ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
P47500 | MDFDKQLFFNVEKIVELTEQLEKDLNKPNLSFEQIKVINKELKHKQPLIVKFKELQKLVENANEAEQILNNSSLKELHEEAKKELEKIKASLPSLEEEIKFLLLPVDENNQKNVIVEIRPAAGGDESCIFLSDLFNMYKNYCTSKNWTVELNEIIPASVGINFVSFAVNGTDVFAKLKFESGVHRVQRVPLTEAKGRVHTSTVTVAVLPQLEEVEITINPSDLRIDTYRASGAGGQHVNRTESAVRITHLPTGIVVACQEGKSQFSNRDKAMKMLRAKLWENAQNKQLSTQADLRKSQVGSGERAEKIRTYNYPQNRITDHRIKLTINKLNTVILGDLDEIIEALQADEKKQQLEKFIS | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1 (By similarity).
Sequence Mass (Da): 40808
Sequence Length: 359
Subcellular Location: Cytoplasm
|
A9G9L1 | MLPIAKLEAVQRRFQELEHLMCSPAVLAAPAELQRLNRERTEIEPVVVAFARMRDVERRIAEDREALSDPDLSELAQAELPELELERERLAAELEVLLLPKDPNDTRNTVIEIRSGEGGEEAALFAADLFRMLCRYAETKRWKVEVLNLSEASAGGYKEVAALITGQDVYSHLRYEGGVHRVQRVPSTETQGRIHTSTATVAVLPEADEVDVHIDEKDLEISIAASGGPGGQGVNTTNSAVQIKHLPTGMIVKCQDERSQLKNKAKAMKVLRSRLLELEQRRQEEAQSAERRTMVGTGERAQKVRTYNFPQNRVTDHRIGLTLHKLDKIIEGDLEELIGALRTHRQAELLRRGGLSGPALEPAT | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 40630
Sequence Length: 364
Subcellular Location: Cytoplasm
|
Q00329 | MLDVNKKILMTGATSFVGTHLLHSLIKEGYSIIALKRPITEPTIINTLIEWLNIQDIEKICQSSMNIHAIVHIATDYGRNRTPISEQYKCNVLLPTRLLELMPALKTKFFISTDSFFGKYEKHYGYMRSYMASKRHFVELSKIYVEEHPDVCFINLRLEHVYGERDKAGKIIPYVIKKMKNNEDIDCTIARQKRDFIYIDDVVSAYLKILKEGFNAGHYDVEVGTGKSIELKEVFEIIKKETHSSSKINYGAVAMRDDEIMESHANTSFLTRLGWSAEFSIEKGVKKMLSMKE | Catalytic Activity: CDP-alpha-D-abequose + NADP(+) = CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + H(+) + NADPH
Sequence Mass (Da): 33775
Sequence Length: 293
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
EC: 1.1.1.341
|
P0A1P4 | MTFLKEYVIVSGASGFIGKHLLEALKKSGISVVAITRDVIKNNSNALANVRWCSWDNIELLVEELSIDSALIGIIHLATEYGHKTSSLINIEDANVIKPLKLLDLAIKYRADIFLNTDSFFAKKDFNYQHMRPYIITKRHFDEIGHYYANMHDISFVNMRLEHVYGPGDGENKFIPYIIDCLNKKQSCVKCTTGEQIRDFIFVDDVVNAYLTILENRKEVPSYTEYQVGTGAGVSLKDFLVYLQNTMMPGSSSIFEFGAIEQRDNEIMFSVANNKNLKAMGWKPNFDYKKGIEELLKRL | Catalytic Activity: CDP-alpha-D-abequose + NADP(+) = CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + H(+) + NADPH
Sequence Mass (Da): 34106
Sequence Length: 299
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
EC: 1.1.1.341
|
Q05342 | MRIVLTGGSGYIGSSLTPVLIKKYGRVYNIGRNTISEVSINGSKEYCEFTYESLFDSLVELSPDLVINLAAGYYNDSGAPDLNVIDGNLKIPFIILEYFKSCNYGRFINIGSYWEFSCSGRGVKGVNPYGIIKSTVRRLLDYYSKYNVIYTNLILYGSYGDNDHRGKIVDCIIDAVNSNETLKLSPGEQKLNLVYIDDIIEAILYIVSSDNGQYDNETLSIYTPTEHTVKEIVCFINEIKDNNLSLGGGRYRNDEVMAPDYKYRNIFHAKDKLKEYITSKIKK | Function: The CDP-abequose synthase is involved in lipopolysaccharides (LPS) synthesis containing abequose which are important antigens of the cell surface responsible for the serological O specificity. Derivatives of the 3,6-dideoxyhexose group have a particular highly immunogenic character.
Catalytic Activity: CDP-alpha-D-abequose + NADP(+) = CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + H(+) + NADPH
Sequence Mass (Da): 32018
Sequence Length: 283
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
EC: 1.1.1.341
|
P37742 | MLTCFKAYDIRGKLGEELNEDIAWRIGRAYGEFLKPKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPISGDTGLRDVQRLAEANDFPPVDETKRGRYQQINLRDAYVDHLFGYINVKNLTPLKLVINSGNGAAGPVVDAIEARFKALGAPVELIKVHNTPDGNFPNGIPNPLLPECRDDTRNAVIKHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVTAAGTPVMSKTGHAFIKERMRKEDAIYGGEMSAHHYFRDFAYCDTGMIPWLLVAELVCLKGKTLGELVRDRMAAFPASGEINSKLAHPVEAINRVEQHFSRDAGGGSHRWHQHDLCRLAALTCASSNTEPVVRLNVESRGDVPLMEEKTKLILELLNK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides. This enzyme participates in synthesis of the LPS O7 antigen.
