ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
| texts
stringlengths 117
4.4k
|
|---|---|---|
A0A7Z9G3F1 | MSAQKTQKNEQRPKGKKGAKKVSKPKPSTSKRWGKWGLDFLLATLAGCMVFLSFPDYDYFPLQWFSLIPLLAVLKGKAPKAAFGWGLWTGTVTNCGGFYWITSMLMDFGHFSLAVAIPICILLCAYQGLVFAFWAAFSSWLSEGFTARVLWVVPLVWVVVEYCIPLIFPWYFANGQYLFYAVIQICEITGVMGLSFLIVLFNTGLYLGIINGSQKGFTARWRPALVVIVLFLANLLYGVVRIGQVDALSEQSEKLKIGMVEANVGIFEKQARGVGDRSKRYDLLQGNVLKHHLLSKELEEKHQVDLIVEPESSFISAWPRAFVRFKRNDLFGVTAGHGRNLWLNNGGSWNGPERLAGKNTVIRGLSAAREDQVFAVGDQGLVLRLKKGEWVSLKSPTESNLLSVWSGAANPRMTAMDGSALNTFVVGEDGSSFVHHPTTGWKTLNTQTRSHLRAVMGSHSNRVYTVGDGGVILRWNGKGWYAQKSNTTYNLHSLWVTPSGVATAVGQSGVLLTLSGSKWRGTRLGNQDLNGVAAFGKNRVAVGNGGVIWEGRNGQWNRVTSPTTKNLHDVSADGWGNFFAVGDAGTVVVRSRDGQTWTMAPPLQPAESLRAVAGIPFTTSHAFARESRYAFVSKAPLPEVNDRIQAAGNIEPAFELDRHTSGMDWNTPLRDTTTPLLLGLLSYERSDPEGDPLASKRSRKNYNSAMLIEPDGRIVDRYDKTFLLMFGEFIPFGDVFPQFYEWLPQASHFYPGTSVKTFAFRGHKLGVMICYEDILPSFSRKLAGQDPHVLINVTNDAWFGKTSEPYLHLALAVFRTVESRLWLVRSTNTGVSAFVDAVGRIVSQTDLDNPEVLVADVPMLRTSTFYRSYGELFTYACFLVFAVLVIGVLSRRRKKRVAQA | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 900
Sequence Mass (Da): 99805
Location Topology: Multi-pass membrane protein
|
A0A7Y5C632 | MPRKKKSEETGTEEAGVATATAEHDHDHDHDHDHDHDHDHGHHHHHGHDHDHDHGEEEFEFAEDPTFDVDYKGECAYEVKVLVPAANRSKQADSMYNEIRESAEVPGFRRGRAPRPLIERKFAKHVKAEVDGKLISAAFQKLVKDKKLTPIKMPDVDGLEALREQPQSEPLAFTLKFEVSPKVELGKYRGVKVERPVVTVDAKDVKEALDELRGRYSTFETADAKTKAKDGDQVIIDFKGAVDGEAFSGGSAENYPYILGTKRFFPEFEKALKGAKTGDELTCTVKLPEESPNADLRGKKAEFTINVKEVKRRSLPDLNDDFAKQVGAENVDALKERIKNQLTSNSAEHSDRVARARALDAVIAVSKYELPKSLVEDVARGLMEDRARELVRQRVPVDQIEHRREELMAESKKQAELEIKRMVTLNEIGDAEGVTVTDEDFETMAEDIAMRTGMRADMVSQYMSEESQRRGTYEGRIFREKAIKIVMENAKITDKEVERDELEEQANDADA | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 511
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence Mass (Da): 57734
|
A0A7Y5GXF7 | MGIQQIDEEIWLKVGVEIPEAAEEPFLGALGEWTSRGVEVLTDGTRPVVPALESMPPCWIRLSLYGRPNEIEELQYVMYEALSLLKSLFIAPDTSRMLPVEAVEPGWRDRWKSFFHVTQVSPRLVIRPSWEQYTAKSGEYVIDLDPGTAFGTGGHATTRLCLVALDALIAKGAPEPRVLDFGTGSGVLAIAAAKLGASVVVALDNDDEAVGVATENVAQNNVARIVSVANTPLEQISQQFDIIVANILGAVLVKLRDVILSKLVGGGTVVLSGILQEEAQQVAAAYVAGGMQMVSRRDEGEWSALELRAPE | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 311
Sequence Mass (Da): 33516
|
A0A7C1CK24 | LDSMVVGENEIMGQLQQTYEAARHAGVLNRTLSVMFQRALKCGKRVRAETRIGAGKVSVASVAVDLAQSILKDLGDKTAMIIGSGQISELALKSLVEHGVGKVMVLNRTLERAQNLAAKFKGEAIVLAALPDHLHRADILISSTGASDLILRRADFERAIVQRGRAPMFVIDIAVPRDIEREAAHVENVYCYDIDDLQSAAQRNLRRRQDEIGDCEAIIQAEVENYLAWRRRLNMEPLIAALTQRFNKIREQELKRTLDKLPELSPEKRGEIEKLSRRIINNLLRDPITAIKSEALGDHSDTLMELAQRLFGVHETEQ | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Length: 318
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Sequence Mass (Da): 35599
|
A0A2J0MJH8 | MKALLHICCGPCAVYPARALKNEGFDVDGFFYNPNIHPYSEYKKRYEAVLAAAERLS | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
EC: 1.17.99.6
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Length: 57
Sequence Mass (Da): 6452
|
A0A2D5QRQ6 | MRKNPRRKRSKDDPKQLLLSLVVVVVFFSIWQQFFPPPVPVAPIDSASQQGQNKLSDLSVENIVSQVAPPSLQNSIPVQNKAHLKPTQAIHTLRDQERFEVVLNSRGELHQWSILEDQYRHRSSETESTPYVLTNFGPKLQAEGGLEAPFLTPMVEVRLNNEVIHGEYQLMPGSTDTQVSFVLRTPQIQVTKHFKIMPNEYRVHAQVEVQNLSASRAHIEVRGITRALQDANASEGGMFSPPLNLLESVCAYGDELERDGVSSVQSKFTDKEPVVFPGARWYGVDSRYFMNSISVTKPVSCAQNVDEKSLRLDRPLPGGFSALITEATLYSDFVGSQSKIQNELTFYGGPKKMELLTASEPSLSEAIDFGIFSPICYLMLWALGFFYSVLPNWGLAIILLTLLVKAITLPLTVKQYRSMAVMKKLQPELQVLKEKFKDDAMRMQQETMGLYKKHGASPLSGCLPMLVMMPIYFALYRTIYSAVELYQAHFFAWLTDLSMPDPYFVTPVVLAGLMFLQAQLQPTNNSMDPAQRRMLTTFMPLMFGGMMLFLPSGLVLYILVNTSLGIVQQKWSQKAMEAQA | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
Subcellular Location: Cell membrane
Sequence Length: 580
Sequence Mass (Da): 65279
Location Topology: Multi-pass membrane protein
|
A0A964NI42 | MNADLDLLKRLEVLSRDLVWTWLEEGPAFWSAFSPEGFAQPPHNPAALLAAMAPEEQLRRAHASMAALLSLETRRAAYLSKMGLDTWHDLVGRPLRGPVAYFSAEFGLHESLPTYSGGLGILAGDHTKSASDLGLPFVGIGLLYRQGYVRQEIDAKGQQQNVYEDFDFATLPISPARALDGGPQLEVLVEMGDETVKCRVFRAVVGRVSLLLLDTDVEGNAPEQRRITQRLYGGDHQTRIRQELVLAIGGLQALCALGIEPQVFHLNEGHSAFLVLERARMALSEGRARDVAEALSLGRRSSVFTTHTPVEAGHDRFDAELLWRHLRPMAEVLGLSRAALLALGHWHDERDAEAPFNMTMLALHACGRYNGVAALHGVVSREMFARFFPGTPVDEVPVRHVTNGVHAPSWQCPELVAMLEHVAPETFRNRPAGDPSWNAVYDLDDAELWHWRTRNKAALFSLIKARETARAARLSRPPPHLELSTDVLTIGFARRFATYKRATLLFSDLPRLEGLLERAPGPIQFLFAGKAHPADHPGQSFIQEVTRLAERFEGRVRFIEGYDIELGRALTRGVDVWLNNPRRPMEASGTSGMKAAMNGVLNLSILDGWWPEGFDGENGWAIGEARVYSTEAEQDAADAASLHHLLEHAVLPTYYTRDALGLPRGWMKMMKRSIATLTPRFSSDRQVQDYVHHIYCPG | Function: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate
Sequence Length: 698
Sequence Mass (Da): 77623
|
A0A964NK03 | MAGPTPRVLVRERRKGGSLRALFRWFFPLTIALAFVGALGLIGAYVHFSRDLPAIYDVDTYAPPGVTRFFARDGRLVGEFTTERRVVVPLADMPASLIQAFLAAEDQRFFEHEGVDVRGVLRAALANFRAGRVVEGASTITQQLCKTLVGKEQSLTRKVREALLARRLESRLSKLDILYLYLNQIYLGHGAYGVQAAAQAYFRKDVGRLSLSESAVLAGLPPKPSLLNPVRDFEGSKERQRWVLGRMVTEGFITTAQADAAAKEPLQVFAEPQDVFADEVPDFVEHVRRYVQATYGYDALNRDALEVHLTVDVDLQRAAERSLKQGLSSLGERQGYVGPITNLDDARAKAALDRLRGRSAAHVHAGPSVGSQVGPPDAAPPVSAMVPAIVRAVSRTRIDIEHAGGLGSITQGDLSWAAPWSAEDARNERRQKDAREVVRPGDLVLVAPTRRPSEFRLAQVPPVQGALVSMELQTGAVVAMVGGWDYDQSEYNRAFQGCRQPGSVFKPIVYSRALDLDYTLATLVSDTPVSVFDVANQLLWKPKNFGGGFLGDVLLHRAFVNSMNVPAIKVLDYIGAETAVAWARHLGLTTPMYPDRSLVLGSSCVLPWDLLQVYAVFGQRGLRARPAFVSRITRRDGTVLEDRTHFADPWAPAGARLDGMLRTWGEPHERVVDERTAYLLQFALKGVVDSGTAVAAKRLGKVAGGKTGTTDAYDAWFVGFTESLVTGVWVGSDRNDRKLGDGETGGRAALPIWLEFMQEALAGRNQADFTSQPPVGIVFADIDLETGRLAATGRPSMQLPFKEGTIPVEAAPAAGTFGRADVDVIEGRF | Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
EC: 2.4.1.129
Subcellular Location: Cell inner membrane
Sequence Length: 829
Sequence Mass (Da): 90382
Location Topology: Single-pass type II membrane protein
|
A0A2E8RWP9 | MSQQGTIVLTGGGTGGHIMPALAVAAALRSQAPDVELHYVGTRGGMEESFARDHGIEFHGLKLYPFFGKPVLTKIRALATLPGSLFSAYRLLKRLRAEVAVAFGGYVSAAVGVVAPRMGIPLFVQEQNAIPGRTTRMLSKRSRLVCAGLPAVATHLPNADVHVTGNPVRPDIEAVGAEERPALSPLRLLIMGGSQGAAFLNENGPAIAALLASRGYELQVHHQIGRGNLDEVQAAYKNIAIEAHVEPFIDDMAAAYRNCHIALARSGALSVSELWTSATPAVFVPFPYAVDDHQTHNAASMVETGAAAVIQQRECSVEALCDALESHCTSAAIYAERRQALRDSAPHRAAEECARQILRALPQRGEA | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
EC: 2.4.1.227
Subcellular Location: Cell membrane
Sequence Length: 367
Sequence Mass (Da): 39042
Location Topology: Peripheral membrane protein
|
A0A2E5HL44 | MVVIGGPTAAGKSGLAMALAERLGGELVSADSAQVYRGMDIGTAKPTAEEQRRVPHHLVDVVDIDEEFDAGRFVELADAAIADIRARGRLPIVVGGTGMYLRALMYGLADAPPADPELRVALQGRIAAEGSAALHGELAEVDPDAAAKIHPNDAVRIVRALEVYQLTGEPISAHQRAHAVHDRPPRHEALQVVVAPER | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 198
Sequence Mass (Da): 20945
|
A0A819MFE1 | MAAVTNNTPVSNSIATSTRFTDEYDLKEELGKGAFSIVRRCIQKSSAQEFAAKIINTKKLSTRDHQKLEREARICRQLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREFYSEADASHCIQQVLEAVRHCHESNIVHRDLKPENLLLASKTKGAAVKLADFGLAIEVTGEQTQWYGFAGTPGYLSPEVLKKEPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYNQIKAGAYDYPSPEWDTVTTEAKRLIDSMLNINPSRRISATDALKHPWICQRERVAGTIHRQETVDCLRKFNARRKLKGAILSTMFVNRTLIPNAAVSATGTQSTSNGKKSSIGTGPILPATNPIMSASASGGNRSRATTQSGSSAIKESGDSNSATIDDTNDIDRLSLEITKVTEQLLQAIANSDYDMYKSLCDPKITCFEPETIGNLVEGLDFHKFYFDTVLSVKASKPTINCTMLTPVVHTLGDESACIAYVLLLQYIDRSGQAQSVRTEETRVWHKKDSRWLCVHFHRSGMFAQYFVLFVLSTCTLISANDDLSSQRFRGHVLKTNGKYEIVTALATSYKEPNKLEDHVLATGFWDQTYNKTGWSVLEIQTLDNETNFDQAYSAGVLEGQFTRELIGYQWQNNIDDICTNKTEFCYYLKQFFLIQLDWMYTQIESYPNDEYWHQVNLLLIQLNGLIDGYNNTLRGPRKELDDPLSFL | Function: Putative phospholipase.
