Location: Cell membrane
EC: 5.6.2.2
|
P26973 | MSDMAERLALHEFTENAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNATAKFKKSARTVGDVLGKYHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKYAELLLSELGQGTADWVPNFDGTMQEPKMLPARLPNILLNGTTGIAVGMATDIPPHNLREVAKAAITLIEQPKTTLDQLLDIVQGPDYPTEAEIITPRAEIRKIYENGRGSVRMRAVWTKEDGAVVISALPHQVSGAKVLEQIAAQMRNKKLPMVDDLRDESDHENPTRLVIVPRSNRVDMEQVMNHLFATTDLEKSYRINLNMIGLDGRPAVKNLLEILTEWLAFRRDTVRRRLNYRLEKVLKRLHILEGLLVAFLNIDEVIEIIRSEDEPKPALMSRFGISETQAEAILELKLRHLAKLEEMKIRGEQDELEKERDQLQGILASERKMNTLLKKELQADADAYGDDRRSPLREREEAKAMSEHDMLPSEPVTIVLSQMGWVRSAKGHDIDAPGLNYKAGDSFKAAVKGKSNQPVVFIDTTGRSYAIDPITLPSARGQGEPLTGKLTLPPGATVEHMLMEGDDQKLLMASDAGYGFVCTFNDLVARNRAGKTLITLPENAHVMPPLVIEDEHDMLLAITQAGRMLMFPVDSLPQLSKGKGNKIINIPSAEAAKGDDGLAHLYVLPPQSTLTIHVGKRKIKLRPEELQKVVGERGRRGTLMRGLQRIDRIEIDSPHRVSHGDSEE | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA . Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 84038
Sequence Length: 752
Subcellular Location: Cell membrane
EC: 5.6.2.2
|
Q99LX0 | MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVMICPDTSLEDAKTQGPYDVVVLPGGNLGAQNLSESPMVKEILKEQESRKGLIAAICAGPTALLAHEVGFGCKVTTHPLAKDKMMNGSHYSYSESRVEKDGLILTSRGPGTSFEFALAIVEALVGKDMANQVKAPLVLKD | Cofactor: Deglycase activity does not require glutathione as a cofactor, however, glycated glutathione constitutes a PARK7 substrate.
Function: Multifunctional protein with controversial molecular function which plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease . It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway . Has been described as a protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. But this function is rebuted by other works. As a protein deglycase, repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Protects histones from adduction by methylglyoxal, controls the levels of methylglyoxal-derived argininine modifications on chromatin. Able to remove the glycations and restore histone 3, histone glycation disrupts both local and global chromatin architecture by altering histone-DNA interactions as well as histone acetylation and ubiquitination levels. Displays a very low glyoxalase activity that may reflect its deglycase activity . Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death . Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria . Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking . Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells . In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting . Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress (By similarity). Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity . In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis .
Catalytic Activity: H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate
PTM: Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential for cell-growth promoting activity and transforming activity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20021
Sequence Length: 189
Subcellular Location: Cell membrane
|
Q2KHV4 | MAWRGWAQRGWGCGQAWTLPVCGGSYEELTAALAPSRLLRRRFNFFIQQKCGFRKAPRKVEPRRSDTSSEAYKRSALIPPVEETAFYPSPYPIRTLVKPLFFTVGFTGCAFGSAAIWQYESLKSKVQSYFDGIKADWLDSIRPQKEGDFRKEINKWWNNLSDGQRTVTGIIAANVFVFCLWRVPSLQRTMIRYFTSNPASKVLCSPMLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFMAVYLSAGVISTFVSYVCKVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPMFTFTAGNALKAIIAMDTAGMILGWKFFDHAAHLGGALFGIWYITYGHELIWKNREPLVKIWHEMRTNSPKKGGGSK | Function: Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptotic signals. Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP). Promotes cleavage of serine/threonine-protein phosphatase PGAM5 in damaged mitochondria in response to loss of mitochondrial membrane potential. Mediates differential cleavage of PINK1 and PGAM5 depending on the health status of mitochondria, disassociating from PINK1 and associating with PGAM5 in response to mitochondrial membrane potential loss. Required for processing of CLPB into a form with higher protein disaggregase activity by removing an autoinhibitory N-terminal peptide. Promotes processing of DIABLO/SMAC in the mitochondrion which is required for DIABLO apoptotic activity. Also required for cleavage of STARD7 and TTC19. Promotes changes in mitochondria morphology regulated by phosphorylation of P-beta domain.
PTM: P-beta is proteolytically processed (beta-cleavage) in a PARL-dependent manner.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
Sequence Mass (Da): 42301
Sequence Length: 377
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.21.105
|
A1Z8R8 | MLMSRALCRSWLPQVARRCHANVNVPILRINSGHPAARSCRQIHSNRKQSSNLKPTTGEPAAAEQNTPVPVNNVIKAVAFTGAFTVGCFAGATILEYENTRSLILEKARQARFGWWQSRSLADRDYWTQIKQDIRRHWDSLTPGDKMFAPILLCNLVAFAMWRVPALKSTMITYFTSNPAAKVVCWPMFLSTFSHYSAMHLFANMYVMHSFANAAAVSLGKEQFLAVYLSAGVFSSLMSVLYKAATSQAGMSLGASGAIMTLLAYVCTQYPDTQLSILFLPALTFSAGAGIKVLMGIDFAGVVMGWKFFDHAAHLGGAMFGIFWATYGAQIWAKRIGLLNYYHDLRRTKQK | Function: Mitochondrial intramembrane protease which plays a critical role in the regulation of mitochondrial function . Essential for mitochondrial development and fusion during spermatogenesis and the development of neurons and muscles . Essential for proteolytic processing of Pink1 and HtrA2 into their mature forms . May also be involved, but not required, for the proteolytic processing of Opa1 .
Catalytic Activity: Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38932
Sequence Length: 351
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.21.105
|
Q9H300 | MAWRGWAQRGWGCGQAWGASVGGRSCEELTAVLTPPQLLGRRFNFFIQQKCGFRKAPRKVEPRRSDPGTSGEAYKRSALIPPVEETVFYPSPYPIRSLIKPLFFTVGFTGCAFGSAAIWQYESLKSRVQSYFDGIKADWLDSIRPQKEGDFRKEINKWWNNLSDGQRTVTGIIAANVLVFCLWRVPSLQRTMIRYFTSNPASKVLCSPMLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFMAVYLSAGVISNFVSYVGKVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPMFTFTAGNALKAIIAMDTAGMILGWKFFDHAAHLGGALFGIWYVTYGHELIWKNREPLVKIWHEIRTNGPKKGGGSK | Function: Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptotic signals (By similarity). Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP) . Promotes cleavage of serine/threonine-protein phosphatase PGAM5 in damaged mitochondria in response to loss of mitochondrial membrane potential . Mediates differential cleavage of PINK1 and PGAM5 depending on the health status of mitochondria, disassociating from PINK1 and associating with PGAM5 in response to mitochondrial membrane potential loss . Required for processing of CLPB into a form with higher protein disaggregase activity by removing an autoinhibitory N-terminal peptide . Promotes processing of DIABLO/SMAC in the mitochondrion which is required for DIABLO apoptotic activity . Also required for cleavage of STARD7 and TTC19 . Promotes changes in mitochondria morphology regulated by phosphorylation of P-beta domain .
PTM: P-beta is proteolytically processed (beta-cleavage) in a PARL-dependent manner. The cleavage is inhibited when residues Ser-65, Thr-69 and Ser-70 are all phosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
Sequence Mass (Da): 42190
Sequence Length: 379
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.21.105
|
Q3B8P0 | MALYSWVQRGWRCGQTWAPLLGGGYRELSATQARQLLGRRFNLLLQQKCGFRKAPRKVEPRRSDTGSSGEAYKRSALIPPLEETVFYPSPYPVRTLLKPFFFTVGFTGCAFGSAAIWQYESLKSRVQSYFDGIKADWLDSIRPQKEGNLRKEINKWWNSLSDGQRTVTGIIAANALVFCLWRVPSLHRTMIRYFTSNPASKVLCSPMLLSTFSHFSLFHMAANMYVLWSFSTSIVNILGQEQFVAVYLSAGVISNFVSYVCKVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPVFTFTAGNALKAIIAMDTAGMILGWKFFDHAAHLGGALFGIWYITYGHELIWKNREPLVKIWHEIRTNGPKKGGGSK | Function: Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptotic signals. Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP). Promotes cleavage of serine/threonine-protein phosphatase PGAM5 in damaged mitochondria in response to loss of mitochondrial membrane potential. Mediates differential cleavage of PINK1 and PGAM5 depending on the health status of mitochondria, disassociating from PINK1 and associating with PGAM5 in response to mitochondrial membrane potential loss. Required for processing of CLPB into a form with higher protein disaggregase activity by removing an autoinhibitory N-terminal peptide. Promotes processing of DIABLO/SMAC in the mitochondrion which is required for DIABLO apoptotic activity. Also required for cleavage of STARD7 and TTC19. Promotes changes in mitochondria morphology regulated by phosphorylation of P-beta domain.