Catalytic Activity: alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
Sequence Mass (Da): 49932
Sequence Length: 453
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
EC: 5.4.2.8
|
P37755 | MTQLTCFKAYDIRGELGEELNEDIAYRIGRAYGEFLKPGKIVVGGDVRLTSESLKLALARGLMDAGTDVLDIGLSGTEEIYFATFHLGVDGGIEVTASHNPMNYNGMKLVRENAKPISGDTGLRDIQRLAEENQFPPVDPARRGTLRQISVLKEYVDHLMGYVDLANFTRPLKLVVNSGNGAAGHVIDEVEKRFAAAGVPVTFIKVHHQPDGHFPNGIPNPLLPECRQDTADAVREHQADMGIAFDGDFDRCFLFDDEASFIEGYYIVGLLAEAFLQKQPGAKIIHDPRLTWNTVDIVTRNGGQPVMSKTGHAFIKERMRQEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELLCLKNSSLKSLVADRQAAFPASGEINRKLGNAAEAIARIRAQYEPAAAHIDTTDGISIEYPEWRFNLRTSNTEPVVRLNVESRADTALMNAKTEEILALLK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides. This enzyme participates in synthesis of the LPS O9 antigen.
Catalytic Activity: alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
Sequence Mass (Da): 50423
Sequence Length: 456
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
EC: 5.4.2.8
|
P26405 | MNVVNNSRDVIYSSGIVFGTSGARGLVKDFTPQVCAAFTVSFVAVMQEHFSFDTVALAIDNRPSSYGMAQACAAALADKGVNCIFYGVVPTPALAFQSMSDNMPAIMVTGSHIPFERNGLKFYRPDGEITKHDEAAILSVEDTCSHLELKELIVSEMAAVNYISRYTSLFSTPFLKNKRIGIYEHSSAGRDLYKPLFIALGAEVVSLGRSDNFVPIDTEAVSKEDREKARSWAKEFDLDAIFSTDGDGDRPLIADEAGEWLRGDILGLLCSLALDAEAVAIPVSCNSIISSGRFFKHVKLTKIGSPYVIEAFNELSRSYSRIVGFEANGGFLLGSDICINEQNLHALPTRDAVLPAIMLLYKSRNTSISALVNELPTRYTHSDRLQGITTDKSQSLISMGRENLSNLLSYIGLENEGAISTDMTDGMRITLRDGCIVHLRASGNAPELRCYAEANLLNRAQDLVNTTLANIKKRCLL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides. This enzyme participates in synthesis of the LPS group B O antigen.
Catalytic Activity: alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52086
Sequence Length: 477
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Subcellular Location: Cell membrane
EC: 5.4.2.8
|
P26404 | MSFLPVIMAGGTGSRLWPLSREYHPKQFLSVEGKLSMLQNTIKRLASLSTEEPVVICNDRHRFLVAEQLREIDKLANNIILEPVGRNTAPAIALAAFCALQNADNADPLLLVLAADHVIQDEIAFTKAVRHAEEYAANGKLVTFGIVPTHAETGYGYIRRGELIGNDAYAVAEFVEKPDIDTAGDYFKSGKYYWNSGMFLFRASSYLNELKYLSPEIYKACEKAVGHINPDLDFIRIDKEEFMSCPSDSIDYAVMEHTQHAVVIPMSAGWSDVGSWSSLWDISNKDHQRNVLKGDIFAHACNDNYIYSEDMFISAIGVSNLVIVQTTDALLVANKDTVQDVKKIVDYLKRNDRNEYKQHQEVFRPWGKYNVIDSGKNYLVRCITVKPGEKFVAQMHHHRAEHWIVLSGTARVTKGEQTYMVSENESTFIPPNTIHALENPGMTPLKLIEIQSGTYLGEDDIIRLEQRSGFSKEWTNERS | Function: Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides. This enzyme participates in synthesis of the LPS group B O antigen.
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Mass (Da): 54046
Sequence Length: 479
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.
EC: 2.7.7.13
|
P26406 | MDNIDNKYNPQLCKIFLAISDLIFFNLALWFSLGCVYFIFDQVQRFIPQDQLDTRVITHFILSVVCVGWFWIRLRHYTYRKPFWYELKEIFRTIVIFAIFDLALIAFTKWQFSRYVWVFCWTFALILVPFFRALTKHLLNKLGIWKKKTIILGSGQNARGAYSALQSEEMMGFDVIAFFDTDASDAEINMLPVIKDTEIIWDLNRTGDVHYILAYEYTELEKTHFWLRELSKHHCRSVTVVPSFRGLPLYNTDMSFIFSHEVMLLRIQNNLAKRSSRFLKRTFDIVCSIMILIIASPLMIYLWYKVTRDGGPAIYGHQRVGRHGKLFPCYKFRSMVMNSQEVLKELLANDPIARAEWEKDFKLKNDPRITAVGRFIRKTSLDELPQLFNVLKGDMSLVGPRPIVSDELERYCDDVDYYLMAKPGMTGLWQVSGRNDVDYDTRVYFDSWYVKNWTLWNDIAILFKTAKVVLRRDGAY | Function: Is responsible for transferring galactose-1-phosphate to the lipid precursor undecaprenol phosphate in the first steps of O-polysaccharide biosynthesis.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-alpha-D-galactose = alpha-D-galactosyl-di-trans,octa-cis-undecaprenyl diphosphate + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56198
Sequence Length: 476
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.8.6
|
P14168 | MKILIMGAFGFLGSRLTSYFESRHTVIGLARKRNNEATINNIIYTTENNWIEKILEFEPNIIINTIACYGRHNEPATALIESNILMPIRVLESISSLDAVFINCGTSLPPNTSLYAYTKQKANELAAAIIDKVCGKYIELKLEHFYGAFDGDDKFTSMVIRRCLSNQPVKLTSGLQQRDFLYIKDLLTAFDCIISNVNNFPKFHSIEVGSGEAISIREYVDTVKNITKSNSIIEFGVVKERVNELMYSCADIAELEKIGWKREFSLVDALTEIIEEEGK | Function: Catalyzes synthesis of paratose and tyvelose, unusual 3,6-dideoxyhexose sugars that form part of the O-antigen in the lipopolysaccharides of several enteric bacteria.