EC: 3.1.1.-
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Length: 714
Sequence Mass (Da): 80597
|
A0A7C7YH33 | MAVTGIVLCGGRSSRMGRDKPWLPWRGRPVLCHVVERLAEAVDEVIVVSAPGQSLPVTHARRVEDHEEGLGPLAGLRAGLAASASGLAFATAADSPFLTPDFVRAVLAPGQAAAPEAEGRVQTLSAAYPTEAGETARSLLEQGRRRPLDLLEHYNFQRLPLSSLPNPESVRGFNTPGEYLAAAQRDTPGGLARVAFDSSAGTTPGKGACEVGIGTLGEVLIAAGAGPEFLQGDSLCAPFVACLDGRIRVKDTRIPIGAGENVTVLKEFTPDEA | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytoplasm
Sequence Length: 273
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 28480
|
A0A964NDU0 | MTEWPLLTGDLEGIGGRLSPLPADFLVDEVPAYAASGEGTHHYVRIEKQGLTTADVRLALATAAGVDPRDVGFAGRKDKHARTTQWFSLPAPAVDPGINGLRLLEVTRHANKLKLGHLRGNRFQITLVDVSEEAERRLPPLLARLADGFPNAYGEQRFGAAGRSYDQALRFVAAPRRRVSDPGFLASVIQAAGFNTWLAARLRDGLFGKGIAGDVLKKRDTGGLFVSPDAETDGPRVERAEVDPTGPMFGRRMFAAEGPSLLREEVAKASMPLTVAEWAVVDQWAAGTRRVARVVAEELSISRTETGLVLSFFLPSGCFATVFLAELMHPPGRLRLPIEG | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
EC: 5.4.99.27
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Length: 340
Sequence Mass (Da): 36811
|
A0A7X7JNE5 | MDQVTSSAAQLRAGLQALAHPLPGGMRDLLPWEARQQLHLSRVVLKAFELHGFQQVILPAFEYADVLEQGLGPIEANSVLRFVEPETGEVVALRPDMTPQVARLVATRLASEPGPVRLSYRGSVLRRRHERARHQQQVVQAGIELVGRGGLAGDLEVLEAATHAVRRAGLERFVLDLGHGRIASSLLDDLSAEARERLLEPLTQKDQAELVRRAEKLGLSAARVRALAALPELQGGGEVFDAARRLLADTAALPLVDELQLLHRAVEEAGLAPSVVVDIGETRPFAYYTGPLFQVLAEGPGQAVGSGGRYDTLYERFGVPRPAAGFAVHVNNLGWAVGDAQRLGIPLRALVVSSPAASGTADAAGAAEVLGTLRTAEIPCALSDGTNPLDYARAWRYSHVVWLTSARRVRVSQLTSDGERDRGEVDVVELPARLLAG | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Subcellular Location: Cytoplasm
Sequence Length: 437
Sequence Mass (Da): 46954
|
A0A956DPI9 | EDRAENIRRVGEVAALFAEAGVIAIASFISPYAVARERARERAGRGAFVEIYLDTPLAVCERRDPKGLYKKARAGEIPEFTGISAPYEVPEDPSLRLDTDALSVEACVDLVVDHLRAERFLSVR | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Function: Catalyzes the synthesis of activated sulfate.
EC: 2.7.1.25
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Length: 124
Sequence Mass (Da): 13689
|
A0A956CRD8 | MSHHSELIEQDIEAYLEQHQSKELLRFVAVGSVDDGKSTLIGRLLHDTHGVYEDQLSAVKRASKQADVEIDFSLFTDGLKAEREQGITIDVAYRYFSTEKRKFIIADTPGHVQYTRNMATGASTANVAIILIDARLGVLQQSRRHAYIASLLGIPHLFVCINKMDLVDYDQQRFETIRGEFTEFARRLGFKDVTFIPISALRGHNVVHPAESMRWYSDAGGKTLLAHLETVPIAEDRNLRDMRFPVQYVLRPNLDYRGFAGQIASGRIQCGDEVLVLPSLRTSRVKSIDTFDGSIEEAFAPMSVTLRLEDEVDVSRGDMLVHASERPQVAQDFDAMLVWMSETPLDLGRSYFIKHTAQYVRAEVQEVLSHTDLETLEPTPAGGLELNEIGRVRIRAHRPLFIDSYARNRATGAFIVIDSVTNDTVAAGMIADSVQRGSTSMGDDHTQVSAGERRRRLGHAPALIELAGDPSEMKSLAFAVERVLFDRNYVAISMGPEQAHTPEAAWATIERLLALGAVVVWLTRAHLIGIFSDDPDVVRLGAAYLGFAVFNFNAYAILILGGGILQGMRLPLYAMGVALFRHVFGPLVVLYLLDPVMGFGLPGIYWGIVIIAWIGSAVTLFYLRRELPDLPAAESLTR | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
Function: With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
EC: 2.7.7.4
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Length: 638
Sequence Mass (Da): 70910
|
A0A956I3X5 | LIEGLQDRQFALYSKIHHAAIDGVGGVRLAQSILSTDPDERRDYSPFSLEAYERAKASRPPRDSEPPTEKEMRRVAEVLRESFGVGKSVFSGLAAYARAWLKPDEHGLTTSWAATPVTSFSTKITGARRFVAQSYSLPRVREVGKALDGTINDVVLAMCGGALRRYLLSRDELPEAPLTAMTPVSLRAETDRGVGNAVGALTANLATHIADPAKRFEVIKTSMTEGKSLLSSMSPKEIELFTQLTHAPPLLIGALGLGDRFPPYSTVISNVPGPRERSYWNGARLDGMYPMSAIYHGFALNFTLLSNADQLDFGVIACRESVPSCQRIIDHLEEALVELEEVAGV | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 345
Sequence Mass (Da): 37631
|
A0A2D9HCQ3 | MVRWIAGGRVIDPDQDVDRLADLELADGKVVGLHPVGTAPSQEDTLDASGRWVMPGMIDIHVHFREPGQEYKEDLLTGARAAVAGGVTTVVCMPNTMPAIDKREVVGLLRRRAAQIGLCDVQVCGAISRGLKGEELADLGEMALAGAACFSDDGHAVMNAGLLRRAFEYASDLDLMLMLHEEEMDLSNGGSMHEGAVSSRAGLRGIPSASESALIARDLEIAHEFGGRMHVCHMSTKRGVELVRAAKARGWPISAEVTPHHLFLTDLAVLESHYHGHTKMNPPLRPWEHVEALREGLKDGTIEAIATDHAPHGDVEKDEAFGCCAFGVTGLETSFSLTRRLVDEGVISLSRAVELHTSGPAKVMNWNDRGTFRAGTRADVCIFDPERVWIVDPSVGFSKSVNTPFTGWELKGQVSTTVFGGRVVYHEGKPAA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
EC: 3.5.2.3
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Length: 432
Sequence Mass (Da): 46634
|
A0A2D5QMX0 | MTKVLIIKTGIANTASVEAAFRRCRVNPILSDDPQQIADAEQVVLPGVGAFGPAMAKLRQTGIDEVLISRINADKPLLGICLGMQLLFANSAESPDVEGLAVFDTKISLISGAELRVPHFGWNEVQPFGQTQYLSPGYAYFAHSFRAKFNDFNELAKSGARSTYGVPFISAIEQGRLLACQFHPELSGVWGAQVLQNWLEGTC | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
EC: 4.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 203
Sequence Mass (Da): 22029
|
A0A7Y5GV68 | MTTFYKAHGLGNDFIVFCDADVATANLTTLAMTLCDRHRGIGGDGLLLLGVGQNPADVSMRVLNSDGSEPEMCGNGIRCAVKVCVEKLGITSNPVRVSTRAGLMTCAWGPSTGHSVQWVSVDMGEAIVGPHIAQVTSIINTDTALAVDIGNPHVALFGEFSLETICQLGPRIQALPVFPKGVNVNFATMVSVAPDTDATEIQLTVFERGAGLTLACGTGACATTAAAAYKKWLPLGKPITVTLPGGNLFIEVNQTDRSPDNRFRVTMTGPAEIVYQGTVEDSFLMV | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
EC: 5.1.1.7
Subcellular Location: Cytoplasm
Sequence Length: 286
Sequence Mass (Da): 30089
|
A0A2H0DGQ0 | MATELRWILLVVGVLILWYLVWDARRTKKNNLNINEMDLSQPDPNMEDALFHPKVQSNNYDSGDRFERGEPQIEEDADTRDHEGIESPVRQVNTQEVHDTFIDQVESQIPNDSIKQSRVLKTEVQPVNTEANARSQQQSEVISPSPKTSSKSKQPETNEPELVISINLMAEMNEEYQGVILNQSLNNAGYHIDYRGIYKRFEAKDGSGEYWFSLANAFNPGFFDLDTLDEFSTLGITFFMVLPGPHQPMKAFDAMLKDAVALQDILGGQLQDATHSVLSQQSIQYYRDQILQYQHRKASKETL | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 303
Sequence Mass (Da): 34643
Location Topology: Single-pass type I membrane protein
|
A0A7C3WW56 | MFEQPEKNNNPNPEIELRQRGEIFRLFNRIASKYDITNRLLSLGQDAYWRKKLVRQIRIEKGQDFFLLDLATGTGEVMKTFREFFPDAGYLIGIDLSEGMIREGMEKFHDKKQKYLFAVMDVLYPGIKSEAINAVTMAFGIRNVSEVSRALKEIYRVLKPGGQVLILEFGLPQKGLWRKIYLFYLRHLLPYIGGFWTGCPSAYRYLSETICKFPSHDHFSQLLQEAGFTNTNWIEFNRGAVLLYTANKPNQSE | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 253
Sequence Mass (Da): 29427
|
A0A7C4YSW5 | MGDLASLSERISVIKLATSLSKTRIGLLFFSKTTFPFESSIFKIGDKGTFTTEEALCKLKKINVSAIFIALHGAFGEDGRIQGLLDWIGIPYTGSGCFACALAMNKIRAKAVVKSFGVRVAEHIIFTQDNWSWDRTDACSSVAKALGFPVVIKPASQGSSVGVTIAKDEKEFLDGIEIAFEWDREVLVEKFIKGKEVTCGIWDCQEGLPPKPLPLTEICPKTSSFFDYTAKYTPGATDEITPARLDETLTRKVQEMAILAHKAISCEMWSRSDFIVDDEGPVWIEINTIPGLTPTSLYPQEAQCAGISYKEMVKAFVEFALRKRIS | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 326