PTM: P-beta is proteolytically processed (beta-cleavage) in a PARL-dependent manner.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
Sequence Mass (Da): 42126
Sequence Length: 377
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.21.105
|
Q6UWI2 | MVYKTLFALCILTAGWRVQSLPTSAPLSVSLPTNIVPPTTIWTSSPQNTDADTASPSNGTHNNSVLPVTASAPTSLLPKNISIESREEEITSPGSNWEGTNTDPSPSGFSSTSGGVHLTTTLEEHSSGTPEAGVAATLSQSAAEPPTLISPQAPASSPSSLSTSPPEVFSASVTTNHSSTVTSTQPTGAPTAPESPTEESSSDHTPTSHATAEPVPQEKTPPTTVSGKVMCELIDMETTTTFPRVIMQEVEHALSSGSIAAITVTVIAVVLLVFGVAAYLKIRHSSYGRLLDDHDYGSWGNYNNPLYDDS | Function: May regulate TLP1 expression and telomerase activity, thus enabling certain prostatic cells to resist apoptosis.
PTM: Highly N-glycosylated and O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 32289
Sequence Length: 310
Subcellular Location: Cell membrane
|
Q6P9X9 | MVCKALITLCIFAAGLRVQGSPTPTLLPVSLTTKSTAPMATWTTSAQHTAMATTPVASATHNASVLRTTAASLTSQLPTHPREEAVTSPPLKREVNSTDSSPTGFSSNSSGIHLAPTPEEHSLGSPETSVPATGSQSPTLLFSQGPTSASTSPATSPSEPLSASVTSNHSSTVNNIQPTGAPMAPASPTEEHSSSHTPTSHVTEPVPKEKSPQDTEPGKVICESETTTPFLIMQEVENALSSGSIAAITVTVIAVVLLVFGAAAYLKIRHSSYGRLLDDHDYGSWGNYNNPLYDDS | Function: May regulate TLP1 expression and telomerase activity, thus enabling certain prostatic cells to resist apoptosis.
PTM: Highly N-glycosylated and O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 30729
Sequence Length: 296
Subcellular Location: Cell membrane
|
Q8W4C3 | MQRRFLSSISATAGNTKTLNQGRWSVKQVKKSNFHVTLDEIRTSIDSSDFIALSLQNTGSYAAAWHRVSAIDTPQTSYLKAKYAAERYQILQFALCPFSLQGSKLTVHPYNFHLFPRDELKCGMPSYSFSCQASRLTAMAREGFDFNICIYEGISYLSRAQESASKFLSENPILADSVTVSSSPATVADTVFVGRIRSRVKNWRQSCIDSGSKTGDDDLVSSLRRLVLGSEQYGSRLCLTIDVCSERQVQLILEMLTEFSDDVVPLLVASKSRGTQAVRTVFMSSKEDKDLFKRELKDLEKEENRRVRGFREVVDFISSSQKPVVSQNYLSDFTSIHAKFLGPLPSNVDDFSSSLSSAFPNVVDLSQFMKEISPLSNISNLPAAMSSLNRFFAPVDVEVANQGCPVKLDEGHQSHGQNAVMISQLFAKLCTIQKSDLSTIQSNEDFQALASDEHANSVTSCSKNAGDENVKVWSKNSRRVSSENLVFIWGLGKKMTAAKLKNVLQKSHPVFAREFDVKYIDRSSAILVFWESGPSETFLSAVNNEEQLDGSLREMVAEGLRGAGYETYKRACRLGFWEADLAESLDKALESSDTDPDSDTKPSEIDWSNELAINFDEL | Function: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 68807
Sequence Length: 618
Subcellular Location: Nucleus
EC: 3.1.13.4
|
Q9LG26 | MRRHKRWPLRSLVCSFSSSAAETVTTSTAASATAAFPLKHVTRSNFETTLNDLRSLVKAADFVAIDLEMTGVTSAPWRDSLEFDRYDVRYLKVKDSAEKFAVVQFGVCPFRWDSRTQSFVSYPHNFFVFPRQELTFDPPAHEFLCQTTSMDFLAKYQFDFNTCIHEGISYLSRREEEEASKRLKMLHGEDGIDSSGETEELKLVRLADVLFAARMEKLLNEWRSGLLHGGNASSEFPRISNGSNQSMETVFHHMRPALSLKGFTSHQLRVLNSVLRKHFGDLVYIHSNDKSSSSRDIVVYTDSDSDKENLMKEAKDERKRLAERKIQSAIGFRQVIDLLASEKKLIVGHNCFLDIAHVYSKFVGPLPSTAEKFVASINSHFPYIVDTKILLNVNPMLHQRMKKSSTSLSSAFSSLCPQIEFSSRSSDSFLQQRVNIDVEIDNVRCSNWNAGGKHEAGYDAFMTGCIFAQACNHLGFDFKQHSQLDDFAQNEKLEKYINRLYLSWTRGDIIDLRTGHSNADNWRVSKFKYENIVLIWNFPRKLKARGIKECICKAFGSASVTSVYHVDDSAVFVLFKNSELVWDFLALKRQLESSDGPVSVLHPLSKILEGGNTGAADYEAYKEICSSHVSEVMFSDQAETVGVKSRTRPNAQCETETREENTVTVTHKASDLIDAFLANRVEVETATSN | Function: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs. Essential for early development, possibly by participating in silencing certain maternal mRNAs translationally. May have a pivotal role in stress response.
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 78010
Sequence Length: 689
Subcellular Location: Nucleus
EC: 3.1.13.4
|
Q7ZU92 | MEVTRQNFKEVLPEVCNAVQEADFISIDGEFTGISDGPSVSALTNGLDTPEERYTKLRKHSMNFLLFQFGVCTFRYDQNQSTYITKAFNFYIFPKPFSRTSPDIKFICQSSSIDFLASQGFDFNKVFRSGIPYLNQEEECQLREQYEERRGQMNGAGPVSYTPPSGTGVCNVPEDQREFIRSVEEKVEALLKNTDQTLDLEPCTGFQRKLIYQTLNSKYSKGLHVEALETEKKERFIQISKVDDEERRRREQQKQQREQEELNDAVGFSRVIRAISKSGKLVVGHNMLLDVMHTIHQFCGPLPEELDDFKEVAMTVFPRLLDTKLMASTQPFKEIIHNTSLAELHKQLRQKPFRPPTTECPEGLQSYDTSTEQLHEAGYDAFITGLCFISMANYLGSFLTPPKSHISARSKLLEPFYNKLFLMRVIDIPYLNMSGPDLQPKRDHVLYVTFPKEWKTSDLYQLFSAFGNIQVSWVDDTSAFVSLSQTEQVQIAMNTSRYAESYRIQTYAEYLQSRQKNTHSSRKWASDGWADTSYPSVAMTTASGYSHTDNWHQAVKRSISPSLDEQNHGADSSWTNYSVKKIKTEGSCTQTYADVAGSCDWPRLQADEGGASVSPVAEEAELDEFSANQSQGKRSRKHKKRKSDASETTPPALFDVPQVW | Function: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 75261
Sequence Length: 660
Subcellular Location: Cytoplasm
EC: 3.1.13.4
|
O95453 | MEIIRSNFKSNLHKVYQAIEEADFFAIDGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGALSYVSPNTSKCPVTIPEDQKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFYCPLPADLSEFKEMTTCVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSFLSPPKIHVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTYAEYMGRKQEEKQIKRKWTEDSWKEADSKRLNPQCIPYTLQNHYYRNNSFTAPSTVGKRNLSPSQEEAGLEDGVSGEISDTELEQTDSCAEPLSEGRKKAKKLKRMKKELSPAGSISKNSPATLFEVPDTW | Cofactor: Divalent metal cations. Mg(2+) is the most probable.
Function: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization . Also able to recognize and trim poly(A) tails of microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar RNAs) leading to microRNAs degradation or snoRNA increased stability .
PTM: Phosphorylation by MAPKAPK2, preventing GADD45A mRNA degradation after genotoxic stress.
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 73451
Sequence Length: 639
Subcellular Location: Nucleus
EC: 3.1.13.4
|
P21861 | MPGTAEVQVRPGVEEDLKPLTDLYNHYVRETPITFDTEPFTPEERRPWLLSHPEDGPYRLRVATDAESQEILGYATSSPYRAKPAYATSVETTVYVAPGAGGRGIGSLLYASLFDALAAEDLHRAYAGIAQPNEASARLHARFGFRHVGTYREVGRKFGRYWDVAWYERPL | Function: Inactivates phosphinothricin (PPT) by transfer of an acetyl group from acetyl CoA. The physiological substrate could be a structurally related compound.