Catalytic Activity: CDP-alpha-D-paratose + NADP(+) = CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + H(+) + NADPH
Sequence Mass (Da): 31501
Sequence Length: 279
Pathway: Nucleotide-sugar biosynthesis; CDP-3,6-dideoxy-D-mannose biosynthesis; CDP-3,6-dideoxy-D-mannose from CTP and alpha-D-glucose 1-phosphate: step 4/5.
EC: 1.1.1.342
|
P26401 | MLISFCIPTYNRKEYLEELLNSINNQEKFNLDIEICISDNASTDGTEEMIDVWRNNYNFPIIYRRNSVNLGPDRNFLASVSLANGDYCWIFGSDDALAKDSLAILQTYLDSQADIYLCDRKETGCDLVEIRNPHRSWLRTDDELYVFNNNLDREIYLSRCLSIGGVFSYLSSLIVKKERWDAIDFDASYIGTSYPHVFIMMSVFNTPGCLLHYISKPLVICRGDNDSFEKKGKARRILIDFIAYLKLANDFYSKNISLKRAFENVLLKERPWLYTTLAMACYGNSDEKRDLSEFYAKLGCNKNMINTVLRFGKLAYAVKNITVLKNFTKRIIK | Function: Catalyzes the transfer of CDP-abequose on D-mannosyl-L-rhamnosyl-D-galactose-1-diphospholipid to yield D-abequosyl-D-mannosyl-rhamnosyl-D-galactose-1-diphospholipid.
Catalytic Activity: alpha-D-Man-(1->4)-alpha-L-Rha-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate + CDP-alpha-D-abequose = alpha-D-Abe-(1->3)-alpha-D-Man-(1->4)-alpha-L-Rha-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate + CDP + H(+)
Sequence Mass (Da): 38579
Sequence Length: 333
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
EC: 2.4.1.60
|
P37746 | MNTNKLSLRRNVIYLAVVQGSNYLLPLLTFPYLVRTLGPENFGIFGFCQATMLYMIMFVEYGFNLTATQSIAKAADSKDKVTSIFWAVIFSKIVLIVITLIFLTSMTLLVPEYNKHAVIIWSFVPALVGNLIYPIWLFQGKEKMKWLTLSSILSRLAIIPLTFIFVNTKSDIAIAGFIQSSANLVAGIIALAIVVHEGWIGKVTLSLHNVRRSLADGFHVFISTSAISLYSTGIVIILGFISGPTSVGNFNAANTIRNALQGLLNPITQAIYPRISSTLVLNRVKGVILIKKSLTCLSLIGGAFSLILLLGASILVKISIGPGYDNAVIVLMIISPLPFLISLSNVYGIQVMLTHNYKKEFSKILIAAGLLSLLLIFPLTTLFKEIGAAITLLATECLVTSLMLMFVRNNKLLVC | Function: May be involved in the translocation process of the nascent O-polysaccharide molecules and/or its ligation to lipid A core units.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45383
Sequence Length: 415
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Subcellular Location: Cell inner membrane
|
Q99191 | MRKLRLVRIPRHLIIAASSWLSKIIIAGVQLVSVKFLLEILGEESYAVFTLLTGLLVWFSIADIGIGSSLQNYISELKADRKSYDAYIKAAVHILFASLIILSSTLFFLSDKLSSLYLTSFSDELKNNSGSYFFIASILFIFIGVGSVVYKILFAELLGWKANIINALSYLLGFLDVVAIHYLMPDSSITFALVALYAPVAILPIIYISFRYIYVLKAKVNFNTYKLLLSRSSGFLIFSSLSIIVLQTDYIVMSQKLSAADIIKYTVTMKIFGLMFFIYTAVLQALWPVCAELRVKMQWRKLHRIIFLNIIGGVFFIGLGTLFIYVLKDYIYSIIANGIDYNISGVVFVLLAVYFSIRVWCDTFAMLLQSMNQLKILWLIVPCQALIGGVTQWYFAEHYGIVGILYGLILSFSLTVFWGLPVYYMYKSKRLA | Function: May be involved in the translocation process of the nascent O-polysaccharide molecules and/or its ligation to lipid A core units.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48947
Sequence Length: 432
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Subcellular Location: Cell inner membrane
|
Q03583 | MKKNILLLFLVHGANYLFPFIVLPYQTRILSIETFADVAKIQAAVMLLSLIVNYGYNLSSTRAIARAVSQAEINKIYSETLIVKLLLATICLALGCVHLMYVKEYSLIYPFIISSIYLYGSALFATWLFQGLEKMKAVVIATTIAKLTGVILTFILVKSPNDIVAALFTQNIGMFISGIISIYLVRKNKYATVICFRLKNIIVSLKEAWPFFLSLAATSVYTYFNVILLSFYAGDYVVANFNAADKLRMAAQGLLIPIGQAVFPRLSKLEGYEYSSKLKIYAIRYAIFGVCISAGLVFLGPMLTTIYLGKEYSLSGEYLQSMFLLPATISISTILSQWMLIPQGKEKILSRIYILGAIVHLLYAFPLVYYYGAWGMVISILFTEVLIVLFMLKAVK | Function: May be involved in the translocation process of the nascent O-polysaccharide molecules and/or its ligation to lipid A core units.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44309
Sequence Length: 396
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Subcellular Location: Cell inner membrane
|