Sequence Mass (Da): 35948
|
A0A972D755 | MTSSPPRATGAREPTVPHSRPREIIRTALAASRPLAHANIAPGLLFGQALAYRLEGAFSWRAFVVVHLFGILDHLFIVFANDYADRETDSPARTLVSGGSGVIVEGRATPRTIGCAAVASGVALLGLGLAHGAVLFGLAVLAIALMLAYSYPPLRLSHRGHGEWLQGVGVGLVLPWVGYYVQTGEVDAPFAAFLGPVLLAAASHVVTAMPDLEADRLAEKRTLPVRLGATRAARVAMVTTAIGVVLTLAFAPIGVVARGVVFAGSLLPLTFAATMPPTPARVMPWVFATASSQSTAILGVALASALGV | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 308
Sequence Mass (Da): 31905
Location Topology: Multi-pass membrane protein
|
A0A7Y3BT32 | MGVYAYRGIDARGKSVKGVRDADSAKGLRALLKRDGVLATEILEQSEAARNASRDIDFRRLFQRVSSVDVAVATRQLSVLLRSGVPLVEAVSALIEQLDHPDLKNAFTDTRNKVNEGSTLADALRAHPKIFPPLYVNMVSAGEASGTLEEVLGRLADFLDEQTRLQSKVRGALAYPVVMAVVVVVILFLMMSVVVPKVTSIFENFNQALPWYTSVLIWVSDIFSNYWWLLAALAGGAIFLFRRWKSTDEGRKKWDLFVIEVPLFGPLMIMVAVARFSRTLATLLASGVPVLAAMDITRNVLGNTELMRIVENARDSVREGEGIAKPLRQAGRFPPIMTHMIAVGERTGQLEEMLMHVADAYDQQIEVRVGAMTSILEPVLIVVMGVVVGGIAFAILMPLLQLNEMIQ | Function: Component of the type II secretion system inner membrane complex required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 407
Sequence Mass (Da): 44834
Location Topology: Multi-pass membrane protein
|
A0A7V2TNN6 | MAEPGGVLAAAAGRSAPQGRTGPGKCIEWDRSVTSANRKHTPTEDKLQGSPVPEESFFLSASRWYPRRKIRIGLVLIICMLLISADHATKWWAVAYLKGAPAWHSPGDLVRIVYAENTGAFLSLGGQLPEPWRLGVMIGLNSVILAGLTAWLLFRREIAMWPLVALSLVLSGGLGNLLDRLFRPGHVVVDFMNIGITTSSFSLRTGIFNIADLAIMGGLFMIVAWEIFLAPRNTETQET | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 239
Sequence Mass (Da): 26081
Location Topology: Multi-pass membrane protein
|
W5LQJ5 | MWSSSSTFTMPVFSFSSFTMSRCVRMLSLLLCLLVSFSMAQRSTQIRSSPPRTREVHWENNGHLFSLRSTLSEYYMPSTLRRTSPVFVSRYTILKSQRRHAQRGPAQPGVSTLSQQSGIAVSRSHQHFLNTSQQTQTTRSALEVKSPTPTSQTLSNSPNTTSGPVHGYTKTTTGSTAAMAADEQRQSASRSSSVTLNNTANSNSQVNPRRISDSGMENGLNSNGESRNSVFYDLNPSAGRQQNRGSGYGTRYFHHGLPDLVPDPHYIQAMMYIQRVQMYALRCAAEENCLSRSAYRPSMRDLDFRVLLRFPQRVKNQGTADFLPVKPRHQWEWHSCHQHYHSMEAFSSYDLLDASTGRKVAEGHKASFCLEDTSCDPGVRRRYACTAHTQGLGPGCYDTYHANIDCQWIDITDVSPGDYVLKVTVNPSFQVQESDFSNNVVRCDIRYTGSHVQAHNCRITGF | PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.
Function: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine).
EC: 1.4.3.13
Catalytic Activity: H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+)
Subcellular Location: Secreted
Sequence Length: 462
Sequence Mass (Da): 51896
|
A0A1B6VPP6 | MSRLPSKIYPVVDHPRWVERLGGAGARFIQLRLKDMPSEEIRAQAETAQELAARHNVALVLNDYWELAIELGYEWLHLGQEDLETADLEAIRQTGIRLGISTHSHEELQRALACKPDYVALGPIWETKLKKMAFGPQGVERLTEWRELSGDVPLVAIGGITLDRLPSCLKAGADSVAAVSDFIRAEDPESQIRQWLAAADT | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 201
Sequence Mass (Da): 22404
|
A0A6A6W1L8 | MYNYSEQAVNALHCDSIILCKCLTQCKHSRASIYSHPSTITPTYYLYPDAKHTLCRNVVIYGHCRYENSGCNFQHDRAKISSSGSQNDSKKKFNADSPAFQPTPLQSTTNLQLSANGASSTPRNATISPKALNAAIFTPKSQNVQPIAPSTLSKDVSQEFVPSQSHQSQDYVDYSAGAYDSQYQMDPSAAMALNYDTYNSNSPMTGLSGAASQMSLDPYSQSAAAAQAAQAGFYQNVNAFQPNWHHYFPAPDYLPPRPAYQKSVHEFFISNNLREELSKKMDACAQTLPGGSSNALAVENYHSLVPLPMSSSKSAPIFGYKSFVFKAIDKDDGKPYAIRRLENFSLFDTVNVKEIVNSWKKIINPNVVGIHKMFTTRAFGDGSFIVVTDYHPLTQSLAIHLPSANRRNRDIPTESVLWGYIVQISNALKDIHALGLAARVITPSKILLTSQNRVRINGCGILDVTQGDSNVAQSLEAHQSEDIRRFGVLILSIGLGQPISVFNTPNVQNGQVLNALSQFSQNRNFSPRLQDVVRWLVQGPSDVSPEALQSYDILSFLRAITPEITSTLSSALHAEDRITSLLGAEVENGRLVRLMTKLGMINERTEYDRDPKWSESGARYPLKLFRDYVFHQVDSDNRPSLDIGHVITCLNKLDAGVDEKIMLTSRDNEHIAIMSYKELSGLVTSAYNELSQKPGQYSR | Function: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1.
Subcellular Location: Cytoplasm
Sequence Length: 699
Domain: Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs.
Sequence Mass (Da): 77427
|
A0A8C4UEV8 | YRHTRSKPPGLGAGGLTARTCPCFQNKPVAPALPFCRVYGREQLGTNLQLQARVTAGKRYSKARPCPGGAKAATARGAAAAATAPGGDPRPGPHAPRGSDAGAGQGAAPRLRGAKPRAGARGGEPPGGARGPAGAGQPALPGSPRTGSRSRRRRARAGAGAPQHPPAAPENGRRGRAGPSSPGGAAPGSRDRRPVPRGRNDSAVPARPPAPELPPPGPGEAAQRGRPPSAKPPRGRGAPPATRPAPAGVPALRCPRRRATAARSPGQRQSRRAAPHRPAAPRPHRPARRADPRSPYRARRRSSSPVPRPRWQPVPAQPEAATLQSREGSAHAPSRPAATAAHGLQLPACPARGAAPAGAVGAADASFACRGPAPGSRQRVAVALGSRVAAGVCWAVRRRGCPGQRGAVRACTSRHVPQQPPGPRPEESYPCAGPRGADISLADWGRKAIEIAENEMPGLMKMREMYAASKPLKGARIAGCLHMTVQTAVLIETLIELGAEVQWSSCNIFSTQDHAAAAIAKAGIPVFAWKGETDEEYLWCIEQTLYFKDGQPLNMILDDGGDLTNLVHTKYPQLLKGIRGISEETTTGVHNLYKMKANGTLKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEVTTMEEACKEGNIFVTTTGCTDIVQGRHFEQMKDDAIVCNIGHFDVEVDAKWLNENAVEAVNVKPQVDRYTLRNGRHIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVLAQIELWTHSDKYAVGVHFLPKKLDEAVAAAHLDKLCVKLTKLSDKQAKYLGLSRDGPFKPDHYRY | Cofactor: Binds 1 NAD(+) per subunit.
Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
EC: 3.13.2.1
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Length: 860
Sequence Mass (Da): 90923
|
A0A348MTW5 | MSSLDQKIIPCTTSHLAIPAYVDIQSLYERHVPRYTSYPTAVEFSDGDFNTPVLASLNTQHQPISLYIHIPFCQSLCNYCGCNKRITQDKSKADIYLDYLANEMRQISAVSPSLKVSHIHYGGGSPSFLTQAQHSRLYELINANFMLLEGAQQSIECDPRNLTPDYIQHLADLGFRRLSLGVQDVNARVQQTINRIQSTEHIEDCLASAYASGFTSINLDLIVGLPEQNTSTIEETLLAVQRFNCERISVFNYAHLPARFPSQRKFEKANMPTIAEKKAMTLQIAKGLSALGYQKIGLDHFAKHDDTLTKALEAGTLSRNFQGYTSDNNDQILGLGVSAISNIGNTRSQNNVDLAKYYEQITQSQLRHRGMSLSQDDLFRGQIISQLMCNFSVDLTHVAKPFHLNIDTYLHNELAQLQALSQLDVLTLEANKVSVNQDHRPLIRVIASVFDRYLQSHHSFSSVI | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet route): step 1/1.
Catalytic Activity: coproporphyrinogen III + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + 2 CO2 + 2 L-methionine + protoporphyrinogen IX
EC: 1.3.98.3
Subcellular Location: Cytoplasm
Sequence Length: 464
Sequence Mass (Da): 52099
|
A0A0S8IGA4 | MKILVINSGSSSIKYKLFQMPGDHLLQKGVIEHIGERGSKIRDHYAGLKMILEKLDTVDAVGHRVVHGAEKFSTHVLINQDVLKEIKRCCSIAPLHNPANLAGILACKKLLPAIRQVAVFDTAFHQTLPNYAYLYGLPYGFYKKQGIRKYGFHGTSHEYVARQASRLLKRPLRQLKIITCHLGNGCSIACVYQGKSADTSMGFTPLEGLIMGTRSGDIDPALITYLMRRMKLDIHGIDQILNKKSGLLGISGVSNDMRIVQRKALQGHRRCNLAINMFIYRIRKYIGAYIAVMGGLDALIFTAGIGENQARIRRKIVSGLFKCLKKKPKILVVPTDEELMIAHKAFELVRRR | Cofactor: Mg(2+). Can also accept Mn(2+).