Catalytic Activity: acetyl-CoA + phosphinothricin = CoA + H(+) + N-acetylphosphinothricin
Sequence Mass (Da): 19205
Sequence Length: 171
EC: 2.3.1.183
|
P16426 | MSPERRPADIRRATEADMPAVCTIVNHYIETSTVNFRTEPQEPQEWTDDLVRLRERYPWLVAEVDGEVAGIAYAGPWKARNAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHDVGFWQLDFSLPVPPRPVLPVTEI | Function: Inactivates phosphinothricin (PPT) by transfer of an acetyl group from acetyl CoA. Can also acetylate demethylphosphinothricin but not PTT or glutamate. This enzyme is an effector of phosphinothricin tripeptide (PTT or bialaphos) resistance.
Catalytic Activity: acetyl-CoA + phosphinothricin = CoA + H(+) + N-acetylphosphinothricin
Sequence Mass (Da): 20637
Sequence Length: 183
EC: 2.3.1.183
|
Q57146 | MSPERRPVEIRPATAADMAAVCDIVNHYIETSTVNFRTEPQTPQEWIDDLERLQDRYPWLVAEVEGVVAGIAYAGPWKARNAYDWTVESTVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLRAAGYKHGGWHDVGFWQRDFELPAPPRPVRPVTQI | Function: Inactivates phosphinothricin (PPT) by transfer of an acetyl group from acetyl CoA. This enzyme is an effector of phosphinothricin tripeptide (PTT or bialaphos) resistance.
Catalytic Activity: acetyl-CoA + phosphinothricin = CoA + H(+) + N-acetylphosphinothricin
Sequence Mass (Da): 20618
Sequence Length: 183
EC: 2.3.1.183
|
A0A1U8QHE3 | MTCADVTDLCTQASQLVQQLRTKDGELGFMSAAVYDTAWVSMVQKTTPEGRQWLLPKCFEYILRTQLEDGSWETYASDVDGILNTAASLLALETHAESRIASTDPPVEEMKERIGRARAALSRQLQAWSVKDTVHVGFEIILPALLRLLREKGHEFEFDGRAELDRLNRIKLSKFRPEYLYSARTTALHSLEAFVGMIDFDKVAHQKVNGSFMFSPSSTAAFLMFSSSWDDECEQYLRLVLQNGAGGGTGGMPSAYPSKYFEVSWVRGQLARLESKLTELQALTTLLDNGYSTGDLGIEDTDSLGEMLRDALVKGGGIVGFAPSIQADADDTAKSLIAVSLLDKPVSAQGLIDAFEGPMHFRTYHGERDPSFTANSNVLLALLNTPDAATVSPQIEKAAAFLCDVWWTADSEIGDKWNLSPYYPSMLMAEAFGKLLQVWSDGGLKSISSQFIRDRVSVCLYQALVRTLQTQNENGSWGSHSHEETAYAILTIAHACQLPVVNQLWTNVQLAVSRGRKFLQNSAGDKAEYLWVEKVTYSSILLSKSYVLAALKVSFERSYPACLANLFIVSKKRVIEFARFHSMLPLFSSMELWKVRAAIVEGYLLLPQLRDRRLAVFSRTGMEEDKYFEYIPFTWTLCNNRRNTFLSTKTLVEMMVISFLNYQADEFMEAVVGRLNSSQRSMTRSCIDEIFRDLKDKPELNDAIQAQSGPRNADANGHRILPQAKRIKMGSQLPSDVSRVLSAFVHHVMDHPSVKAAAPLEYERVKNELQVFLLSHIEQADDNGRFAAQLESTRDDFETARSSFYRWVSSTSSDHTSCPYSFAFYQCLLGFEQASHNAACFQTCEEKYVAEAMCRHLAVMCRMYNDYGSLARDRDEKNLNCVNFPEFAQAGPKSDAVRQKQLFSLAEFERSNMKRGLEVLTEMAAQDRAKMRMLEKVQMFCDVTDVYGQIYALEILRVGCDLAHDCFMLELPAQWSNST | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes . Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene . The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
Sequence Mass (Da): 110118
Sequence Length: 979
Domain: The VYDTAW motif is widely conserved among diterpene cyclases in plants and fungi.
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 4.2.3.-
|
A0A1U8QLG8 | MSPPLDSALEPLSEYKETAFPRTEKDPSQYKEHDLVTPEKEIQTGYFSPRGSHSSHGSHDSSASSNISLDDARMSDVNNSPNVFHDDPDTIDEKLSMYWKAANETVIREPYDYIAGIPGKEIRRKLLEAFNHWYKVDEQSCQAIATTVGMAHNASLLIDDIQDSSKLRRGVPCAHEVFGIAQTINSANYVYFLAQNQLFRLRSWPQAISVFNEEMVNLHRGQGMELFWRDNLLPPSMDDYLQMIANKTGGLFRMIVRLLQTSSRQVIDVEQLVDVLGLYFQILDDYKNIREEKMAAQKGFFEDLTEGKFSFPICHAIGEGAKNRTALLHMLRLKTDDMKIKQEAVCILDNAGSLDYTREVLYGLDRKARSLLREFKTPNPFMEALLDAMLSSLQACH | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes . Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene . The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
Catalytic Activity: dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate
Sequence Mass (Da): 45185
Sequence Length: 397
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 2.5.1.-
|
C8VN86 | MPESQIIELGTLGQIPLYSLERALQDPLRAVKLRRQIVSQHQATGNIDFTTDGSALPYEGYDYKAVLGACCENVIGYMPIPVGVAGPIKINGKMVFLPMSTTEGALVASTNRGCMAINAGGGVTALVLGDGMTRAPIVRFPSLEEAGAAKQWLGSDAGFLIIEDAFNASSRFARLQNIKATAVGSDLYIRFTASTGDAMGMNMISKGVEQALEAMQKHGFESMDVVSLSGNFCADKKPAAVNWIEGRGKTVTAQATIPEHAVRETLKTSVEALVELNVSKNLVGSAVAGALGGFNAHAANVVTAIYLATGQDPAQNVQSSNTLTVMKNVNGDLQISVFMPSIEVGTVGGGTVLGPQKAMLHMMGVQGADPEQPGRNAQELALLVAAGVLAGELSLCSALSAGSLVKSHLTHNRKKG | Function: 3-hydroxy-3-methylglutaryl coenzyme A reductase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes . Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene . The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
Catalytic Activity: (R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 43383
Sequence Length: 416
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
Subcellular Location: Membrane
EC: 1.1.1.34
|
A0A1U8QXK4 | MNTLNAPRNPTRHPAMTADTLVDAPALPHQNGSTEEKLKERGSFGKLYTYKRSPRALGIQAVAKSIGLELEQVELQPANGVPDFYWNLNPLGKTPTFVGADGLVLTECMAIALHVTNEDSTTTLLGSSSLDFVQIIRWISFTNTDVVTRMASWVRPLIGYTPYSKEEVLKAQQQTTQAIGVFEDSLRDRKYLVGDRLTLADIMCVSLVSFGFAQIFDKEWREAFPYFSGWYMMVMHLPIMKAVVEEVPFVEEGLPNAPPTEPFRAP | Function: Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes . Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene . The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
Sequence Mass (Da): 29717
Sequence Length: 266
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 2.5.1.-
|
A0A1U8QP15 | MVSLKTVQASNAGLRALPNITALFVGGTSGIGQSTLRQLARYADSPTAYIIGRNEARTRPFLSELQQLNPKGRFHFIEADVSLVRNVDAACQQILQQQKKLNFLFMTPGGISLGGRNETVEGIDYLFALRYYSRMRFIQNLLPLLEASSPSRVISVYGGGFEYSINTADLDLKHNFSLLNAYKHSITMTSLSMEHLARTHPAVSFIHVYPGLVGTNIYTNSFPAPVSTFYNYLVWPFMKPFSVDLGESGERHLFHLSSAHYPAKQGIVPQGVPLEAGEVAKGITGEPGSGAYLLNWKGDVRPSTKILAQYREQKIPQLVWDHTESLMDQAVHR | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes . Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene . The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