P37748 | MIYLVISVFLITAFICLYLKKDIFYPAVCVNIIFALVLLGYEITSDIYAFQLNDATLIFLLCNVLTFTLSCLLTESVLDLNIRKVNNAIYSIPSKKVHNVGLLVISFSMIYICMRLSNYQFGTSLLSYMNLIRDADVEDTSRNFSAYMQPIILTTFALFIWSKKFTNTKVSKTFTLLVFIVFIFAIILNTGKQIVFMVIISYAFIVGVNRVKHYVYLITAVGVLFSLYMLFLRGLPGGMAYYLSMYLVSPIIAFQEFYFQQVSNSASSHVFWFFERLMGLLTGGVSMSLHKEFVWVGLPTNVYTAFSDYVYISAELSYLMMVIHGCISGVLWRLSRNYISVKIFYSYFIYTFSFIFYHESFMTNISSWIQITLCIIVFSQFLKAQKIK | Function: May link the O-antigen tetrasaccharide units into long chains, giving rise to typical smooth LPS.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44744
Sequence Length: 388
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subcellular Location: Cell inner membrane
|
Q00474 | MLPFPPGAILRDVLNVFFVALVLVRFVIDRKKTYFPLVFTIFSWSAVILWVIALTIFSPDKIQAIMGGRSYILFPAVFIALVILKVSYPQSLNIEKIVCYIIFLMFMVATISIIDVLMNGEFIKLLGYDEHYAGEQLNLINSYDGMVRATGGFSDALNFGYMLTLGVLLCMECFSQGYKRLLMLIISFVLFIAICMSLTRGAILVAALIYALYIISNRKMLFCGITLFVIIIPVLAISTNIFDNYTEILIGRFTDSSQASRGSTQGRIDMAINSLNFLSEHPSGIGLGTQGSGNMLSVKDNRLNTDNYFFWIALETGIIGLIINIIYLASQFYSSTLLNRIYGSHCSNMHYRLYFLFGSIYFISAALSSAPSSSTFSIYYWTVLALIPFLKLTNRRCTR | Function: May link the O-antigen tetrasaccharide units into long chains, giving rise to typical smooth LPS.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44824
Sequence Length: 399
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subcellular Location: Cell inner membrane
|
P0A236 | MLIISYIALCLLFIVYLYTLSVRIEGKIINVMVPYLIITVPTLYVFEGIFVYLSEVQNYTVEYLFFYTCYITYIASFVISYLYTQRKPIYNKSNTKNKPRYVFTSLLFTFLAFIIYLPVLMEFREYILSPRRIYELTRTGYGIYFYPSLMFSLVASICAFFTYKKSKLFCISIVLFNCILIFLHGNKGPIFSIFIAFILYLSYIENKKIKFMFLVKSFAVIAVIVTAFFAYTFTDGNPIENMANYSDYTRNAVLVASSNFDFMYGKLLMESEVYSRIPRAIWPDKPEDFGALYLAKVFFPDAFYRNQGAPAFGYGELYADFGLFTPVWLVISGVFKGVLAKYFSNKTQETKSAHYFIMFLFCIGISVIPVSMGWLFPEHLMIAFMVYIASSFVFSEHIRFVLLRNNK | Function: May link the O-antigen tetrasaccharide units into long chains, giving rise to typical smooth LPS.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47461
Sequence Length: 407
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subcellular Location: Cell inner membrane
|
Q03584 | MTYFTGFILILFAIIIKRLTPSQSKKNIVLIANAFWGILLVGYTFNEQYFVPLSATTLFFILAFLFFFSMTYILIARSGRVVFSFGTGFIESKYIYWFAGMINIISICFGIILLYNNHFSLKVMREGILDGSISGFGLGISLPLSFCCMYLARHENKKNYFYCFTLLSFLLAVLSTSKIFLILFLVYIVGINSYVSKKKLLIYGVFVFGLFALSSIILGKFSSDPEGKIISAIFDTLRVYLFSGLAAFNLYVEKNATLPENLLLYPFKEVWGTTKDIPKTDILPWINIGVWDTNVYTAFAPWYQSLGLYAAIIIGILLGFYYGIWFSFRQNLAVGFYQTFLCFPLLMLFFQEHYLLSWKMHFIYFLCAILLAMRKALEYE | Function: May link the O-antigen tetrasaccharide units into long chains, giving rise to typical smooth LPS.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43732
Sequence Length: 380
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subcellular Location: Cell inner membrane
|
P37784 | MNNINKIFITFLCIELIIGGGGRLLEPLGIFPLRYLLFVFSFILLIFNLVTFNFSITQKCVSLFIWLLLFPFYGFFVGLLAGNKINDILFDVQPYLFMLSLIYLFTLRYTLKVFSCEIFIKIVNAFALYGSLLYISYIILLNFGLLNFNLIYEHLSLTSEFFFRPDGAFFSKSFYFFGVGAIISFVDKKYLKCLIIVLAILLTESRGVLLFTTLSLLLASFKLHKLYLNTIIIILGSVLFIIMLYMVGSRSEDSDSVRFNDLYFYYKNVDLATFLFGRGFGSFILDRLRIEIVPLEILQKTGVIGVFISLVPMLLIFLKGYFLNSTKTSLMMSLILFFSITVSITNPFLFTPMGIFIIGVVVLWVFSIENIQISNNLTSGAK | Function: May link the O-antigen tetrasaccharide units into long chains, giving rise to typical smooth LPS.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43724
Sequence Length: 382
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subcellular Location: Cell inner membrane
|
Q56328 | MNGAVCVLSALIAVFTCFSCRPAVQDERAVRIAVFVPGFRHDSPVYAMLCDGVERAVTQERATGRSIGLDIIEAGPNQALWREKLAHLAAEQRYRLIVSSNPALPHVLEPILRQFPLQRFLVLDAYAPQEHSLITFRYNQWEQAYLAGHLSALVSASAMRFANADKKIGLIAGQSYPVMTQTIIPAFLAGARAVDPAFEVDVRVVGNWYDAAKSADLARILFHEGVDVMMPICGGANQGVLAAARELGFYVSWFDDNGYARAPGYVVGSSVMEQERLAYEQTLRCIRGELPSAGAWTLGVKDGYVRFIEEDPLYLQTVPEPIRVRQSALLRRIQSGELTLPVR | Function: Probably part of the ABC transporter complex RfuABCD involved in riboflavin import. Binds riboflavin.