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
EC: 2.7.2.1
Subcellular Location: Cytoplasm
Catalytic Activity: acetate + ATP = acetyl phosphate + ADP
Sequence Length: 352
Sequence Mass (Da): 39434
|
A0A956KG59 | MARLQDGSAGDDAPLARRGLALAALLLFACAQPSTEEPVKAKQEAPPPEEAPAPDPGGPPGPPLRADGTIFAGAEQMGTRVTIKVWVGDHSTRAAEIAIREAFAEIERIEEIASEWRPQSELSQFNAHAGREPIDMSADLFALLQRSKEIAAASGGTFDPTFHGVGQLWSFEPGAQPPPREAIAEKLKLVNWRAIELDPETHRGRLTNPGMKIGLGAIAKGYAVDRASELLRRRGFVHHIVEGGGDTYVS | Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
EC: 2.7.1.180
Subcellular Location: Cell inner membrane
Sequence Length: 250
Sequence Mass (Da): 26791
Location Topology: Lipid-anchor
|
A0A956GHL5 | MGPTELLIVLAIVVLLFGATRLPALGKALGDTMKAFRDSSKGDSGKDKIESDKKDVVRIEDAQVERDEPKKLEDKGSDKA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 80
Sequence Mass (Da): 8656
Location Topology: Single-pass membrane protein
|
A0A6B2M2K8 | MRIFKTLLFLQTLLIPVCVLFSAADKFEFESRDDVPASYKWDFTLFYPDWEAWESDLLRMEELYNEVATYEGRLGEGPATLLEVYQLSDEASKVSTRLWGFAGQRRDVDTRDNFVQGQVGKLLATYSRISASISWFTPEVLTIPQETMIEWIDATPGLEQYRFGLMDAYRTGRYTLNSEGERLLSLHGKVRRTAAQVFSSLTNADGDRPEVTLSDGTVITVTPGLYSKALTTYRNPEDRKAVQEAWMEQFEDRQNTFASIYEGVLNQGWALAEARGYASTIEMELDENNIPLEVVESLVEVARDGGEVLQRYHQLRQRLLGLEHYGWSDMFMPLVDDTTSYNYDEIVPLIVESVVPLGEEYSSKMAQQFSAGFVDVFETPGKRSGAYNAGRYGIGSFVLLNYRGTLDDVFTVAHEMGHSMHTRLSQEYQPYATHWYTIFVAEVASILNEKLLLRQFLETVDDPAQRIAFLESQLMKIKGTFFLQTMMADFELQAHAMAEKGEGITAESLTNLWKSIVKSHHGDIIPDDDPYMLSWSRIPHLYRTPFYVYQYATCYASAAYLMKQMETDPEGTVEKYLTLLKSGGNDYPMTQLRKAGIDLENADILKAVVDEFSQLVDLLESEYLRYLESEEIEKPA | Cofactor: Binds 1 zinc ion.
Function: Has oligopeptidase activity and degrades a variety of small bioactive peptides.
EC: 3.4.24.-
Sequence Length: 636
Sequence Mass (Da): 72642
|
A0A7X7GYJ2 | MNHHLELRPPTSTEGPALWQLVRATGVLEPNSAYAYALLCRDFSETCLVAEVKEDGIEGDLVAFVTAYRPPARPEAVFVWQIGVHPRAQGQGLGRRLLLELLRRPAAADATHLEATVGVSNTASARLFQSVARELGAPCEILPWFTERHFPSPEGRAPPHEDEPLYRIGPLRRRNA | Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 2/3.
Function: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A.
EC: 2.3.1.178
Catalytic Activity: acetyl-CoA + L-2,4-diaminobutanoate = (2S)-4-acetamido-2-aminobutanoate + CoA + H(+)
Sequence Length: 176
Sequence Mass (Da): 19491
|
A0A7Z9LRY5 | MKAKTQLIIVAGGLGTRLKHSEPKALVPLVDSPLLIHTLNAFQNLDLTKDAIIVYPGGHESAFAGVLNTDFPDGNLTLVAGGKERYDSVALGLKKLSPDTEIVLIHDAARPFVQEQTVRDVLDAAIQFGAATIAMRCKDTILQANADGFLEDTPDRSRLWACQTPQVFRREIIEKAYASPKPTTITDDATLVRQSGVPVHIVESSHTNLKITTPNDLQYAEFLITKGLV | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Length: 229
Sequence Mass (Da): 24909
|
A0A936D8F2 | MTIGVGLLGCGTVGSGVVKLLRQRQAEIEARVGDRVEIVAVAVRDLAKARVSELGSVRLTASPAEVVHEPRVNVVVELMGGLEPAKTHVLDALSRKKAVVTANKALLAYHGPEIFRAAREARVDVAFEGAVGGGVPVVRALRDALAGDRVRRIVGILNGTSNYVLTRMQREGLGFDEVVRDAQRLGYAEADPSLDVDGHDAAHKLVVLSALAFGRRVRPEEVDTRGLRSLEPVDHACADRFGFVVKPLAVAEDTGLSDPERGPCLALRVGPALVSKDALLGSVSGVLNAVLLEGDALGPLVLSGRGAGEGPTAVSVVSDVLDVARAIHEGSTGMLTAALRTEPSWVRAAGEDVLPHYARFVVRDEPGVLGRITTSLGRAGVSIRELVQLRRGDTNADVIMLTHASSRAAFEAALAEVDVAPFAVEKTRLFPVVAA | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 435
Sequence Mass (Da): 45738
|
A0A2F0AR84 | MSVSSVVAVAMGGALGCVCRFGIASLFSAGLQFPIGTFSANMIGCFVIGLAYVFFSHHVDLPDALRLSILVGFLGGFTTFSSFGLESVQLIESGRVRLAITYVLTSNLIGLALVYAGTRLGRLYLNAA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 128
Sequence Mass (Da): 13405
Location Topology: Multi-pass membrane protein
|
A0A9D7D2L5 | MTRRSSRKTVTSSFKSRAASPRAPWPDEASRSWVAPTPAASSNTTSCSASTGPTAWAATWPSWASNKRSWRRPRAASSTPKARTKTAGIATGASTSRWRRAPKRRRRRATRRATSSPRPRAEPRLDGAATARQTTGAAGRFPRPLLCTGRGRPVTSRFEPKPPWLKVRAPGGESYAHLKDTFRALDLHTVCEEARCPNIGECWTEGTATVMLLGDVCTRGCRFCAVTSGDPRGAVDVREPEHVARALSRMELQYVVLTMVDRDDLLDGGASHVARTVTRLKELRPDMLVETLLGDFGGHLDYVDTTVDARPDVWAHNIEVTERLQRKIRDARCSYAQSLGVLARVKARDPKRVTKSSIMVGIGETDAEVEQTLRDLRSAGVDIVTLGQYLRPTPKHAPVDRFVTPEAFARFAELARGRGFLYAASGPLVRSSYKAAEVFVRSFLVPGDETAAKAHMDERLADARRAASAQGEAPNGAPRSTSELAARAAAALLMPASQLVRR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
EC: 2.8.1.8
Subcellular Location: Cytoplasm
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Length: 502
Sequence Mass (Da): 54831
|
A0A2F0ASC1 | MKKLVVATGNAHKLDEYRALLPGIQLASMSEFPPMEPVEEDAPDFIGNAILKALAVHSHTGLAALADDSGLEVEALNQRPGVFSARYAAGTDRDRYLKLLGEMENQPNRLARFACAIAIAGLPEKNSDDSIIYRDGCWVSVGYCYGQITEEPNGTNGFGYDPIFSVNDGRTMAQLTAAEKHAISHRGQATKPIINVLRSLMGVYSGSI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
EC: 3.6.1.66
Catalytic Activity: H2O + ITP = diphosphate + H(+) + IMP
Sequence Length: 208
Sequence Mass (Da): 22469
|
A0A8B9LWY9 | MTDPSALFEMETDLTNFNLPINHNNFPAKLWCLANSPNTLSIRWDPSGKTVIIDQPLFEAEFLSPEPKTRSASLEFFKTTNFTSFVRQLNLYGFRKVAVDADSLEKYCKPASDCAQHHFHNPNFKQGHPELLANLKRLTSANKAKMEAGLKVSCRPPAQAHRLMLNADEDTSIKGSVSKRQPSQRRVKGAPSPYHPSGSQQLKPCDRTPVPPRTWTMGHGNVSSPTHIYTDKGVPLSMIYNMPIDLPYTVQPNSTIVQHGSQSAAAVGHKIGPFFYHHPQYWPGFYTEVLPCSSPSSFQVPDMAVSHHPAAPYFHYSYYPTYTLGYFHPSDHNPDCWSGGSGDSRTSDVNLDTVFKIVDELQSPHKLNSVHVSSPDQCPSTSTAEKSPAGFSQPKTVRASLIASFKKSHPLSLCNTSEDERQDSLFISIVKLESPESKVPQCQPLLDKARLALQRGAQAVIFDISDDASAANELRDSGSLLRPVVLVKATDAEELMLLVNKNEEAMVEINIKVETQTWV | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 519
Sequence Mass (Da): 57589
|
A0A7X7CAC8 | MEKFHPIKIGTLSLKNNLIAAPMAGLSALPYRVLAMEMGCALAMSEMVSAEGTIRAGEKTKRYFKNDESVRPFGLQVFGANPESIGKSIEMLSSEPVDLFDINMGCPVHKVCKKGAGAALMKNPELVSKIVAAARKATEKPLTIKIRAGWNSKSINCIEIAKIAESCGADAVAIHARTREQEFSGKADWSHIAAVKSALKIPVIGNGDIKSRHDALEMIEQTRCDAIMIGRAAIGNPWIFRAILDSDFSEPGRKERLLTATRHLEMLREFLGEHSAALAMRSIISWYTKGIPGVKEFMRNIQRSKGTAEMKSLIDQFAANI | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
EC: 1.3.1.-
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Length: 321
Sequence Mass (Da): 35112
|
A0A7S3M320 | MNLANLTAGIESLTKQAQEFAIGATAGAPHMDLNSLISSQPRGLYNFISDIRNAKSKEDERSRVDKELANIRQKFANSSSLSSRDKKKYVWKMCYMYMLGYDIDFGHLEFISLLSSTKFQEKSVGYMAFSLMLRPGDELMTLVVNSMRNDLIGQLIWGQTLALAAVSNIGGNDLAEALAGDVQRLILGTMETKAYNNVAVSAEEEIRNKSLICKKACLCLLRFYRTNPDCLVLEDWMKRLGKLLEDRDLGVVTSVMSLMLGLVSSNPPYFEPLVPYVISILNRLVISRSCSADYLYYRTPSPWLQVKCLRLLQYYKMPNDNELLNEILGNILIRTEVSESLNKSNADHSILFEAINLVIFYGADAASYLKDQVCSLLGRFIAVKDPNIRYLGLDAMTRMAKLDGSEAVQMHQSTVLESLKDTDISVRKRALNLVYVLTDRSNAQVIVADLLAHLPEADSAMKEDIVVKIAILAEKFATDLRWYVNTMVQVILVAGDFVAEAVWYRVVQIVINNASIHEYAAEKMLLTVESKYAHDNIVAVAAYLLGEIGVNICEHTGMSGYDQFVALHQHMPTASLKVQAILLTTYMKLLNLYPDQVSEQINEVFAKYSTSCYLELQQRACEYKALPSIAADTMEAVLNPMPPFEMEGRESSLLSLAAGSSHNSGANADKVASNTERPEGEKAGRNNANEASPVMKPKPAAAKEAVVDLLSMDDDSSVNSSPPGSAGGNRHRTASGGSASAAGLSGEVLAEVPKWLRNATLVRVPTAKSVLLKTDLLTITVSADFRAHQARMAVFFENTSRFDIQNLKVTVTTVATSAGGINVKQQDPSVRISPGEETKLQLALESARPFPDAYPLEMEVHFTISGSAYSYPLLLPVTAASFFEALPCDKATYMARWKSLDGTDAEAQQVFACGRPVDAALMTQLRNVLVPAMKLGLAEGLDNERTITGTASFLTGTAGPDGKPISVGVMMRLEADPAQGKFRITARAKNALVAQGLKNFLVHQLS | Function: Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration.