Sequence Mass (Da): 36962
Sequence Length: 333
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.-.-.-
|
A0A1U8QJR1 | MVDATSPPGVNAVVNYYVPNSDGSPPATNDMAVMLGQKDMISHKMRIRDLRPYKEEYSLDRNGFQYATIHSTLTDATDETQIKEVYYREIEKLVQDITGAKRVLAFHHAVRTRTGNEFGEQIKDRYQGVEGPAYRVHIDQTPQGALSIVQFMFPDLADDVRNGSFQVINVWRPLTRVQRDPLMVADAAEMPPEDLLLISRKYYNGLHSSNFVIKYDGRMAAGEGPTDGLSGDGKHSWWYIGDQEPTEALVFSSSGFRNGKAIIGTAHDLYSAEPMINAYERKNASSLYGHDESQI | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes . Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene . The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
Sequence Mass (Da): 33101
Sequence Length: 295
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.-.-.-
|
C8VN91 | MDNYTWHSGTLIPSDSPSSIDRSQLYLEILGVLSVVYLLQTLVAYSKSFKAPFVGFRFWYEPKWLVGLRFSQGALAQVNEGYAKYKNAMFKVARNDSDILVIPNKYVEELRSLPDEKISAIRAHIKNLLGKYSTTLILLESDLHTRMLQTKLTPNLGSFIEVIESELLFAMDQEIPANLDDWQSVNVFHIVLRIVARISARVFLGVPACRNEEWLQTSIHYTENVFATVMLLRRFPKWMHPIVGHLLPSYWAIHRNLRTAKRIISPMVRQRRAEEAKRNPDYVKPNDLLQWMMDGANENDGQPDKLAHRQLLLSLASIHTTTMAAAHCFYDLCQHPEYFEPLREEINDVIAQDGGWKKTTLNKMRKLDSFLKESQRINPPSLLAFNRIVSEDLTLSDGTLLPKGTHFSMPSAAILQDNGVEPGADQFDGFRYYKKRLNPEEANKHQFAMTDNNNLHFGHGKYSCPGRFFASNEIKIIMAHLLTDYEFKYPRGATRPRNLTADENLYPDPSARLLMRRRVVAPPQASITPQLVSA | Function: Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes . Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene . The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61207
Sequence Length: 534
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
|
Q9FE20 | MGCFSCFDSSDDEKLNPVDESNHGQKKQSQPTVSNNISGLPSGGEKLSSKTNGGSKRELLLPRDGLGQIAAHTFAFRELAAATMNFHPDTFLGEGGFGRVYKGRLDSTGQVVAVKQLDRNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEFMPLGSLEDHLHDLPPDKEALDWNMRMKIAAGAAKGLEFLHDKANPPVIYRDFKSSNILLDEGFHPKLSDFGLAKLGPTGDKSHVSTRVMGTYGYCAPEYAMTGQLTVKSDVYSFGVVFLELITGRKAIDSEMPHGEQNLVAWARPLFNDRRKFIKLADPRLKGRFPTRALYQALAVASMCIQEQAATRPLIADVVTALSYLANQAYDPSKDDSRRNRDERGARLITRNDDGGGSGSKFDLEGSEKEDSPRETARILNRDINRERAVAEAKMWGESLREKRRQSEQGTSESNSTG | Function: Protein kinase required for plant defense mechanism mediated by the disease resistance (R) protein RPS5. In case of infection by Pseudomonas syringae, AvrPphB triggers RPS5-mediated defense mechanism via the cleavage of PBS1. Both kinase activity and cleavage by avrPphB are independently required to trigger the RPS5-mediated resistance. Contributes to PAMP-triggered immunity (PTI) signaling and defense responses downstream of FLS2.
PTM: Cleaved by avrPphB in infected plant cells. Its cleavage serves as a signal that triggers the RPS5-mediated defense system.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 50384
Sequence Length: 456
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
P08018 | MEDKFANLSLHEKTGKSSIQLNEQTGSDNGSAVKRTSSTSSHYNNINADLHARVKAFQEQRALKRSASVGSNQSEQDKGSSQSPKHIQQIVNKPLPPLPVAGSSKVSQRMSSQVVQASSKSTLKNVLDNQETQNITDVNINIDTTKITATTIGVNTGLPATDITPSVSNTASATHKAQLLNPNRRAPRRPLSTQHPTRPNVAPHKAPAIINTPKQSLSARRGLKLPPGGMSLKMPTKTAQQPQQFAPSPSNKKHIETLSNSKVVEGKRSNPGSLINGVQSTSTSSSTEGPHDTVGTTPRTGNSNNSSNSGSSGGGGLFANFSKYVDIKSGSLNFAGKLSLSSKGIDFSNGSSSRITLDELEFLDELGHGNYGNVSKVLHKPTNVIMATKEVRLELDEAKFRQILMELEVLHKCNSPYIVDFYGAFFIEGAVYMCMEYMDGGSLDKIYDESSEIGGIDEPQLAFIANAVIHGLKELKEQHNIIHRDVKPTNILCSANQGTVKLCDFGVSGNLVASLAKTNIGCQSYMAPERIKSLNPDRATYTVQSDIWSLGLSILEMALGRYPYPPETYDNIFSQLSAIVDGPPPRLPSDKFSSDAQDFVSLCLQKIPERRPTYAALTEHPWLVKYRNQDVHMSEYITERLERRNKILRERGENGLSKNVPALHMGGL | Function: Kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Seems to phosphorylate HOG1 on a tyrosine residue.
PTM: Activated by phosphorylation by SSK2 or SSK22. Ser/Thr phosphorylation is also necessary for SHO1-mediated activation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 72720
Sequence Length: 668
Domain: Alternative way of activation involves binding the proline-rich motif to the SH3 domain of SHO1.
Subcellular Location: Cytoplasm
EC: 2.7.12.2
|
Q9XUV0 | MWGETFDDFENDEGEMAMAKQNLIAEPARADFTFAKLPLGIQPVDFMKTHFAETAGKSMQFRKGTTTLAFVYEPATPADKGGIIVAVDSRASSGEYISSKSVMKILDIGDRMVATMAGGAADCQFWTRIVAKYCTLYELREKTSITVSAASKYFANTLYGYRGQGLSVGSMVAGYDKKGPQIFKVDSEGDRCQLKVCSVGSGSLNAYGILDNHYKPKMTDDEARKLGLRAIMHATYRDSGSGGVCNLCHITPTEKIRLPPMDVSKLWYEFADELGRDITYNPVE | Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins . This complex plays numerous essential roles within the cell by associating with different regulatory particles (By similarity). Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins (By similarity). The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required (By similarity).
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 31230
Sequence Length: 284
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
Q08017 | MSASRFMLRPLTRALLMHGATRTRLAGTGLGLALTLTAAPYVQAQEWTLNIPSQPLAQALQTLGQQTSLQIIYSPESLQGLRSTALNGRYQDDESLKAMLNGTGIRYQRDGNTVTVLGPATGSAMELAPTNVNASRLGATTEGSNSYTTGGVTIGKGVHSLKETPQSVTVMTRKMLDDQNLNTIEQVMEKTPGITVYDSPMGGKYFYSRGFRMSGQYQYDGVPLDIGSSYVQADSFNSDMAIYDRVEVLRGAAGMMKGAGGTAGGVNFVRKRGQDTAHTQLSLSAGTWDNYRGQVDTGGPLNDSGTIRGRAVVTEQTRQYFYDVGSRKDQIYYGALDFDLSPDTTLGLGFAWEDVDATPCWGGLPRYADGSDLHLKRSTCLNTAWNNQRSKRATYFADLKHQFNDDWSLKVAGVYSRNTQDMEYAFPSGAVPVGATATNTLMLGSIYDYDQRDYGFDAYVDGKFDAFGQQHELTIGANASRSHKDDFYAVAALPQRQNVLDPNHHIPQPDESYYLANASRGGPVDMHIKQYGAYSIARLKLADPLTLVLGSRVSWYKSDTDSVQYFRGEGTQVDTKSTETGQVTPFAGVLFDLNDNLTAYASYTDIFTPQGAYKTIDGSTLKPLVGQSYELGIKGEWFDGRLNSTFNLFRTLQKDAAQDDPRCEDSSCSINSGKVRAQGFEAEVSGEVIDRLQLLAGYTYTQTKVLEDADATQDGVVYNSYVPRHLLRVWGDYSLSGPLDRVTIGAGVNAQTGNYRTSPIGGDNIDGAGYAVWNGRIGYRIDDTWSVALNGNNLFDKRYYSTIGTEGFGNFYGDPRNFVMSVKADF | Function: Specific receptor for the siderophore ferric pyoverdine (pseudobactin) M114.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90388