Location Topology: Lipid-anchor
Sequence Mass (Da): 37882
Sequence Length: 343
Subcellular Location: Cell inner membrane
|
O83321 | MMIAERGVRASARGVLSLHHIGKTYPRVMPRSKRGVWGMFGHPGRRAVDDAHTAHGPCSGARETDAAEHSVLSDVNLSFFTGEIHALLGKNGAGKSTLAHILSGFCVPTHGQLRLDGKEQRFSVPFDALRAGIGIVHQQPVFAERATVFENVVMGSAALTGVRWVRRAQVRERIDRIIAQWRMPLKKEEYVACLSADKRFFVSLLCVLFRNPRFIILDEPRCAPAQSRAVFFSHLEEFFVRSSHAPRCGGGVIVVTHRFADALRWAQRISLIEGGKACSFLRTDLLDEYCSAHQVNECIQKVSCALMSASTVTSSAVSSFSSLSDTQSCATVPRTSSARPWVLRVESLQVSKHADVPLTDISFSVAASAIIGIVGTPEDGVHVLEDILCDMHAGASRTHCTGNILLQEHDQVWCLPLQRNTPSLLRAHGVACVPSNCIQRGASMQLTLFDLLVPYTLRTWRTRVRAQMRFVARLLAEEEIYCDPLQPACTLSGGQLQRVILARELATRPRLLILAEPAEGLDSASEQRLLARLRQVAQAGTALVLLAREQHQAQWRALCTERFLLRAGTLCAEVSGTPSPSQDSHT | Function: Probably part of the ABC transporter complex RfuABCD involved in riboflavin import. Probably responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 64410
Sequence Length: 586
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
O83323 | MKRVINSCIAVLLGVAVMSAVIVLCSENPSVSLAAFFLKPFSTRGYIRALFHKAGLFVCMALGASCALKTGMINLGGDGQIYAAGFVTALLLREYWGVGFLLQWSVALLCALSVAGILACVSGILKAWLATSEMITSFLLSTACVPLIDALIITVTRDPAGNLLATAPVHSHFILQQQTSLFGVPAVLTYASLVALAVGCFFSYTRVGYQFRICGKAPEFGRFVGFPVWATYVWGMVLSGALFGLTGFFSVVGLFGTCYVGFSVGMGYAALAHALIAHAHITVLVPLAFFFAWMETASEAAVLGAHLTVNVVLFLQAAIFLLISAQWSAPWNAVRRGARRVYRFLVTVFCFRGEKHRTRRRHALSVHDTHHRRSRWE | Function: Probably part of the ABC transporter complex RfuABCD involved in riboflavin import. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40888
Sequence Length: 377
Subcellular Location: Cell inner membrane
|
O83324 | MGVIGTTVIAILHRAAPLACAAAGALATEYAGVLGIFMEGVITFSSFCIAFFALVWGSYWGGLGITVCVVPLCLFFVAVGTERMRANPFLTGIAVHFSAMGMSAFGASSMFARAAASAMQMDTAAHGVSFTHVSLAHTRVLPHPLWGTAVAFALVWVFHLYLYSTNVGINFMHSGEGALALQVRGTDAARYRMVSWAVAGVCAVCAGGLLVLRVGTYTPQMAAGRGWTALAIVFLARKRMMWCVPAAIFFSGIEHMCDVLQGTHVVPTGVLFALPYILSLVVFVCTRRTSPCRRGERRRSRLLFAYLQRVTCA | Function: Probably part of the ABC transporter complex RfuABCD involved in riboflavin import. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33534
Sequence Length: 313
Subcellular Location: Cell inner membrane
|
D2HWM5 | MAQEAMEYNVDEQLEHRVAEQPVPAEVVSTQGGPPPLQPLPTEVVSSQGAPPLLQPAPAEGTSSQVGPHLLQPAAQLSVDLTEEVELLGEDRVENINPGASEEHRQPSRVNRPIPVSSLDSMNSFISGLQRLHGMLEFLRPPSDHNVGPVRSRRRRGSASRRSRTVGSQRTDSARSRAPLDAYFQVSRTQPHLPSMSQDSETRNPVSEDLQVSSSSSSDSESSAEYEEVVVQAEDTRAVVSEEQGGTAAEQEVTCVGGGETLPKQSPQKTNPLLPSVSKDDEEGDTCTICFEHWTNAGDHRLSALRCGHLFGYKCISKWLKGQARKCPQCNKKAKHSDIVVLYARTLRALDTSEHERMKSSLLKEQMLRKQAELESAQCRLQLQVLTDECSKLHSRVQDLQKLTVQHRDQISQSPSGSQARSLNCLPSSQNQRKYHFQKTFTVSPTGNCRIMTYCDALSCLVVSQPSPQASFLPGFGVKMLSTANMKSSQYVPMHGKQIRGLAFSSRSKGLLLSASLDSTVKLTSLETNTVVQTYNAGRPVWSCCWCLDESNHIYAGLVNGSILVYDLRNTSSHIQELVPQKARCPLVSLSYIPRAASAAFPYGGVLAGTLENASFWELKMGFSHWPHVLPMEPGGCVDFQTESSTRHCLVTYRPDKNHNTLRSVLMEMSYKLNDAGEPVCSCRPVQTFLGGPTCKLLTKSAIFQNPENDGSILVCTGDEASNSALLWDAGSGSLLQELQADQPVLDICPFEANHSSCLATLTEKMVHIYRWE | Function: E3 ubiquitin-protein ligase required for the repair of DNA interstrand cross-links (ICL) in response to DNA damage. Plays a key role in RPA-mediated DNA damage signaling and repair. Acts by mediating ubiquitination of the RPA complex (RPA1, RPA2 and RPA3 subunits) and RAD51 at stalled replication forks, leading to remove them from DNA damage sites and promote homologous recombination. Also mediates the ubiquitination of p53/TP53 in the late response to DNA damage, and acts as a positive regulator of p53/TP53 stability, thereby regulating the G1/S DNA damage checkpoint. May act by catalyzing the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. In response to ionizing radiation, interacts with MDM2 and enhances p53/TP53 ubiquitination, possibly by restricting MDM2 from extending polyubiquitin chains on ubiquitinated p53/TP53.