Subcellular Location: Membrane
Sequence Length: 1006
Sequence Mass (Da): 110295
Location Topology: Peripheral membrane protein
|
A0A9E5VLD6 | HRELMSTWISKLGAFFSMGAYRRLKRETDPNMYSGAPLLGVKGVVIILHGSCSSLGVKNSLLGARRAVRSRINEHIRHGIERLRNTEAHLNAQEANP | Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
EC: 2.3.1.274
Subcellular Location: Cytoplasm
Sequence Length: 97
Sequence Mass (Da): 10820
|
A0A2J0MGC3 | MIMAGLTGGFSAGKTAVLAMFKRSGAKILNSDSVARQVLLQDKRVIKKIREAFGEGVFRKGRIDRKLLAKKVFNNKRYLEKLNSLVHPAVKRKVFEMRRHLKARRGRTIMVVEVPLLFESGFDRFFDVTIGVAVGLKGQRERLLKNSRFSAKDIKARMSAQLPSEEKVRRCDFVIDNNGTKKKTLEQVRRLMELFKGGNAQWKN | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Length: 204
Sequence Mass (Da): 23324
|
A0A7X7Z4J5 | MNRSESPTVLVAMSGGVDSTVAAALLREQGYHVVGATLRLHDLTPPGAAAACGDPSGVAAAEQAAKFLGIEHRVIDGRDRFREAVLKASWDDYANGRTPNPCTWCNRELKFGFLWETARDLGAAMIATGHYARLVPGEGAVELYRGRDPQKDQSYFLFALTAEQRARSLLPLGEYTKPEVRELARRLGVANAERTESQDACFASGDEIFAEDLRRFFQAPGRAGTIVDESRRILGRHEGLHRFTIGQRQGLGVALGKRAWVERIDAADATVVVTTDPERLRASGLVAAPVCWSREPWVGPCEVQIRYRHKASPARIEMADAATAVVRFNQPLRAVTPGQAAVFYDGDRVIGGGWIREALVGAE | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
EC: 2.8.1.13
Subcellular Location: Cytoplasm
Sequence Length: 363
Sequence Mass (Da): 39579
|
A0A3B8LGL4 | MTASSPFNATTKLCMIVGSPVSHSLSPVMHNTAYRALGIEDKYVYLASEVAKGDLERVVAGVRSMGIRGLTCTIPHKQDILPFLDDIEPMAQRLGAVNTVVQSEDGQLTGYNTDWLGIIRPLLRTLNASQDDDAALAGNNIAILGAGGTARAAAWGVQSLGGTPSLFNRTLEKAEQLAQEVGCAAYSLQAHDMIHDADIIINTTSVGMPPMHDASPLPSDCLRPTQIIMDAIYTPFETVLLRQAKDKGARLIRGAQMFLEQGVEQFSLYTERDAPRDVMADVICQHFGVSSL | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 292
Sequence Mass (Da): 31456
|
A0A3B8LBJ5 | MTQQLIPPTRPLEAGLYLVATPIGHLEDITLRALRILRDVDQIAAEDTRTARKLLNAYDLQKPTFSLYRDNEAQRVPRLIEHLQEGQSVALISEAGMPGISDPGYVAVQHVLEAGFPVIPIPGANAVTTALLPSGLPCDRFMFLGFLPPKSGKRRQHLAPYLHVPSTLVLYASPHKLPSLLEDLENILGDRRACIARELTKSHEEFCRGTLSELAAQFADESRRKGEFVLLIEGHQGPVETVLESEQQETEEARIKARIRTLLKEGVRPSKLARKLTAEFPSLSRKRAYQQILALEKHDEDGQKESEES | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.198
Subcellular Location: Cytoplasm
Sequence Length: 309
Sequence Mass (Da): 34500
|
A0A1H1YS61 | MTTSPSQLSLAAPPTSPQLSAPPSPLSRTEERNPRSAGIDRMSTLELLHLINSEDRHVPEAVAQVLPQLAAAVELAVTALSGGNRVHYVGAGTSGRIAVLDAAELIPTFGLEPDRVIAHIAGGPPALTRPSEAAEDDETAGSAVVTAVEAGDVVVGVTASGRTPYVHAALTTARTLGAHTVLISANPASPISAAADVHIAPDTGPEVLTGSTRMKAGTAQKLILNAFSTATMVRLGRTYSNLMTDMLATNAKLKDRRLRILAEATGADLTECGHALRSADGNAKVALLTLLAGSSPDTAARALAVTEGHVTRALRLLAVNGT | Pathway: Amino-sugar metabolism; N-acetylmuramate degradation.
Function: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate.
EC: 4.2.1.126
Catalytic Activity: H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate
Sequence Length: 322
Sequence Mass (Da): 32959
|
A0A956I7A8 | MSRQDRKKKQKKAAKEQAREALRAAVPHAQRPWRSPVPLEPIDEVRWRIPKQGAMRTHGVVYADTTLLPDLQADASLEQVANVATLPGIVGPSMAMPDIHWGYGFPIGGVAAFDLDEGVVSPGGVGYDINCGVRLLASDVDVEGARLVSTSKGLERTRKLVDELFDAIPSGVGERSDERIGGDVLRGLLEGGLPFARTLGWATDEDVAHVEERGVLPGADADAITSRARMRGGPQLGTLGSGNHFAEIGVVDQVYDAPAAEAFGLRLGQITLMIHSGSRGLGHQVCVDAISEMLRAAAKYDIPLVDRQLCCAPVKSEEGRHYLAAMAAAANFA | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.8
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 333
Sequence Mass (Da): 35512
|
A0A1Z8KVD4 | MNVLGIDPGLVNTGYGIISSINNNFELIDYGVIKTNSKDKLSNRLKIIFNEVSQLINKYNPKVLSIEEIFYSKNVKSSLLLGHARGVAMAAASVNEMLVYEFAARKVKQSLTGNGNAHKDQVRFMVKNLLKMNEAPKSEDASDALGIALCYMFQNKLEHL | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
EC: 3.1.21.10
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Subcellular Location: Cytoplasm
Sequence Length: 160
Sequence Mass (Da): 17769
|
A0A2E8RUV7 | MAPTFSSTSSADSSASSLHGKTVLLGVSAGIAAYKACELARLLVKAGADVHVQMTEGATQFVQPLTFAALTSNPVGTRIFDADTEAAMPHTELGMKADLIILAPATADVIARIAAGMANDLLTTTMLVATCPVLVCPAMNRDMWSNEIVQRNISTLDEFERYTILPPDSGELACGVTGPGRLPEPENIARIAASLTQEQSLIGRRVLISGGPTREYIDPVRFLSNPATGSLAIALASCAQARGAETTLVLGPTHLKPPPGVELIRVTSAQEMCDAIMARVSDVDVLCMSAAVADYQPLSMADAKHKKTADDTSLRLTRTPDILEAVNQAQSKPIVLGFAAETETNLEALKTAGRNKMLKKNCNLLFVNHVYTDQRGFGPGDTEGILLGPGEFDLHISPQAKSSVARILCDALEQELSQSALRDKEVS | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
Function: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.
Catalytic Activity: (R)-4'-phosphopantothenate + CTP + L-cysteine = CMP + diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine
Sequence Length: 427
Sequence Mass (Da): 45224
|
A0A2E8S182 | MANALGRHLLCEFYDCSTTVLNDAAKVQHYMHRAAECMGATIVEEVFHEFSPYGVSGVVVIAESHIAIHTWPEHGYAAVDIFTCGAEMEPRRGIELLVEFFSAGNHSVREIARGVLESQNPPKAIGDGEAWR | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
EC: 4.1.1.50
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Length: 132
Sequence Mass (Da): 14543
|
A0A7C1GTS9 | MFRPGHGDFTFYKKYGWRDHRGGGRQSGRETATRVAAGAFARKLLENLGIRIVAHAVEIAGIQARKCDYDVIEENPVRCADPDIAPMMEEAILNARACKDSVGGVIQLEVTGLPPGLGDPVFGKLDARLCSAIMTIGAVKGVEVGDGFAITRLTGSQANDCMADGAFLSNHHGGILGGISSGAPIIMRIAVKPTASITTVQQTCTVAGENCTVEVRGRHDPCIVVRAVPVVENMAAFVLLDAFEVQAKLNPAWAESVGYGV | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 261
Sequence Mass (Da): 27590
|
A0A7C1GLI2 | MFELIRQNKRRSLLLMGFMLLLLLGVGFAIGFAVVPASEPLDMGGATLYLPWGGLLGMGVAFLVWGVQALAAYSSGDRLLMAAAGAKKIQKQDHPRLFNVVEEMSIAAQLPKPPKVYIIEDMSLNAFAAGRDPNHAAVAVTAGLLSKLNRDQLQGVVAHEIAHIANRDVLFMTMAGIMVGSIIMLTEVFFRVMWYSNIGASRRYRSRRSSRDGEGAAKLILLVVALILAIVAPLLAQLLYFACSRQREYLADAGGAVYTRYPEGLASALETISGNPGDKKSVSKAMAPMYIVNPLEAGQRAISSLTSTHPPIEERVRILRSMGGGGSFADYAAAWNKVDGAGAARIPASALAQTAPVAARAANAQEPMAAITAAAAAPVGQASKTGVPTPSRRATPEATPRQRQRDTGDLLRRMNKFRFINCDCGIRIKLPPEYAKPKVKCVRCGKIHEVPRQP | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 454
Sequence Mass (Da): 48760
Location Topology: Multi-pass membrane protein
|
A0A7Y5GYX8 | MKTAYETIIGLEVHAQLKTQSKVFSMCPAKANELPNTLTDVVTLGLPGVLPVLNAQAVRFAVMMGLATHCSIRKVSRFARKHYFYPDLPKGYQISQYDEPLCEHGWIDIDLESGETKRVGITRIHMEEDAGKTIHDADRNESRVDFNRAGVPLIEIVSGPDMRSPDEAVAYLKVLHNILRYLDICDGNMEEGNFRCDANISLRLHGQERFGTKVEIKNINSFRYVHKALVYEQQRQAQFLDDGKTIVQETRLWNSEVNRTESMRSKEDAHDYRYFPDPDLLPLVLTDETLQAIASELPELPDDKRRRFVRDFHLSEYDSAVLTSTPELSRYYDAVLASWGADPKLAANWVSTELLGALAKDGKPIEKTPVSPENLARILHHLSSGSISGKMAKEVFEKVYNEGADPDSVVSTMGGQVSDPEALLAILRDIIANNPAQVEKYRAGKTQLLGFFVGQVMQRTKGKANPTLTNELAIAELNR | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate
Sequence Length: 479
Sequence Mass (Da): 53759
|
A8IXY0 | MRAVIQRVKSASVTVDGEVVSSIGPGLMVLVGIRESDMEKDLSWIVKKILSVKAWPHPETQKAWDVSVTGAGLEILLVSQFTLYARLKKPKPDYSKAMGPTQAKDLYSQLVEEVRRQYGAPERVKDGVFGAKMDVALVNDGPVTYIVDSNDPDA | Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
EC: 3.1.1.96
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 16888
|
A0A517M8U9 | MNDPNHPTSPWTPAGAVRQLRDKIQRTSSERIRLDQATGRILSTSLTADRDSPAADVSAMDGYALRMQDLANPGSLDVCGESRPGHAPPSGSSQGIVRIFTGAIVPSEFDCVIRREETKESATSITLRDSARRAKHGDNIRRQAENISSGEVVLEAGTLLNAAAIAAAANFGASQIEVQKQVRVSVIVTGDELQPVGQSVTPWQLRDSNGPTLQAMLIHRPDVHLHPVQRVIDSLPNIQTKLNQALAISDVVVFTGGVSMGDYDHVPAAVLACGGELVFHRVPLRPGKPILAAVTKQGQLILGLPGNPVSAAVGARRFLLPLLACFQGAVERHPPAIPLVDPPSKTLPLWWLRLVKIDSQGNANIVPGKGSGDLVALAASDGFIEQPPEASGPGPWTYWEW | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 401