Sequence Length: 826
Subcellular Location: Cell outer membrane
|
Q797E3 | MNFKVFLLAASTIAVGLVELIVGGILPQIANDLDISIVSAGQLISVFALGYAVSGPLLLALTAKIERKRLYLIALFVFFLSNLVAYFSPNFATLMVSRVLAAMSTGLIVVLSLTIAPKIVAPEYRARAIGIIFMGFSSAIALGVPLGILISDSFGWRILFLGIGLLALISMLIISIFFERIPAEKMIPFREQLKTIGNLKIASSHLVTMFTLAGHYTLYAYFAPFLEETLHLSSFWVSICYFLFGISAVCGGPFGGALSDRLGSFKSILLVTGSFAIIMFLLPLSTSSMIFFLPVMVIWGLLSWSLAPAQQSYLIEIAPDSSDIQQSFNTSALQVGIALGSAIGGVVLDQTGTVVSTAWCGGSIVIIAVLFAFISLTRPVQTAKKSSL | Function: Involved in the efflux of purine ribonucleosides, such as guanosine, adenosine and inosine, as well as purine bases guanine, adenine and hypoxanthine, and purine base analogs 2,6-diaminopurine, 6-mercaptopurine and 2-fluoroadenine. Therefore plays a role in maintaining the cellular purine base pools and protecting cells against toxic purine base analogs. Modulates expression of the purR and G-box regulons.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41535
Sequence Length: 388
Subcellular Location: Cell membrane
|
O34987 | MKTFFQFDELGTSYRNEIIGGLTTFLSMAYILFVNPITLALESVKDFPEALRIDQGAVFTATALASAAGCILMGLIARYPIAIAPGMGLNAFFAFSVVLGMGISWQAALSGVFISGLIFVALSLTGFREKIINAIPPELKLAVGAGIGLFITFVGLQGSGIITANPSTLVTIGNIHSGPVLLTIFGVIVTVILMVLRVNAGVFIGMLLTAVAGMIFGLVPVPTQIIGSVPSLAPTFGQAWIHLPDIFSVQMLIVILTFLFVGFFDTAGTLVAVATQAGLMKENKLPRAGRALLADSSSIVIGAVLGTSTTTSYVESSSGVAAGARSGFAAIVTGILFLLATFFSPLLSVVTSNVTAPALIIVGALMVAPLGKIAWDKFEVAVPAFLTMIMMPLTYSIATGIAIGFIFYPITMVCKGKAKEVHPIMYGLFVVFILYFIFLK | Function: Involved in the uptake of the purine bases hypoxanthine and guanine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46191
Sequence Length: 440
Subcellular Location: Cell membrane
|
O34978 | MFHLKEQQTSIKQEIIAGLTTFFTMVYIVVVNPVILANAGVPFDQVFTATIIASIVGTLWMALAANYPIAIAPGMGLNAYLAFHVVSASDGGITYATAFSAVFTAGVLFIILSLTPLRKQLIEAIPNNLKYGITTGIGLFIAFIGLRQAGIVAADESNLVTLGNLHSPGVILTLVGLLISVVLMVLNVSGALFIGMAATALIAFFTGQLHFSKGFMSLPHLPEGLMISNPFTAFGDVIHHGLYAVVFSFLLVTIFDTTGTMIGVAEQAGLMKNNKLPNVRKALLADSTATTVGAVFGTSPTTAFIESSAGVAAGGRTGLTALTVAVMFAASMFFSPLVSALSGIAAITSPALIIVGSLMMGSVSNMNWKEMDEAFPAFLVILAMPLTSSISTGIALGFISYPIVKAARGKWREIHPLVIVFAILFFIQLFIL | Function: Involved in the uptake of the purine bases hypoxanthine and guanine. May work at purine concentrations higher than 100 uM.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45420
Sequence Length: 432
Subcellular Location: Cell membrane
|
P42086 | MRNGFGKTLSLGIQHVLAMYAGAIVVPLIVGKAMGLTVEQLTYLVSIDIFMCGVATLLQVWSNRFFGIGLPVVLGCTFTAVSPMIAIGSEYGVSTVYGSIIASGILVILISFFFGKLVSFFPPVVTGSVVTIIGITLMPVAMNNMAGGEGSADFGDLSNLALAFTVLSIIVLLYRFTKGFIKSVSILIGILIGTFIAYFMGKVQFDNVSDAAVVQMIQPFYFGAPSFHAAPIITMSIVAIVSLVESTGVYFALGDLTNRRLTEIDLSKGYRAEGLAVLLGGIFNAFPYTAFSQNVGLVQLTGIKKNAVIVVTGVILMAFGLFPKIAAFTTIIPSAVLGGAMVAMFGMVIAYGIKMLSRIDFAKQENLLIVACSVGLGLGVTVVPDIFKQLPSALTLLTTNGIVAGSFTAVVLNIVYNVFSKAKKIEQEADLAEQKTAV | Function: Transport of xanthine in the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46238
Sequence Length: 438
Subcellular Location: Cell membrane
|
P40424 | MDEQPRLMHSHAGVGMAGHPGLSQHLQDGAGGTEGEGGRKQDIGDILQQIMTITDQSLDEAQARKHALNCHRMKPALFNVLCEIKEKTVLSIRGAQEEEPTDPQLMRLDNMLLAEGVAGPEKGGGSAAAAAAAAASGGAGSDNSVEHSDYRAKLSQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVSIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFNKQATEILNEYFYSHLSNPYPSEEAKEELAKKCGITVSQVSNWFGNKRIRYKKNIGKFQEEANIYAAKTAVTATNVSAHGSQANSPSTPNSAGSSSSFNMSNSGDLFMSVQSLNGDSYQGAQVGANVQSQVDTLRHVISQTGGYSDGLAASQMYSPQGISANGGWQDATTPSSVTSPTEGPGSVHSDTSN | Function: Transcription factor which binds the DNA sequence 5'-TGATTGAT-3' as part of a heterodimer with HOX proteins such as HOXA1, HOXA5, HOXB7 and HOXB8 . Binds to the DNA sequence 5'-TGATTGAC-3' in complex with a nuclear factor which is not a class I HOX protein . Has also been shown to bind the DNA sequence 5'-ATCAATCAA-3' cooperatively with HOXA5, HOXB7, HOXB8, HOXC8 and HOXD4 . Acts as a transcriptional activator of PF4 in complex with MEIS1 . Also activates transcription of SOX3 in complex with MEIS1 by binding to the 5'-TGATTGAC-3' consensus sequence (By similarity). In natural killer cells, binds to the NFIL3 promoter and acts as a transcriptional activator of NFIL3, promoting natural killer cell development (By similarity). Plays a role in the cAMP-dependent regulation of CYP17A1 gene expression via its cAMP-regulatory sequence (CRS1) (By similarity). Probably in complex with MEIS2, involved in transcriptional regulation by KLF4 . Acts as a transcriptional activator of NKX2-5 and a transcriptional repressor of CDKN2B (By similarity). Together with NKX2-5, required for spleen development through a mechanism that involves CDKN2B repression (By similarity).
Sequence Mass (Da): 46626
Sequence Length: 430
Domain: The homeobox is required for PBX1 nuclear localization and for transcriptional activation of NFIL3.
Subcellular Location: Nucleus
|