PTM: Phosphorylated at Ser-46 and Ser-63 upon DNA damage by ATM or ATR. ATM phosphorylation occurs at early times upon DNA damage, while ATR is the major kinase at later times. Phosphorylation by ATM and ATR is required to stabilize p53/TP53. Part of the phosphorylation depends upon RPA2 presence.
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.
Sequence Mass (Da): 84945
Sequence Length: 773
Domain: The coiled coil domain may be involved in RPA2-binding.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
|
Q6PCD5 | MAHEAMEYDVQVQLNHAEQQPAPAGMASSQGGPALLQPVPADVVSSQGVPSILQPAPAEVISSQATPPLLQPAPQLSVDLTEVEVLGEDTVENINPRTSEQHRQGSDGNHTIPASSLHSMTNFISGLQRLHGMLEFLRPSSSNHSVGPMRTRRRVSASRRARAGGSQRTDSARLRAPLDAYFQVSRTQPDLPATTYDSETRNPVSEELQVSSSSDSDSDSSAEYGGVVDQAEESGAVILEEQLAGVSAEQEVTCIDGGKTLPKQPSPQKSEPLLPSASMDEEEGDTCTICLEQWTNAGDHRLSALRCGHLFGYRCISTWLKGQVRKCPQCNKKARHSDIVVLYARTLRALDTSEQERMKSSLLKEQMLRKQAELESAQCRLQLQVLTDKCTRLQRRVQDLQKLTSHQSQNLQQPRGSQAWVLSCSPSSQGQHKHKYHFQKTFTVSQAGNCRIMAYCDALSCLVISQPSPQASFLPGFGVKMLSTANMKSSQYIPMHGKQIRGLAFSSYLRGLLLSASLDNTIKLTSLETNTVVQTYNAGRPVWSCCWCLDEANYIYAGLANGSILVYDVRNTSSHVQELVAQKARCPLVSLSYMPRAASAAFPYGGVLAGTLEDASFWEQKMDFSHWPHVLPLEPGGCIDFQTENSSRHCLVTYRPDKNHTTIRSVLMEMSYRLDDTGNPICSCQPVHTFFGGPTCKLLTKNAIFQSPENDGNILVCTGDEAANSALLWDAASGSLLQDLQTDQPVLDICPFEVNRNSYLATLTEKMVHIYKWE | Function: E3 ubiquitin-protein ligase required for the repair of DNA interstrand cross-links (ICL) in response to DNA damage . Plays a key role in RPA-mediated DNA damage signaling and repair . Acts by mediating ubiquitination of the RPA complex (RPA1, RPA2 and RPA3 subunits) and RAD51 at stalled replication forks, leading to remove them from DNA damage sites and promote homologous recombination . Also mediates the ubiquitination of p53/TP53 in the late response to DNA damage, and acts as a positive regulator of p53/TP53 stability, thereby regulating the G1/S DNA damage checkpoint . May act by catalyzing the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome . In response to ionizing radiation, interacts with MDM2 and enhances p53/TP53 ubiquitination, possibly by restricting MDM2 from extending polyubiquitin chains on ubiquitinated p53/TP53 .
PTM: Phosphorylated at Ser-46 and Ser-63 upon DNA damage by ATM or ATR. ATM phosphorylation occurs at early times upon DNA damage, while ATR is the major kinase at later times. Phosphorylation by ATM and ATR is required to stabilize p53/TP53. Part of the phosphorylation depends upon RPA2 presence.
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.
Sequence Mass (Da): 85094
Sequence Length: 774
Domain: The coiled coil domain may be involved in RPA2-binding.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
|
Q7TQ33 | MGVRAAPSCAAAPAAAGAEQSRRPGLWPPSPPPPLLLLLLLSLGLLHAGDCQQPTQCRIQKCTTDFVALTAHLNSAADGFDSEFCKALRAYAGCTQRTSKACRGNLVYHSAVLGISDLMSQRNCSKDGPTSSTNPEVTHDPCNYHSHGGVREHGGGDQRPPNYLFCGLFGDPHLRTFKDHFQTCKVEGAWPLIDNNYLSVQVTNVPVVPGSSATATNKVTIIFKAQHECTDQKVYQAVTDDLPAAFVDGTTSGGDGDVKSLHIVEKESGRYVEMHARYIGTTVFVRQLGRYLTLAIRMPEDLAMSYEESQDLQLCVNGCPMSECIDDGQGQVSAILGHSLPHTTSVQAWPGYTLETASTQCHEKMPVKDIYFQSCVFDLLTTGDANFTAAAHSALEDVEALHPRKERWHIFPSSCGGCRDLPVGLGLTCLILIMFL | Function: Member of the repulsive guidance molecule (RGM) family that contributes to the patterning of the developing nervous system. Acts as a bone morphogenetic protein (BMP) coreceptor that potentiates BMP signaling. Promotes neuronal adhesion. May inhibit neurite outgrowth (By similarity).