Sequence Mass (Da): 42756
|
A0A956PA84 | MKYVVLLCDGAADEPIASLGGKTPLEYAKTPNMDRLATLGRLGRMETTAPGLHAGSDTNNLNVMGFNPNAVYTGRSPLEAASIGVEMADGDVSFRCNLVTLEGDGDRAVMADYSGHDIKTEHGRIIMKALDARLGSEDFTFYPGVSYRNLLLWRGGASKMRGIRTTAPHDISDREIGDYLPTGPGSDALRHFMKESRKIIAELVASEIPDCKATSAWFWGEGTRPNMPAFRDRTGLKGAVVSAVDLVKGIGRFAGMDVIEVPGATGWIDTNYEGKAAAGIHALEDHDYVFLHVEATDEAGHKGSAEQKVLACEYFDRRIVAPVLEALERRGDYRVLLTCDHPTPVATKTHTKDAVPFVYFDSSHPRAAGPRGFSEREAMESGVYYDNCRTLVGEFLGKALD | Pathway: Carbohydrate degradation.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 401
Sequence Mass (Da): 43579
|
Q11FC3 | MSLEAFYAVSALIVLLLTGIPIALALTLAGAFGLWLLDFPMLVVIQRFAAGSESFVLLAIPFFILAGAVMEAGGISRRLIGFCDACLGYLPGGLANANIGASMVFGGISGSAVADTSAVGSVMIPAMEREGYSRRYSAAVTAAASPVGMIIPPSIPMIVWSYISGQSLNELFMAGIVPGILITLALALVSTWICQRRGFQRGFRPFRAGFFLSSLKDGLLALGAPVIIIGGILIGAFTPTEASVVALAYALILSFGVYRELSPRKLAAVFVQAGKTSASIMFIICGATVFSFFLTVSGMPAQIGSLILSVSETPLGFIIAAGLLMFVLGMFLDTTTTILMAGPIIIPLFSQVGVDPLVATMVIMVILAIGLITPPVGLCLFVVSSITPVKVWDVARECVPFILAMTAVAALIWIFPPLVTWVVP | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 424
Sequence Mass (Da): 44325
Location Topology: Multi-pass membrane protein
|
A0A2M6X9B9 | MIFSPILGIFYPFMQDTEEIKSRLNVADVLAEYIQLTPSGANFKAKCPFHNEKTPSFYVSPEKQIWHCFGCNLGGDIFTFVQKMEGIEFREALKILADKAGVRLAARNPDQEAKRNRLVGLCDWASRFYHQALLRSREGKIARDYLASRQINSETIENFLLGYSPDSWNLTLNFLRKKGFSEAEIFDAGLTSQKTPGRFYDRFRGRLMFPLRNVHGQTIGFGARVLNEKKDFLGKYINSPQTLVYDKSNFLYALDQAKTKIKEEKLSVAVEGYLDVISSHQAGIANVVGVSGTALTPGQLNLIKRYATNLALCFDADEAGFSAGRRGLENAIAAGIAVRMVILPKGEDPDSLIRKDKKAWSEAIAKAAGVLEFYFDLACKTHDPGRLEDKKMIAAELLPLIQKIPDQIEQAYYLQKLSSLIDIPEASLREAMQGLGAENSPDRETQGAPDVSSPPAPPAEILGRRLLGLGLKYPKNLAIILKKLPLPLFSQELQDIYNFLQKYYNLKRGFDLSRFIRKIKAVYPHYATPIEVAILDVEKDFEEKPEDEAIAKEVRAVLKRLREEHYHSELANIEREMQKAEKAGQKDILQSLTQKLQSLTQNRL | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 604
Domain: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Sequence Mass (Da): 68132
|
A0A955YIT3 | MGKLIVLAACVVGTVAVGRLIERHVRTSPAFAIRSITFSGHEQLEEAELLRTSGLAIGQNVFDLAPEDVRDRLGRHPWIASVEVQRRLPGTFTIDVRERRAVAILALEQLYLVGEDGTVFKQLGEEDLVDLPVIVGIPRERFVRDRAYRASVLLEIVALMHDYRGVGLWRREPIAEVHVEADDSLSLYVGEDATYVRLGRGPFRDKLQKIRRVFDALDARETRAAYIYADNVRRPDRVTVRLREERALVASQGAN | Function: Essential cell division protein.
Subcellular Location: Cell membrane
Sequence Length: 255
Sequence Mass (Da): 28762
Location Topology: Single-pass type II membrane protein
|
A0A955UWL6 | MEPRRRAKILATIGPATRSESAIRDMIAAGADAFRLNASHGEPDAWREEARMVRAVAAEAGRPIAIVFDVCGPKLRLGAHVPSLGFEAGDPARFASEGTAADALPVAWPGFAALVTPRRSEIVIGDGTPRFAVLGVDGDAVEARCLRGGQIGPRKGVFVTFAGTTGRALTEKDLADLDVAAEIGADFVALSFVRSAADVQLLRDELAARGSRARVIAKIEKLEAVENLAEIVAAADGVMVARGDLGVEAGVHEVPLLQKRIIRRATTAGKLVVTATQMLESMLTAAEPTRAEASDVANAVLDGTSALMLSGETAVGEHPVQAVQAMAAIAGRAQEALSYALDIPTVEQDNAEAVLRSAAHLAQQIDAAALVIPTTTGGSVRAAAKCRTPRPIIALARDDVVARQLALEWAVIPGTLPAHSGRIEELIDEAVGVARTIGGLDDGAHVVVTYGQSGRVSGGTDLIVVRQVGAEKPSGFVSDPAQMREA | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 486
Sequence Mass (Da): 50446
|
A0A1Q3PYQ2 | MYIAITVLIIIVCVFLSLVVLIQNPKGGGLTSTFGGVGQQILGARRSTDMVEKATWTFAILLLVLSVGSAFFIDKRADVKTKTQIEKSEVEQQMNNQPFNPASLPQAAPAGGNTAPAQTAPAESAPAQPAQ | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 131
Sequence Mass (Da): 13783
Location Topology: Multi-pass membrane protein
|
A0A2E5HHT9 | MALPAPPGDDGPGALRRFVLPMIFVAALFVALFMRRPDGDANNEAWTFSGPTMGTTYNVKVLPGDAGGDREAAEAAIQAALANVNARMSTYQADSELSRFNANPSTDPVPISAELATVTAEALRVGALSGGAFDVTVGPLVNAWGFGPNSRGEPPSEEKLAELKAIVGADKLTLDPKAPSLTKAHPGVYVDLSAIAKGYGVDQVARALDSLGHKDYMVEVGGEVRARGESPRGGAWRIGIEKPDENARAIHEVVMLADTSLATSGNYRNFYEDERGQRVSHTINPVTGRPVTHRLASVSVLHKDCMTADGLATALNVLGEEAGYELALKQELTALFIIKDPTGRFIEKATPAFEALRPDKKDAGATSAP | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 369
Sequence Mass (Da): 38960
|
A0A956CML4 | MSGGARISLDEVRHVARLARIALSEDEVVRLQRELDPVLDYVAALSAVDVDGVPPTMHVQDMPAELRADAVEPMLDRDVALAQAPSPEDGAFAVPKVLEVGG | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate
Sequence Length: 102
Sequence Mass (Da): 10868
|
A0A956AWH4 | MTLRRMRAADAEAVVALTHATLDAHYSAESLRVELSEPNAHQWVLCEGDQLVAWLDFRVVLDEVELIEIAVAAARRRQGHGRRLMDHLIGQGRDLGAAVIHLEVRADNAAARALYEAFGFGATGLRRRYYRDGADAVLYQLLLARHGA | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 148
Sequence Mass (Da): 16442
|
A0A7C1CIZ6 | MEKHDTVADCIARMSARLAPITDTPRLEAEMLLAHALGVSRASLLARLREPVDARAAARLLARRLDHEPLAYIFGEWEFFGLSFLVPPPLLTPRPETEHLVEAALKYLAVGRAASPDCPRVADLCCGVGCVAVSIGKHRADASLCACDVRADAVETTLRNAARHRVRIHCVQGDLFAPLDNVCDCFDVVVSNPPYVPAGEWQDLAPVITKHEDPGALLAGKDGLEVIRRIIPAAFSRLRIGGMLAMELGDGQFPAAAALMRKQGFAQVAAVRDLSGTD | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Length: 278
Sequence Mass (Da): 29942
|
A0A7C1CNN5 | MAHKGIYARTGRTMSRAQSDDALLTQMARTITRHKLFAAGERVLAAVSGGVDSMVMLHALRKLGCPVEAAHFDHQTRHGASAEDAAFVRETCRRLGIPCHEGSESVEADAAGRSFEAYARERRYAFLLSAAKQAACAVIATAHQEDDQAETVLMGALGMTSGVGATGIAPCVERDGIRIVRPMLDCARADMEAWARRNGVAWRDDHTNREPHCTRNRVRMELLPLLETHNPRARHALARLADISRADSEYLDGVAAASLDKCVAEQGAFVVFDRHLFRNFHKAIQRRMVKLLARRMGTEIAYERVVAATQFIAEAETGRRFDCGGGTTLYITGEEAQIHPRGSGPQEEPPAPAPLNVPGETRVSGYVFRTRMLRRNALPEREIRDLCAPGRQYFDADKLPGRLHLRARKPGDRMTPFGMKQSRKLQDIMVDCRIPAHLREAVPILLHEQEILWLPGYRRSDSAPVDDTTTTVLEIAFHRPTRSANRGKHAE | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 491
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 54571
|
A0A7C1CMV1 | MSLVVGIETSCDETGVAVLRNGEQVLSNVVSSQIDVHRVFGGVVPEIASRMHTEIISQLMEQALNEAGLSCKNGRPPVNAVAATFGPGLMGSLLVGLSFGRAVACAWKIPFVPVHHIEGHLFSAFLGENRPEFPYLALVVSGGHTQIVQCAAPHQYRILATTRDDAVGECFDKVARLLGLPYPGGPSIQKAAETGDDGAFDFPRGLVAKDTLDFSYSGLKTAVLYMLRERPDAAVPDVAASFQRAAVDALIQKTDRAVKQSGIHRLVIAGGVAANKRLRESAAQLDVELFLPPFAYCLDNGAMIAAAAHSRLQHGCPLPGDTPAAASISLVSKP | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
EC: 2.3.1.234
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Subcellular Location: Cytoplasm
Sequence Length: 334
Sequence Mass (Da): 35301
|
A0A7X7GUQ8 | MDDSRARAGAPENQAWQRAGSPSPRRRRGALEGSLPLGTWWGIPISAAWSVLIIFGLVAGQLGMVALPIWHPEWSAATTWMVALGAAVLFFVSILLHEMSHSVVARARGMKVEGITLFVFGGVSRIEGEAPSPKTEFLVAIVGPLMSLLIAVAGLVGASLLGANELANVSEENLGEALASLSPGATMLLWLGTMNLVLAMFNMVPGFPLDGGRVLRSLLWWMTGSLDKATRWASRVGQGVGFLLIAWGVGVLLQGALLGGMWRILIGWFLNNAAKASYRQMRVSQALHDVSVARLMQREPPTIAPDATVGDLVQLALRVEQRAIPVVEDHELRGLITLEQVQRLPEGQWDTTPVRQLMTPAAQLPNVPEEMPAQEAMQLLSEAEQLPVLKGHELVGILRRRDVLQWLSLHLPGMAPPPAPGTSPPSSRI | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 429
Sequence Mass (Da): 46274
Location Topology: Multi-pass membrane protein
|
A0A7C1GT47 | MKRIFFIAGESSGDMHGANLIRALRACAPDIHCEGLGGARMADAGMELFYDLAGDGIMGFVEVLKKALPIRRLFLDTLERLRRNPPDCLVLIDYPGFNIRVAKAAHALGIPVVYYISPQVWAWKKKRMDTLARVVRKMLVIFPFEEELYRDKGVDCVYVGHPLADQIAQYAPAAAGDVSGTQGQTRLTPVGRSLGSAAAGDVSGTQGQTRLT | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Length: 212
Sequence Mass (Da): 23121
|