O60330 | MIPARLHRDYKGLVLLGILLGTLWETGCTQIRYSVPEELEKGSRVGDISRDLGLEPRELAERGVRIIPRGRTQLFALNPRSGSLVTAGRIDREELCMGAIKCQLNLDILMEDKVKIYGVEVEVRDINDNAPYFRESELEIKISENAATEMRFPLPHAWDPDIGKNSLQSYELSPNTHFSLIVQNGADGSKYPELVLKRALDREEKAAHHLVLTASDGGDPVRTGTARIRVMVLDANDNAPAFAQPEYRASVPENLALGTQLLVVNATDPDEGVNAEVRYSFRYVDDKAAQVFKLDCNSGTISTIGELDHEESGFYQMEVQAMDNAGYSARAKVLITVLDVNDNAPEVVLTSLASSVPENSPRGTLIALLNVNDQDSEENGQVICFIQGNLPFKLEKSYGNYYSLVTDIVLDREQVPSYNITVTATDRGTPPLSTETHISLNVADTNDNPPVFPQASYSAYIPENNPRGVSLVSVTAHDPDCEENAQITYSLAENTIQGASLSSYVSINSDTGVLYALSSFDYEQFRDLQVKVMARDNGHPPLSSNVSLSLFVLDQNDNAPEILYPALPTDGSTGVELAPRSAEPGYLVTKVVAVDRDSGQNAWLSYRLLKASEPGLFSVGLHTGEVRTARALLDRDALKQSLVVAVQDHGQPPLSATVTLTVAVADSIPQVLADLGSLESPANSETSDLTLYLVVAVAAVSCVFLAFVILLLALRLRRWHKSRLLQASGGGLTGAPASHFVGVDGVQAFLQTYSHEVSLTTDSRKSHLIFPQPNYADMLVSQESFEKSEPLLLSGDSVFSKDSHGLIEQAPPNTDWRFSQAQRPGTSGSQNGDDTGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 100955
Sequence Length: 932
Subcellular Location: Cell membrane
|
Q9Y5G2 | MKASSGRCGLVRWLQVLLPFLLSLFPGALPVQIRYSIPEELAKNSVVGNLAKDLGLSVRDLPARKLRVSAEKEYFTVNPESGDLLVSDRIDREQICGKQPLCVLDFDTVAENPLNIFYIAVIVQDINDNTPLFKQTKINLKIGESTKPGTTFPLDPALDSDVGPNSLQRYHLNDNEYFDLAEKQTPDGRKYPELILKHSLDREEHSLHQLVLTAVDGGDPPQSGTTQIRIKVTDANDNPPVFSQDVYRVTLREDVPPGFFVLQVTATDRDEGINAEITYSFHNVDEQVKHFFNLNEKTGEITTKDDLDFEIASSYTLSIEAKDPGDLAAHCSIQVEILDDNDCAPEVIVTSVSTPLPEDSPPGTVIALIKTRDRDSGENGEVYCQVLGNAKFILKSSSKNYYKLVTDGALDREEIPEYNLTITATDGGKPPLSSSIIVTLHISDVNDNAPVFQQTSYMVHVAENNPPGASIAQISASDPDLGPSGQVSYSIVASDLKPREILSYVSVSAQSGVVFAQRAFDHEQLRAFELTLQARDQGSPALSANVSLRVLVGDLNDNAPRVLYPALGPDGSALFDMVPRAAEPGYLVTKVVAVDADSGHNAWLSYHVLQASEPGLFSLGLRTGEVRTARALGDRDAARQRLLVAVRDGGQPPLSATATLHLIFADSLQEVLPDLSDRREPSDPQAKLQFYLVVALALISVLFFLAVILAISLRLRLSSRSDAWDCFQPGLSSKPGPGVLPNYSEGTLPYSYNLCVASQSAKTEFNFLNITPELVPAQDLVCDNASWEQNTNHGAAGVPFASDTILKQAPPNTDWRFSQAQRPGTSGSQNGDDTGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 100875
Sequence Length: 931
Subcellular Location: Cell membrane
|
Q9UN71 | MGSGAGELGRAERLPVLFLFLLSLFCPALCEQIRYRIPEEMPKGSVVGNLATDLGFSVQELPTRKLRVSSEKPYFTVSAESGELLVSSRLDREEICGKKPACALEFEAVAENPLNFYHVNVEIEDINDHTPKFTQNSFELQISESAQPGTRFILGSAHDADIGSNTLQNYQLSPSDHFSLINKEKSDGSKYPEMVLKTPLDREKQKSYHLTLTALDFGAPPLSSTAQIHVLVTDANDNAPVFSQDVYRVSLSENVYPGTTVLQVTATDQDEGVNAEITFSFSEASQITQFDLNSNTGEITVLNTLDFEEVKEYSIVLEARDGGGMIAQCTVEVEVIDENDNAPEVIFQSLPNLIMEDAELGTHIALLKVRDKDSRHNGEVTCKLEGDVPFKILTSSRNTYKLVTDAVLDREQNPEYNITVTATDRGKPPLSSSSSITLHIGDVNDNAPVFSQSSYIVHVAENNPPGASISQVRASDPDLGPNGQVSYCIMASDLEQRELSSYVSISAESGVVFAQRAFDHEQLRAFELTLQARDQGSPALSANVSLRVLVDDRNDNAPRVLYPALGPDGSALFDMVPHAAEPGYLVTKVVAVDADSGHNAWLSYHVLQASEPGLFSLGLRTGEVRTARALGDRDAVRQRLLVAVRDGGQPPLSATATLHLVFADSLQEVLPDITDRPDPSDLQAELQFYLVVALALISVLFLVAMILAIALRLRRSSSPASWSCFQPGLCVKSESVVPPNYSEGTLPYSYNLCVAHTGKTEFNFLKCSEQLSSGQDILCGDSSGALFPLCNSSELTSHQQAPPNTDWRFSQAQRPGTSGSQNGDDTGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 99927
Sequence Length: 923
Subcellular Location: Cell membrane
|
Q9Y5G0 | MGSGAGELGRAERLPVLFLFLLSLFCPALCEQIRYRIPEEMPKGSVVGNLATDLGFSVQELPTRKLRVSSEKPYFTVSAESGELLVSSRLDREEICGKKPACALEFEAVAENPLNFYHVNVEIEDINDHTPKFTQNSFELQISESAQPGTRFILEVAEDADIGLNSLQKYKLSLNPSFSLIIKEKQDGSKYPELALEKTLDREQQSYHRLVLTALDGGHPPLSGTTELRIQVTDANDNPPVFNRDVYRVSLRENVPPGTTVLQVSATDQDEGINSEITYSFYRTGQIFSLNSKSGEITTQKKLDFEETKEYSMVVEGRDGGGLVAQCTVEINIQDENDNSPEVTFHSLLEMILENAVPGTLIALIKIHDQDSGENGEVNCQLQGEVPFKIISSSKNSYKLVTDGTLDREQTPEYNVTITATDRGKPPLSSSISVILHIRDVNDNAPVFHQASYLVSVPENNPPGASIAQVCASDLDLGLNGQVSYSIMASDLEPLALASYVSMSAQSGVVFAQRAFDYEQLRTFELTLQARDQGSPALSANVSLRVLVGDRNDNAPRVLYPALGPDGSALFDMVPRAAEPGYLVTKVVAVDADSGHNAWLSYHVLQASEPGLFSLGLRTGEVRTARALGDRDAARQRLLVAVRDGGQPPLSATATLHLVFADSLQEVLPDITDRPVPSDPQAELQFYLVVALALISVLFLLAVILAVALRLRRSSSPAAWSCFQPGLCVKSGPVVPPNYSQGTLPYSYNLCVAHTGKTEFNFLKCSEQLSSGQDILCGDSSGALFPLCNSSESTSHPELQAPPNTDWRFSQAQRPGTSGSQNGDDTGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 99875
Sequence Length: 923
Subcellular Location: Cell membrane
|
Q9PP01 | MKKFDKLGLDNIKEIFHNLSYDELNAHEKANNEGLSTDNDTFCVDTGIFTGRSPKDKYFVKQDPSSKYIAWGKVNQPITKELFDKLLTKAKQELSGKKIYVQDVFCGASLQSRKAVRFVTEIAWQAHFVKNMFIRPSQEELENFKADFIVYNACKCINEDYKQDGLNSEVFVIFNVEENIAVIGGTWYGGEMKKGIFSMMNYWLPLENKLSMHCSANVGEKDDVALFFGLSGTGKTTLSTDPKRRLIGDDEHGWDDEGVFNFEGGCYAKTINLDPEHEPEIYGAIKRNALLENVVLRADKSVDYADASKTENTRVSYPIEHIENHEPSLKAGHPKNIIFLSADAFGILPPVSKLSKEQAMYYFLSGYTAKVAGTERGITEPQATFSACFGEPFMPLHPTVYARLLGEKIEKHEVNVYLVNTGWSGGSYGVGKRMSIKATRACINAILDGSITKCEFENFEVFDLAIPKALEGVESVLLNPINTWLDKNAYIATRDKLAHMFIQNFKRYEDVKEGIEFSKFGPKI | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequence Mass (Da): 59054
Sequence Length: 524
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.1.1.49
|
Q21BR2 | MQETGVRNGAYGADKFGLKNLKGVKWNLTAPHLYEDALRAGEGVLSGDGSLCVDTGIFTGRSPKDKYTVRDANTENTMWWGGNQSITAEQFENLYQDFLKHAEGMSLFAQDLYGGADPSFQIKTRVFTEMAWHSLFIRTLLRRPETAELASFVPELTIIDLASFRADPARHGCKSENVVAIDFTRKIVLIGGTQYAGEMKKSVFTTLNYYLPDKGVLPMHCSANVGPDGDTAIFFGLSGTGKTTLSADPNRTLIGDDEHGWGKDGVFNFEGGCYAKCIKLSAEAEPEIFAASNRFGAILENCVLDPITRKPDFNDGSKTENTRSAYPLESIPNASPTGRAGQPKNVVMLAADAFGVMPPIAKLSPAQAMYHFLSGYTAKVAGTERGVTEPTPVFSTCFGSPFLPRDPSVYGNMLRELIAKHGVDCWLVNTGWTGGMYGTGHRMPIKVTRALLTAALDGSLRNVEFKTDPYFGFAVPTALPGVPSEILDPVKTWADKAAFDTTARKLVAMFQKNFTQFEAQVDAEVRAAQPEAKLAAE | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequence Mass (Da): 58390
Sequence Length: 537
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.1.1.49
|
Q13E86 | MQETGVHNGAHGADKFGLKNLKGIYWNFGAPQLYEHALRNGEAVLSADGALVADTGVFTGRSPKDKFTVRDATTETTMWWGGNQSITAEQFETLYQDFIKHAEGMTLFAQDLYGGADPSFQIKTRVFTELAWHSLFIRTLLRRPDRADLAAFVPELTLIDLPSFRADPKRHGCRSENVVAIDFARKIVLIGGTQYAGEMKKSVFTTLNYYLPERGVLPMHCSANVGPAGDTAIFFGLSGTGKTTLSADPNRTLIGDDEHGWGKDGVFNFEGGCYAKCIKLSPEAEPEIFAASSRFGAVLENVVLDEITRKPDFDNGSKTENTRSAYPLESIPNASPTGRAGQPKNVVMLAADAFGVMPPIAKLTPAQAMYHFLSGYTAKVAGTERGVTEPTPEFSTCFGSPFLPRDPSVYGNMLRDLIHNHNVDCWLVNTGWTGGKYGTGHRMPIKVTRALLTAALDGSLRNAEFRTDPYFGFAVPTALPGVPSDILEPAKTWADKAEFDKTARALVGMFQKNFAKFEAQVDADVRAAAPDVKIAAE | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequence Mass (Da): 58485