PTM: GPI-anchored.
Location Topology: Lipid-anchor
Sequence Mass (Da): 47181
Sequence Length: 436
Subcellular Location: Cell membrane
|
Q6ZVN8 | MGEPGQSPSPRSSHGSPPTLSTLTLLLLLCGHAHSQCKILRCNAEYVSSTLSLRGGGSSGALRGGGGGGRGGGVGSGGLCRALRSYALCTRRTARTCRGDLAFHSAVHGIEDLMIQHNCSRQGPTAPPPPRGPALPGAGSGLPAPDPCDYEGRFSRLHGRPPGFLHCASFGDPHVRSFHHHFHTCRVQGAWPLLDNDFLFVQATSSPMALGANATATRKLTIIFKNMQECIDQKVYQAEVDNLPVAFEDGSINGGDRPGGSSLSIQTANPGNHVEIQAAYIGTTIIIRQTAGQLSFSIKVAEDVAMAFSAEQDLQLCVGGCPPSQRLSRSERNRRGAITIDTARRLCKEGLPVEDAYFHSCVFDVLISGDPNFTVAAQAALEDARAFLPDLEKLHLFPSDAGVPLSSATLLAPLLSGLFVLWLCIQ | Function: Acts as a bone morphogenetic protein (BMP) coreceptor . Through enhancement of BMP signaling regulates hepcidin (HAMP) expression and regulates iron homeostasis .
PTM: Autocatalytically cleaved at low pH; the two chains remain linked via two disulfide bonds . Also proteolytically processed by TMPRSS6, several fragments being released in the extracellular space; regulates HJV activity in BMP signaling and thefore iron homeostasis .
Location Topology: Lipid-anchor
Sequence Mass (Da): 45080
Sequence Length: 426
Subcellular Location: Cell membrane
|
Q7TQ32 | MGQSPSPRSPHGSPPTLSTLTLLLLLCGQAHSQCKILRCNAEYVSSTLSLRGGGSPDTPRGGGRGGLASGGLCRALRSYALCTRRTARTCRGDLAFHSAVHGIEDLMIQHNCSRQGPTAPPPARGPALPGAGPAPLTPDPCDYEARFSRLHGRAPGFLHCASFGDPHVRSFHNQFHTCRVQGAWPLLDNDFLFVQATSSPVSSGANATTIRKITIIFKNMQECIDQKVYQAEVDNLPAAFEDGSINGGDRPGGSSLSIQTANLGSHVEIRAAYIGTTIIIRQTAGQLSFSIRVAEDVARAFSAEQDLQLCVGGCPPSQRLSRSERNRRGAIAIDTARRLCKEGLPVEDAYFQSCVFDVSVSGDPNFTVAAQTALDDARIFLTDLENLHLFPSDAGPPLSPAICLVPLLSALFVLWLCFSK | Function: Acts as a bone morphogenetic protein (BMP) coreceptor. Through enhancement of BMP signaling regulates hepcidin (HAMP) expression and regulates iron homeostasis.
PTM: Autocatalytically cleaved at low pH; the two chains remain linked via two disulfide bonds. Also proteolytically processed by TMPRSS6, several fragments being released in the extracellular space; regulates HJV activity in BMP signaling and thefore iron homeostasis.
Location Topology: Lipid-anchor
Sequence Mass (Da): 44848
Sequence Length: 420
Subcellular Location: Cell membrane
|
Q8UBN2 | MARAERSVLLRLENISKEFPGVKALSNVHFDLRSGEVHAVCGENGAGKSTLMKIISGVYQPSEGTILHKGEKVQYASPLQSEAAGIAIIHQELNLVPHLSVAENIYLAREPRRGFLVDRKKLRLDAKRCLDRLGVDINPDQLVRSLSVAQCQMVEIAKALSLDAEVLIMDEPTSSLTEQETRLLFKVIRDLKASGVGIVYISHRLDEMAEIVDRVTILRDGRYISTDDFASITVDDIVTRMVGRSLEDKFPERTSRPTDDILFSVEGLTRNGVFSDVSFSLRRGEILGFAGLMGAGRTEVARAIFGADPLDAGKIVFNGRELSIGSPQDAIEEGIAYLSEDRKSDGLAIKMSVAANTTLANLGEVSNRFGLIDFKKHDDVAKRYVDLLNIRTPSIDQTVRLLSGGNQQKIIIGKWLFRQSRVLFFDEPTRGIDVGAKFAIYKIMDELAAQGIGVILISSELPEILGLTDRIAVFHQGRITGVLETAKTNQEEIMRYASGYGRAAQ | Function: Part of an ABC transporter complex involved in carbohydrate import. Could be involved in ribose, galactose and/or methyl galactoside import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55629
Sequence Length: 505
Subcellular Location: Cell inner membrane
EC: 7.5.2.11
|