A0A7C1CMQ0 | RLLAEYKSLENLYDHIGEIKGKLREYLEQDREQAFFSRELVTIKTDVPLDISPEQCVRKPWDAKQLQQCFEELAFHSLLKEMLPESAPKKMEGAYTLVDSLEKLESVIKEMESAKMIAVDTETTDVHPMFARLVGVSLCAHPGVAYYVPVEHAPLDLEEMMSADGGGGHDLSIDGKRAVELLKPLLEDASIGKIGHNIKYDIIVLQRAGIRVRGVVMDSMVASYLTDASRLRHNLDDLSLHYFNHKKIPISDLIGSGAKSITFDYVPVEKATAYACEDADMTFRLAAALRPLLEKDGLDALFNTIELPLVHVLADMEMQGIAIDTEQFASLQAEIVENLKKLESRIHKLAGETFNINSPKQLQVVLFEKLGLTPVRKTKSGYSTDVDVLEALAPEHPLPEAVLEYRTLEKLRGTYVEALPKLVHPETKRIHTSFNQAVTATGRLSSSSPNLQNIPVRTEYGRRIRQGFVAGAPSLRLVAADYSQIELRILAHLSKDDRLLEAFNADEDIHRDTAARVFGMKPEEVTPDMRRQAKAVNFGVVYGISDFGLARNLGIARGEARKFIDNYFETYPGVARWLEKTKEEAKRDGYVTTMFQRRRYINDIKSRNTVSRNAAERMAINTPVQGSAADIIKIAMVRLYEALKNMEKTHLLLQVHDELVVETPAEHADATAATMKDIMEGVVELAVPLKVDIGVGSHWAEIH | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 703
Sequence Mass (Da): 78733
|
A0A956G6Z2 | MAKSTVPERSTIPEERRWNTRHLFKNDKAWHAEREALAASFSTLAALRGTLGNGAEAVLTCLQTLFEANRRLGRLESYAARRNDEDTRVTTYQAMREVIDKVGADLRATSAFIEPQLLALPTKTIRDYIADPRFADYDRYLRELLRQKKHVLSPKEEALLARTSLMQDAGHNTYSAFTGADLTFPRITDEKGREVQLSQALFARYRASADRAVRKRTFDAFFSTFAGFKNTFASLLGAQVNANLIYARARRYDSALEAALDPDEIPVDVYTNMISAVNKHLPKLHRYLALRRDLLGLDSLRYYDLYPPIVEKVRLKFPYDKGCRTLVEAMAPLGSDYARALERGLQPKSGWIDALPNKGKRSGAYMDGSAYDVHPYVLGNYLEDFNSLSMMAHEMGHAMHSYYSNQQQPYPKADYSIFVAEVASTLNEHLLAEHLLAELKGKRRLFLLGEQLEGFRQTFFRQAMFAEFELDVYRLAEAGEAITADALSERYLAVARRYYGHDEGVVTVDDAYGMEWAYIPHFYYNFYVFQYVTGITAATALAEGILAHGAPARDRYIENLLYAGCRAAPIDILAAAGVDLTTTAPYDVAMSVFERTLDQAEAVTAGARGGHAVAS | Cofactor: Binds 1 zinc ion.
Function: Has oligopeptidase activity and degrades a variety of small bioactive peptides.
EC: 3.4.24.-
Sequence Length: 615
Sequence Mass (Da): 69162
|
A0A7C1GXV3 | IRLLAEYLESKGLDVVVTREPGGTPLAERIRDLLLNRGEETVTPLTELLLYEAARAQHVHSVVLPALARDKVVLCDRYADSTSAYQGAGRRLAGDFITLLNRLAAGAAWPNRTFILDMPAEEGLRRARERGSDDRMMAEGLAFHKRIREEFLALARREPDRITVIDATGSVAEIQNGLRSHVDRLPEIAKAGKSGARRKDPAAP | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 204
Sequence Mass (Da): 22528
|
A0A955X333 | MIAVQVTLAALGFDAAEEAALQALSDPALYPARVSSIHKGGFEILSARGTEQARLFGTLKHRFRQDPAARPAVGDWVAVRPQGEATPGIAAVLPRRSAFIRRAAGRRAEPQVVVTNVDTVFLVVGLDVDVSVRRAERYLATIWESGAQPVLVLNKGDLVAKLGAEGEAHLADVRAELAAVASEVPTLVTSGKAPADAAALLRPYLAPGRTVALVGSSGVGKSTLANALLGAPLLATRKVRERDGRGQHTTTRRALFPIPDLEGRPFGLGMLIDTPGMRELALWNVEEGLSELFADIIALADTCRFTDCAHRLEPGCAVREAILQEELDPDRLESYCKLAAEQATQEERARRR | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
EC: 3.6.1.-
Subcellular Location: Cytoplasm
Sequence Length: 352
Sequence Mass (Da): 37682
|
A0A1Z8KTW5 | MNVAVILAAGNSSRFGNKTPKQFQKFKNKMVFEYSLNTFLKHPEIDEVLLLVSNKYYDFINEKIKTCKIFVGGKTRQESSLIALKNCSKETKNILIHDAARPFINNEIISNCINTLKSNVAVCPALPSIDTIAQINNDEINKVLTRSELFHLQTPQGFSYSILADCHNQIKEHVTDDISIIQKCGFKPKIILGSKKNMKITYKEDFEILKVLI | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Length: 213
Sequence Mass (Da): 24183
|
A0A3M2FE69 | MRSEPGAFRGGKRDPEREKCSGTDRGARGIDRDAGREKRKGGRTEAAEKVNRFLGLSEADRRKITQRIGLTEKDLFASVKRATFLEDWPSEREEVLRNRFRILERSPEERLTGGGIGPFPIPAVVDAMASRSEFVTAYTPYQPEVSQGTLEVIFEFQTRVCDMTGLEISNAGLYDGSTAVAEAISMAAAVTKRREVLLARTVSPRIREVVRTLLAGRGFHFREVSFDRESGILKEVGDEATPSEETACLVIQSPNAFGLFESRGREWFAAAREVGAVPIQIFHPLAVFVSEKPASSGAAIAVAEGQPLGIPLSGGGPFLGMIAAEERFLRRMPGRIVGETVDANGRRALVLTLQAREQHIRRERATSNICSNQALMALRATLFCAALEWEGITDFARRLSDLANDKARAEAIFPGRVFNEYAVKGNRGLPLDYPELGAISVVGVGTECDE | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Length: 450
Sequence Mass (Da): 49303
|
A0A3M2F394 | MYRKDSTVPRGYGILYSLFLLGSAPRYLLRTVRNRRGPGIVQRFGLGVGFPSTRAGDCRLPGEGSERVSKRERDISRRDSSTSDVRSDRSVRPARSLWFHACSVGEVETAMPLVRLFARAYPDDALILSTVTETGQARARKLLGNEFVRYLPFDFGFAIRRHLSSVPLPRFFIVMETEIWPKLYSELSQHNIPLFIANGRISDRAWRRYRRAVEFLRGTMACVRAVGARTVQDAERFRILGARNVSVLGNIKFDRGAAPAPEGMPSGKFLLFASTHPGEDELFVRTWRSLRNRFPRLRAVLAPRHIERAPALAKKYGGALRSAGWKDESLLVLDTHGELAGLFSGATVAIIGGSFVPHGGHNPFEAAVQGVPILWGPHMQNFRDAVEVLEGRGGETVRENEELAEALEALLSDEDLRRQRGAAARAAASENTGAAERHFNFFRDRLFEGEGERR | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
EC: 2.4.99.12
Subcellular Location: Cell membrane
Sequence Length: 454
Sequence Mass (Da): 50773
|
A0A955W2I6 | MGRPEPPVRYDEIAPRAPDGPIDLSSLAPGGGPIELDIGFGRGRSLFERAEAAPEARIVGVELKAKWAWRVEQRRRRLGLDRVVVFAGDARDLLDRAGPDGSVARVFVHFPDPWWKKRHAKRRVLGPSFLDTLARLLEPGGALYVQTDVEARALLYRDLIAAHADFALDGGRGWVEANPFGARSNREARADEDGLPVYRLLAHRLPLGPPAP | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 212
Sequence Mass (Da): 23387
|
A0A3D1RZN0 | MSTIFSPEHINAHQALLQFLSINPVQQYDVSTKTWHAAEDIFSATLTTPVLTISAQHLNAYLVQSILAQLPSDVSNIAIRLHPLSDAFSASVVQVVLNEAVDKAWLAAIATQYYVDVFCITDAPRLADPGVIVMDMDSTVIQIECIDEIAKLCGKGDEVSAVTELAMEGKLDFTQSLRQRVSVLDGIDVNLLKGIRDSIPLMPGIHALLQTLQGNGWKTVIASGGFTFFAHYLQARLALDGAHANELEVVDGRLTGRVLGDIVDAQVKAQTVLNYAQHFDIPLSQTIALGDGANDLVMMGQAGLGMAFHAKPVVEAQADAAIRFGGLEQTLYALV | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
Catalytic Activity: H2O + O-phospho-D-serine = D-serine + phosphate
Sequence Length: 335
Sequence Mass (Da): 36061
|
A0A973HT54 | MVGGAAGAVLRFLSVEFAARCFGLAAYRTIFLVNLLGCFALGVFVGSLASPDGTLAAFIARWAPDQPDLPATWLASLIGTGLLGGFTTFSTFALDSLVLARERRRVEFLVDVLGTPALGIALAALGWIVAARGLV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 135
Sequence Mass (Da): 14030
Location Topology: Multi-pass membrane protein
|
A0A1H7RBF9 | MPDPANTRVIVGMSGGVDSSVSALLLQQQGYQVEGLFMKNWDEDDGTDYCTAKEDLADAQAVADKLGMKLHTANFAAEYWDNVFEHFLAEYKAGRTPNPDILCNREIKFKAFLDYALSLGADLIATGHYVRRRDSQGQSLLLKGLDGNKDQSYFLHAVGGEQIGKTLFPVGELEKPKVRRIAEEHGLATAKKKDSTGICFIGERRFSDFLKQYLPAQPGKIETVDGEEIGQHHGLMYHTIGQRQGLGIGGMKDASDEPWYVLAKDLARNVLIVGQGNDHPWLFSGTLHASDIYWVNPIDLSSPRRLTAKVRYRQSDQACVLEKTADGYRVTFEQPQRAVTPGQSVVFYDGEVCLGGGVIEQAEPADAGIQRP | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
EC: 2.8.1.13
Subcellular Location: Cytoplasm
Sequence Length: 372
Sequence Mass (Da): 41067
|
A0A2K3E271 | MAQAAFRAVEAMSASGTACPLACVRRLPPAAPAPRPASLSLTLHTTSLPRGSALRTRAAAPQSPAPAPHPSSAPSAADDAAAASDASDATEAVAAQAADAAALVGAAWDPEGLFAKAAGPLDFAAGQQMGDLILRRQREREARMAAAASAATAAAAAAAPAAAPAAPAAASAAPPPPSGGDVLPLPPLPAGLPPLRPLPVPVPAPEVGLTPAELPAAVVAEAEALLRERFMAVDLGTPGLRLLHLDPPVVTVDGFLPDDVCDAMVRAAEASGRMAGSRIGAGNASAAYGPNAASARRTSRGMMVTPGVAGPAMDGVVSELHARGKKLLRAAEGAAWGISGKLPRPRQYCYEALQVTRYDAGQHFLAHEDGFPPHLAASNAFQRHATLLVYLNDCEQGGATRFDQLGLAVRPRKGKLLLFFPAFADGSADPRSLHTACDAVDTKYVTQQWVARGLALPGSSTSSSSSSSGAARAVRGAVSAEARQAEARLEELEKAKAGKAKTSGKAGGKGFGAGKK | Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 516
Sequence Mass (Da): 52057
Location Topology: Single-pass type II membrane protein
|
A0A518BYC5 | MISPSTPDNDQRIAEIATSVLAGNLVSREQAQFLASLEGDDLYDLFYWANKIRIRFVGRQVKFCSIVTGKTGACSEDCSYCSQSKHYKTHVTPDKMTVDEMLQATEEARANGANSMGIVNSGRGPTDRELDWLEPFYRKTAEQGTIRPCATLGELTPEQAQRLKDMGVQRINHNLETSARHFKNIVSTHDYKDRVQTIRNAKNAGLSICAGGIFGLGEDWDDRIDMALALRELDVDVVPINFLNAIQGTPLYGEVTRLEPMQALHIIAVYKFILPQQELKIAGGREKILRDLQSWIFFAGGSSFLIGNYLTTFGRTPQQDHQMLKDLGLTYTTFDEVEHEAQPDAAMTRSPGHDSPAREGALLSRRDGSLVALPVLNQGEKLVTT | Cofactor: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
EC: 2.8.1.6
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Length: 385
Sequence Mass (Da): 42824
|
A0A2N2DRG6 | MNKNTLKNIVSPLLEWFGENARSMPWRSDPTPYKVWISEIMLQQTRVEAGRSYFLRWVEALPDVEALANVEESKLMKLWEGLGYYNRARNLKKAAGVVMEQYSGKIPETFEQLLSLPGIGPYTAGAIGSIAFQLPVPAVDGNVLRVVARVTGDRSDIRSEAVKRFYSESIASIMPSHRPGDFNQALMELGALVCIPNGMPRCDLCPLAGQCIAHMKKVTAEIPSKRKKPDRTITERTIFVLKIGSCILLRKREDKGLLAGQWELPGTDRLLSEDELEPLLESWGYRIRSMEELPPSRHIFSHVEWRMKAYKIEAEASFLKEDDAIWICADQERLSHEIALPSAFNAYRPSFF | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs.