Sequence Length: 537
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.1.1.49
|
Q16AH6 | MTHGRVNPDFRLEDQGITGLGTVYYNLIEPDLIQYALARGEGSLGKGGSFLVTTGKFTGRSPKDKHVVKTDSVADTIWWENNREMSPEGFDQLYTDMLAHMEGRDYFVEDLTGGSDPKHAINVRMVTELAWHGLFIRHMLRRPDREDLDDFIADFTVINCPSFQADPAKHNCRSETVIAMNFDKKLILIGGTEYAGENKKSVFTLLNYLLPEKGVMPMHCSANHAVGNPVDTAVFFGLSGTGKTTLSADPARTLIGDDEHGWSDTGTFNFEGGCYAKTISLNPEAEPEIYATTEKFGTVIENMVYDAETKDLDFEDDSLTANMRCAYPLHYISNASQAARGGHPKNIIMLTCDAFGVLPPISRLTPAQAMYHFLSGFTSKVAGTERGVTEPEPTFSTCFGAPFMPRRPEVYGNLLREKIATHGATCWLVNTGWTGGAYGTGSRMPIKATRGLLTAALDGSLADAEFRKDPNFGFQVPVDVTGVPGILLDPRRTWDDAEAYDRQAAKLVKMFSDNFEQYLPFIDEDVRAAAIS | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequence Mass (Da): 58648
Sequence Length: 532
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.1.1.49
|
Q1AY78 | MDLAVRKMTLEGLGVSQLGAVHENLPPARLVEASVRRREGMLAENGALVCLTGKRTGRSPKDRFIVENGLTRGPVDWGPVNKPFPGERFERLLAKASAYLENLEEVYVVDAYAGADPRYRLNVQVVCEYAWQALFTRQLFRRPSREELDAFEPDWTVISVPGLLTDPEEDGTESETFVGIDFGRRVVLICGTRYAGEIKKSIFSVLNFVLPTEHGVFPMHCSANVGPGGDVALFFGLSGTGKTTLSSDPERYLIGDDEHGWSDEGIFNFEGGCYAKCIDLSREKEPQIYDAIRFGAVLENVVVDRITRRVDYSDASLTENTRAAYPLEYIEGAVDSGRAGHPAAVLFLTADAFGVLPPISVLSPEQAAYYFLSGYTAKLAGTEADMEADVEATFSACFGAPFLPLPATTYAAMLSEKLREHGSRCYLINTGWSGGPYGVGERVDIAATRQMVRAVIAGNIDESKTYTDPFFGLQVPLEVPGVPSGILNPRETWADRAAYDDQAAKLADLFRENFKKFEDGVPEGVRKAGPNV | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequence Mass (Da): 58233
Sequence Length: 532
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.1.1.49
|
O54075 | MTAEGPLAPEDRVLDREAIGRLCVSLIAAEQQDLLREGRVGHHQMIGARLLTAGHPSPDDLLIDEDTLGLDSLLMLSLVTRVAGFFHLSDSNTEDYLLVRRRLGEWVDLIDHHHTLMGPKARFTFATSGSTAGPKPVTHSAAALLSEGQAIAKILTERPPEVRRVLSCVPAHHIYGFLWSCLFPSRRGLEAKQLANLSASGIMRHARSGDLVVGTPFIWEQFADLDYRLPGDVVGVTSGAPSTAETWRCASALGPARMLDIYGSTETGGIGWRERRDDPFRTLPDLACFHDTLSRLGRRLDLQDEIAWDKDGGFTILGRKDEILQVAGSNVSPAAVRDILLRNPRVRDAAVRLDGRRLKAVISVAEGADEAEIEIELRATAARHLPAPARPDRFLFATELPRTGAGKLADW | Function: Converts p-coumaric acid into p-coumaryl CoA. This is necessary for the activation of the photoactive yellow protein (PYP) chromophore.
Catalytic Activity: (E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphate
Sequence Mass (Da): 45008
Sequence Length: 411
EC: 6.2.1.12
|
P42516 | MQGLNADEVLRLLRSLIPGELATGRGQRGDPPEAQDLCADSRLDAEPIRADSLDRLNLASALNRFFRLHETGVEDRLLAVRRIGDMAELIADASQHTSGLTFSTSGSTGTPQPHHHSWAALTQEAEALANALGSHPRVIAWLPVHHLYGFVFGVALPRALGSTVIESHAAPTALFREPAPDDLIATVPARWRYLFDSNHRFPGGTGISSTAALETACRNGLLQAGLDALLEVYGATEAGGIGLRWAPSEDYRLLPHWHGDATATSSALNPDGAAVTVAPLDRLQWRDERVFRPTGRIDDIIQIGGVNVSPGHVARRLESHEAVAACAVRSHGEGSRRRLKAFIVPARSDADPETLRQTLENWIWEHLPAVERPTDLRIGTELPRNAMGKLQ | Function: Converts p-coumaric acid into p-coumaryl CoA. This is necessary for the activation of the photoactive yellow protein (PYP) chromophore.
Catalytic Activity: (E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphate
Sequence Mass (Da): 42439
Sequence Length: 391
EC: 6.2.1.12
|
O69140 | MVRRLLISLIRAEARRGRNQILPEAAFTGDPRIDEEGLGFDSLARLDLIGAVRDFFDLSRTGIEDYVYVEPTLQGWIDRIMQHFDLLAARSETAQAVFRTSGSTGTPKPIPHPWPKLMREAASMARDQGLVPAPGGAVIGLVPAHHLFGCLFTALLPELAGAALRDLTAAPPASALRTAQPGDLIIATPHLWAHLGAAGAFPPGLRGVSSGAPMPDALWHSLLAAGLEDLTEVYGASETGGIGLRRAPGAAFTLLPFLSRSADDGISDGPAPLPLQDRLRWTGPVRFVIEGRLDQALQVGGVNVRLGHVKSVLEAEPGVEALALRLGGDRLKAFVVCAADAEAGLEARLRARAEAGLDAPARPQHYRFGRALPLTREGKARDWD | Function: Converts p-coumaric acid into p-coumaryl CoA. This is necessary for the activation of the photoactive yellow protein (PYP) chromophore (By similarity).
Catalytic Activity: (E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphate
Sequence Mass (Da): 40942
Sequence Length: 384
EC: 6.2.1.12
|
A7IQE5 | MNQAAVQLPLPGFEQASGQWRSDYSRQVAGEKPVRNRSGIEVQPLYSPRDWAGERYLDDLGFPGQYPFTRGIYPSMHRGRTWTQRQLIGLGTPQDYNVRVRRIIDAGATAISLLPCCSGFRGIDCDEVDPVLLGTCGTVVNTTDHMDAALDGVPLGTISTAMNDPSPFTLLAFTLGVARRRGIDWRSITGTSNQSDYISHFIANHQFYRLSLPGSRRVLLDHIEFCRRALPNWNPLSVVGQHMQQAGATPAETMGFTLSSAIQYAQDCIERGMDVDDVLRRFTFFFDISISFFEEIAKFRAGRRIWARIARERLGAKDPACWRFKFHGQTSGVDLTQQQPLNNIARVSVQAMAGILSGLQSMHTDAYDEAIACPSEETARIAVATQNILRDEAQLCAVIDPLGGSYYVERLTDQMEAEIEAVIARIDAAGGMYKAAEVGLVQTMIGESALAFQEQLETGERKIVGVNCYQVEEDPTIPPAERPDPEAMERHVERFKVFKRERSQDAVARALDALARAANSERENVFEKVVEAAEAGVTHGEMVGCLRRELGFGHPLIIA | Function: Together with Xaut_5044, catalyzes the reversible isomerization between pivalyl-CoA and isovaleryl-CoA, using radical chemistry. Does not exhibit isobutyryl-CoA mutase (ICM) activity.
Catalytic Activity: 3-methylbutanoyl-CoA = 2,2-dimethylpropanoyl-CoA
Sequence Mass (Da): 61992
Sequence Length: 559
EC: 5.4.99.-
|
Q9SWW5 | MEVASLYRRVLPSPPAVEFASAEGKRLFAEALQGGTMEGFFNLISYFQTQSEPAFCGLASLSVVLNALAIDPGRPWKGPWRWFDESMLDCCEPLHKVKAEGITFGKVVCLAHCAGARVQSFRADQTTIHDFRAHLTRCASSQDCHLISSYHRSPFKQTGTGHFSPIGGYHAEKDMALILDVARFKYPPHWVPLTLLWDAMNTTDEATGLLRGFMLVSRRSSAPSLLYTVSCGHGSWKSMAKYCVEDVPNLLKDESLDNVTTLLSRLVESLPANAGDLIKCVIEVRRKEEGESSLSKEEKERLFLKEKVLQQIRDTDLFRVVHELQYPKGLCGSCSSSSDEDSLAEIAATVCCQGAAFLSGNLVSRDGFCCRETCIKCIEANGDGLKTVISGTVVSKGNEQAVDLLLPTSSSKTSLCNSNLKSKIVKYPSSTDVLTVLLLVLQPNTWLGIKDENVKAEFQSLVSTDNLPDLLKQEILHLRRQLHYLAGCKGQEACQEPPSP | Function: Involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants.
Catalytic Activity: [Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly + glycine
Sequence Mass (Da): 55045
Sequence Length: 500
EC: 2.3.2.15
|
Q9ZWB7 | MSMASLYRRSLSPPAIDFASFEGKQIFNEALQKGTMEGFFGLISYFQTQSEPAFCGLASLSMVLNSLSIDPGRKWKGPWRWFDESMLECCEPLEIVKDKGISFGKVVCLAHSSGAKVEAFRTNQSTIDDFRKYVVKCSTSDNCHMISTYHRQVLKQTGTGHFSPIGGYNAERDMALILDVARFKYPPHWVPLKLLWDAMDSIDQSTGRRRGFMLISRPHREPGLLYTLSCKDESWISIAKYLKEDVPRLVSSQHVDTIERILYVVFKSLPANFNQFIKWMAEIRRTEDVNQNLSSEEKSRLKLKQELLKQVQETKLFKHVDKFLSSVYEDNLPYVAAKVYCDGDEILSGYESDESCCKETCVKCIKGLGEEKVTVVAYPSGNDVFTALLLALPPQTWSGIKDQSLLQEMKQLISMVSHPTLLQQEVLHLRRQLEMLKRCQENKEDEELSAPA | Function: Involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants.
Catalytic Activity: [Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly + glycine
Sequence Mass (Da): 51551
Sequence Length: 452
EC: 2.3.2.15
|
Q6UW60 | MRPAPIALWLRLVLALALVRPRAVGWAPVRAPIYVSSWAVQVSQGNREVERLARKFGFVNLGPIFPDGQYFHLRHRGVVQQSLTPHWGHRLHLKKNPKVQWFQQQTLQRRVKRSVVVPTDPWFSKQWYMNSEAQPDLSILQAWSQGLSGQGIVVSVLDDGIEKDHPDLWANYDPLASYDFNDYDPDPQPRYTPSKENRHGTRCAGEVAAMANNGFCGVGVAFNARIGGVRMLDGTITDVIEAQSLSLQPQHIHIYSASWGPEDDGRTVDGPGILTREAFRRGVTKGRGGLGTLFIWASGNGGLHYDNCNCDGYTNSIHTLSVGSTTQQGRVPWYSEACASTLTTTYSSGVATDPQIVTTDLHHGCTDQHTGTSASAPLAAGMIALALEANPFLTWRDMQHLVVRASKPAHLQAEDWRTNGVGRQVSHHYGYGLLDAGLLVDTARTWLPTQPQRKCAVRVQSRPTPILPLIYIRENVSACAGLHNSIRSLEHVQAQLTLSYSRRGDLEISLTSPMGTRSTLVAIRPLDVSTEGYNNWVFMSTHFWDENPQGVWTLGLENKGYYFNTGTLYRYTLLLYGTAEDMTARPTGPQVTSSACVQRDTEGLCQACDGPAYILGQLCLAYCPPRFFNHTRLVTAGPGHTAAPALRVCSSCHASCYTCRGGSPRDCTSCPPSSTLDQQQGSCMGPTTPDSRPRLRAAACPHHRCPASAMVLSLLAVTLGGPVLCGMSMDLPLYAWLSRARATPTKPQVWLPAGT | Function: Proprotein convertase involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues (By similarity). In males, important for ADAM2 processing as well as other acrosomal proteins with roles in fertilization and critical for normal fertilization events such as sperm capacitation, acrosome reaction and binding of sperm to zona pellucida (By similarity). Also plays a role in female fertility, involved in the regulation of trophoblast migration and placental development, may be through the proteolytical processing and activation of proteins such as IGF2 . May also participate in folliculogenesis in the ovaries (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 82795
Sequence Length: 755
Subcellular Location: Membrane
EC: 3.4.21.-
|
P29121 | MRPSQTELWLGLTLTLALLAVRWASAQAPIYVSSWAVRVTKGYQEAERLARKFGFVNLGQIFPDDQYFHLRHRGVAQQSLTPHWGHRLRLKKDPKVRWFEQQTLRRRVKRSLVVPTDPWFSKQWYMNKEIQQDLNILKAWNQGLTGRGVVISILDDGIEKDHPDLWANYDPLASYDFNDYDPDPQPRYTPNDENRHGTRCAGEVSATANNGFCGAGVAFNARIGGVRMLDGAITDIVEAQSLSLQPQHIHIYSASWGPEDDGRTVDGPGLLTQEAFRRGVTKGRQGLGTLFIWASGNGGLHYDNCNCDGYTNSIHTLSVGSTTRQGRVPWYSEACASTFTTTFSSGVVTDPQIVTTDLHHQCTDKHTGTSASAPLAAGMIALALEANPLLTWRDLQHLVVRASRPAQLQAEDWRINGVGRQVSHHYGYGLLDAGLLVDLARVWLPTKPQKKCAIRVVHTPTPILPRMLVPKNVTACSDGSRRRLIRSLEHVQVQLSLSYSRRGDLEIFLTSPMGTRSTLVAIRPLDISGQGYNNWIFMSTHYWDEDPQGLWTLGLENKGYYFNTGTLYYYTLLLYGTAEDMTARPQAPQVTSRARACVQRDTEGLCQESHSPLSILAGLCLISSQQWWWLYSHPQQPVTEGQASCHPPVTPAAAA | Function: Proprotein convertase involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. In males, important for ADAM2 processing as well as other acrosomal proteins with roles in fertilization and critical for normal fertilization events such as sperm capacitation, acrosome reaction and binding of sperm to zona pellucida . Also plays a role in female fertility, involved in the regulation of trophoblast migration and placental development, may be through the proteolytical processing and activation of proteins such as IGF2 (By similarity). May also participate in folliculogenesis in the ovaries .
PTM: N-glycosylated.
Sequence Mass (Da): 73214
Sequence Length: 655
Subcellular Location: Cytoplasmic vesicle
EC: 3.4.21.-
|
P29122 | MPPRAPPAPGPRPPPRAAAATDTAAGAGGAGGAGGAGGPGFRPLAPRPWRWLLLLALPAACSAPPPRPVYTNHWAVQVLGGPAEADRVAAAHGYLNLGQIGNLEDYYHFYHSKTFKRSTLSSRGPHTFLRMDPQVKWLQQQEVKRRVKRQVRSDPQALYFNDPIWSNMWYLHCGDKNSRCRSEMNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRYDASNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNYIDIYSASWGPDDDGKTVDGPGRLAKQAFEYGIKKGRQGLGSIFVWASGNGGREGDYCSCDGYTNSIYTISVSSATENGYKPWYLEECASTLATTYSSGAFYERKIVTTDLRQRCTDGHTGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSRPAHLKASDWKVNGAGHKVSHFYGFGLVDAEALVVEAKKWTAVPSQHMCVAASDKRPRSIPLVQVLRTTALTSACAEHSDQRVVYLEHVVVRTSISHPRRGDLQIYLVSPSGTKSQLLAKRLLDLSNEGFTNWEFMTVHCWGEKAEGQWTLEIQDLPSQVRNPEKQGKLKEWSLILYGTAEHPYHTFSAHQSRSRMLELSAPELEPPKAALSPSQVEVPEDEEDYTAQSTPGSANILQTSVCHPECGDKGCDGPNADQCLNCVHFSLGSVKTSRKCVSVCPLGYFGDTAARRCRRCHKGCETCSSRAATQCLSCRRGFYHHQEMNTCVTLCPAGFYADESQKNCLKCHPSCKKCVDEPEKCTVCKEGFSLARGSCIPDCEPGTYFDSELIRCGECHHTCGTCVGPGREECIHCAKNFHFHDWKCVPACGEGFYPEEMPGLPHKVCRRCDENCLSCAGSSRNCSRCKTGFTQLGTSCITNHTCSNADETFCEMVKSNRLCERKLFIQFCCRTCLLAG | Function: Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway, with unique restricted distribution in both neuroendocrine and non-neuroendocrine tissues.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 106420
Sequence Length: 969
Domain: The propeptide domain acts as an intramolecular chaperone assisting the folding of the zymogen within the endoplasmic reticulum. Isoform PACE4D lacks the propeptide domain.
Subcellular Location: Secreted
EC: 3.4.21.-
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.