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Sequence Length: 352
Sequence Mass (Da): 39915
|
A0A955UM02 | MHIKRFEAGTLEEALAAVKRELGPDALILSTRTLRRGGPIFGLMGGRRVEVQAARERGPGRASARVGADGPAGDLARCEADFESKSNPGAQEPRSEVDARGEGDGLVRGVDGALVEALRGELSRWRDRERFEEEVRSELRGLRRALAGVLGERVPDAADPLVRRLAGGGLDWVHAEGLVASLRDPAGSGQAHGIGMPGLLRRRLESKLAPPRPDEGSRVRVLVGAPGVGKTTTLAKLAARDEEGEREVALVALDHYRIGAPEQLRAYADLLDSPFCEVGDASELPRVVDRLRGRAVLVDTAGRGPRDEEALASLRPIRDLLGRRVSIELVVDATARREVQRAQLARFAALSPDRVILAKTDECDSLADVANLVLDADCPPVCWMGTGQRVPEDLELVEPGRLVQAVLGEAA | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 411
Sequence Mass (Da): 44104
Location Topology: Peripheral membrane protein
|
A0A7X7Z470 | MGFHVGIAGGLDLAPERAHRLGARAMQLFTRSPRSWQAPPLNGETAVAFRQETLAHGLLPVAHAIYLINLASPDEELRARSVAAFSDEIERCARLGIDRVVIHPGSHGLLTRAQGLRQALRSLKECTRRTRTAAVTILLETTSGAGRQLGGELADLAWMIDHHPEPERLGVCFDSCHLFAAGRALHEPDGLDRLLAETEKTIGLGKLGCWHLNDSLGDWNSHRDRHARIGRGKLGRDFFRRLLADERLFGVPKILEVPGGDEAFAADLRLLARLAPRG | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
EC: 3.1.21.2
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Length: 278
Sequence Mass (Da): 30500
|
A0A7Y5CC64 | MATKQVTAPTSGTPKQAPTSPTQAKPGLIATVREFFEDVVSEMKKVSWPTQAELKSLTQLVLWSLLISGIVLGIYDFIFNNLMALILKLG | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 90
Sequence Mass (Da): 9821
Location Topology: Single-pass membrane protein
|
A0A7K5Z861 | LWVSARPPTRTMTFGWHRSEMLGALASVLSIWVVTAALVYLAAARIISNDYEIEARAMLATSASAVGVNLIMAYILHQSPHGHGHGAGGYEQLEGGGGCQPSRAPLPGRAPLPGSTSVRAAFVHVVGDLLQSLGVLVAATIIYFKPQCKIADPISTLFFSVFVLGSTVTILRDVFRVLMEGAPRGTEFEAVKATLLGVRGVRGAHDLHLWALTPSHHAVAVHVATEASADPEAVLRDVTAQLQGRFGFASCTVQVERHREEMV | Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Subcellular Location: Membrane
Sequence Length: 263
Sequence Mass (Da): 28049
Location Topology: Multi-pass membrane protein
|
A0A1E5P7X5 | MESGHARSQQPGRQPQSPRRPWVVGVSGASGTPYAAAVLRGLRDAGESVDLVVSRASRLTLLDETGIAFRDAHWQEDLRTWLARGADGKPGTFTADVGDVRYWAAGDLAAGPSSGSYPAKGMLIVPASTASVAGVALGLSKDLLQRVASVTLKERRPLVVAVRETPLSGQTLRHMVALDEAGAVVLPASPAFYAGATHIQDLVDFVAGRVLDAAGVPHRLYRRWEGEIGGSRED | Function: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
EC: 2.5.1.129
Catalytic Activity: dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2
Sequence Length: 234
Sequence Mass (Da): 24727
|
A0A1F4U236 | IGDDVLMVSGSDCFGTPITVEADKEGKAPEEVANSYHEKDVHLFKDILDLSYDLYTKTLTDQHIKVTQDFFVKLLENGYIFVDKSSQYFSPTEKRFLPDRYVIGKCPNCGFADARSDQCDSCGKVLNQGELINPVSTISKEPVELKETQHYFIDWPKLQPKIVQYVKTHSSGWKDWVRAETLGWLNEGLKPRAITRDIDWGVPIPKDRIPENMLINDIDTKRIYVWFDAVIGYYSASLLWAQETGGDWKSFWYNKDAYHYYFMGKDNLMFHTIFWPGQLMGFDDQLHLPDLPSINMFFHLEGEKFSKSRGVTIEIKDLVEKYGNDRVRFYITLVMPETRDSSFSWSDFKEKINGVLVANIGNFIHRALSVGYNNGFNVSADKIFPEVLAEVKSSFSTARNYLEKCEFRNYLEVILKLAGFGNKLCDEEKIWELAKKDTTRFGAVMTNLYFIIGSLGYLFAPLMPEA | Function: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
EC: 6.1.1.10
Catalytic Activity: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Sequence Length: 466
Sequence Mass (Da): 53671
|
A0A971FCT0 | MTRAGTERHWMRRKLPRELHWQFALAALALYILGSTLGVTVFRSPNLSEAYLEAHGGEHREYLEIKKSEWFMLHEERPLLHPPATEEQHEMAEFVKKYEARPWFQEERSRASHYVLYFRVLNALVLVALFGWFLRTPLLDLLDGRIGEVRRGLEQAADARAETGRLEAEAGRRIGAFMEVEEQVKREAEDTLARDAERMERAFEARRAELEKDTEERVRAERHRAHAALRAGLVEEAVALAERACRAAADTDRLDAEVETFTRLLERAS | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 269
Sequence Mass (Da): 31189
Location Topology: Single-pass membrane protein
|
A0A956KBC3 | MNDRATLQLTVQTPTGLVVDERVTGVTAEDATGRFGVRPRAEPLVAALVAGILTARSIDGGERLVAVGPGILFTYDDRVEVAVRHAVVCDSLEHVQQCLENASQTQTAREKDLRLTFRDLMRKLAVTMVRGERDA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 135
Sequence Mass (Da): 14715
Location Topology: Peripheral membrane protein
|
A0A3D1R6D8 | MPTEFELIDRFLKPFARKGAGVVIGPGDDCAVLRPSPGADLCVTTDAVVEGVHFTSAFFSDADIGHKALAVNLSDLAAMGARPRWFVCSVACPPEALARLPAIARGMARLAAKSAIMLAGGNFARADALSLHITAFGEVARGEALTRSRARPKDRIYVTGTFGDAALGLALRSIGRKPGAAVAARQLRPEPRLKMGLLARGFARAAIDVSDGLVQDLGHVAEASGVGIRIDAQKVPTSRTFGDLAANRDLALTGGEDYELVLFVPPARAVAFERACKQAREQVTLIGEATKKPGIELLNAPQLAHTGFDHFGGPASRPRGRARRPKG | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Length: 327
Sequence Mass (Da): 34416
|
A0A7S3GYU5 | FTPYVNDQKLDWERHAVFKGYFNAIRYHMGSIAFGSFLILTLRPLRIMLHIFDTLQAKLCPGHQQQHFRLLRHISKDAYLMLAMCSDTFLRSAKSAEYMRNNSE | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 104
Sequence Mass (Da): 12283
Location Topology: Multi-pass membrane protein
|
A0A956DBS8 | MTKKSEKPTFTPRTKAALAACLVATAALTAADLGSKAWAFDRLSAERVGEPPPVCQADEHGYIQYQRARMEPIVVGEGWFELRYAENCGAAFGLLRNSTPALRHTIFGAAAILASLALLWMFASGRGGQWFAYSVPFIVSGAIGNLVDRLRLGYVVDFLRVYWDRPLPLIGSEWPTFNVADITITIGVGFLLVDGWLEGRREKAAERAAAAAEKPATT | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 218
Sequence Mass (Da): 23705
Location Topology: Multi-pass membrane protein
|
A0A8J7XHX1 | MWQWQWKSLRPHKPKKSREKLEAERMKKIQSYIDEGILKTPELIEVFKRVPREEFVPYDYRDYTYREAPLPLPALEGTISCPHSYPLFYEAMGLKSGDYFLEVGTGSGYGAALARDIVGKEGRVISLEIDRSAYDFAKSNLTRLGYNDIVLIRGDGYLGYEPEAPYDKISITAAVPSMPETFLDQLKDDGLAVAPIGPIENQRLMLIRKDGSMEMISESAVFVPMVGRYRHGR | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
EC: 2.1.1.77
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Length: 233
Sequence Mass (Da): 26564
|
A0A0S8HTV0 | MIELNFTLIFQLVIVLILMVALSGLVFKPFLGVLQARRDWVEGAEKKARELHRRTEELMEQHRDSMNAAQAQGASVRDEIRKEGLARETEILQKAQKEANRFMDEMKGRIQQESRAARAGLRIQAQNLSREIAAKMLGRNIQ | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 142
Sequence Mass (Da): 16299
Location Topology: Single-pass membrane protein
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.