Q2KAW9 | MSATLQRVAPLSGGEGHRTPIDSGAGFVLEMRSITKAFPGVLALDGMSLKVRAGTVHVLVGENGAGKSTLMKILSGIYAIDGGEILFRGEKLDHQSAAAALERGISMIHQELSPVLDMTIAENIFLGREPTYSRTGVLSRFVDFDRMNSDTQTLLDRLGLKYSPQTKMRDLSIATMQLIEIVKAISREASLIIMDEPTSAISDTEVAMLFRQIADLKAAGVAIIYITHKMDEIFQIADDITVMRDGQFVAAAPASEYEPAKLISQMVGRTISSIFPKEEVPIGDIVLSVENLSRDGVFDNVGFEVRAGEIVGLSGLIGAGRTEVARVIFGLDAADAGVVRLNGKPLKLTSPKDAIANGIAMVSEDRKAEGLVLCRSVGENISLANLKKFASGIFISERQEETASQRMIKMLQIKTPDTAMIVENLSGGNQQKIVLAKWLLGDLKLLILDEPTRGIDVGSKSEIHRLMTEFARQGLAIIMISSELPEILGMSDRVVVMSEGRVTGELTRAEATQENIMRLATGGH | Function: Part of an ABC transporter complex involved in carbohydrate import. Could be involved in ribose, galactose and/or methyl galactoside import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56549
Sequence Length: 524
Subcellular Location: Cell inner membrane
EC: 7.5.2.11
|
Q92MP8 | MTVLVSLSGISKNFSGVQALKGVDFDLRAGEVHALVGENGAGKSTLMRVLAGEMKPTSGTVSIHGETMQHSGPRGAAGRGISVIHQELALAPDLTVAENIFLGRLPRIVNHRRLRKAASEILERLGFDIDPAIHAGRLTVAHQQVVEIAKALSNRARIIVFDEPTAVLANTDAERLLAIIRELRAGGTGAVYISHRLNEVFDLSDRITVMKDGSHVETLETSATDVDAVIARMVGRQMSALFPSKAGRVPGEVVVRVRNVSRGRKVRDVSFSVRAGEVVGLGGLVGSGRTEVARLVFGADKMDSGTVELNGKPLHLSSPREAVRARIGLVPEDRKQQGVILDAPIRINTTLAKIRSISRLGFLDAGKERQVAVALGAEMRLKASSVDAPVSSLSGGNQQKVALAKWFHADCDLLILDEPTRGVDVGAKGEIYNLINDLAKAGKAILVISSEHQELFGICDRVLVMAEGAIVGELTESKFTEQQLLTLAMTRSARERDETSQ | Function: Part of an ABC transporter complex involved in carbohydrate import. Could be involved in ribose, galactose and/or methyl galactoside import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53666
Sequence Length: 501
Subcellular Location: Cell inner membrane
EC: 7.5.2.11
|
Q8U9B0 | MTATASALRMRGISKIFPGVKALSNVNFTVEYGRIHAVVGENGAGKSTLMKILSGSYAPTTGTTEIAGVEVQMRRPADAQKLGIRMVHQELNLVPDLTVAENIYLGRMPHRRFLVDRQAMLRKAAAVLKELEAAIDPKARLGDLPISQQQLVEIAKSYSADPRIIVLDEPTSSLSEHETTALFSILRKMKSQGIAIIYISHRLKEVLDIADDVTILRDGSMIDTRPAAGITAAEMIRLMVGREVANVFPKTPSKIGPVAFKVTGLSDGEKFHDVGFDVRSGEILGLTGLVGAGRTEVAQAIFGLAPLATGRIEINGKAVTIGSPAAAVKAGVAYVPEDRKGDGIVPSMSVRENISLPVLRRLSRLGRIGMSRDRGLAAKYTRDFSIVPPDPERRINLLSGGNQQKAIISRWLAAGPKVLILDEPTRGVDVGAKAEIHRIIGELVAGGMAVVMISSELPEVMGVCDRVVVMRDGRASSPIARGDLTEERIMALATGEEPA | Function: Part of an ABC transporter complex involved in carbohydrate import. Could be involved in ribose, galactose and/or methyl galactoside import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53477
Sequence Length: 499
Subcellular Location: Cell inner membrane
EC: 7.5.2.11
|
P49758 | MAQGSGDQRAVGVADPEESSPNMIVYCKIEDIITKMQDDKTGGVPIRTVKSFLSKIPSVVTGTDIVQWLMKNLSIEDPVEAIHLGSLIAAQGYIFPISDHVLTMKDDGTFYRFQAPYFWPSNCWEPENTDYAIYLCKRTMQNKARLELADYEAENLARLQRAFARKWEFIFMQAEAQVKIDRKKDKTERKILDSQERAFWDVHRPVPGCVNTTEMDIRKCRRLKNPQKVKKSVYGVTEESQAQSPVHVLSQPIRKTTKEDIRKQITFLNAQIDRHCLKMSKVAESLIAYTEQYVEYDPLITPAEPSNPWISDDVALWDIEMSKEPSQQRVKRWGFSFDEILKDQVGRDQFLRFLESEFSSENLRFWLAVQDLKKQPLQDVAKRVEEIWQEFLAPGAPSAINLDSHSYEITSQNVKDGGRYTFEDAQEHIYKLMKSDSYARFLRSNAYQDLLLAKKKGKSLAGKRLTGLMQSS | Function: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. The RGS6/GNB5 dimer enhances GNAO1 GTPase activity .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54423
Sequence Length: 472
Domain: The RGS domain interacts avidly with Galpha and mediates the acceleration of Galpha-mediated GTP hydrolysis.
Subcellular Location: Cytoplasm
|
Q9Z2H2 | MAQGSGDQRAVGIADPEESSPNMIVYCKIEDIITKMQDDKTGGVPIRTVKSFLSKIPSVVTGTDIVQWLMKNLSIEDPVEAIHLGSLIAAQGYIFPISDHVLTMKDDGTFYRFQAPYFWPSNCWEPENTDYAIYLCKRTMQNKARLELADYEAENLARLQRAFARKWEFIFMQAEAQVKIDRKKDKTERKILDSQERAFWDVHRPVPGCVNTTEMDIRKCRRLKNPQKVKKSVYGVTDETQSQSPVHIPSQPIRKTTKDDIRKQITFLNAQIDRHCLKMSKVAESLIAYTEQYVEYDPFITPAEPSNPWISDDITLWDIEMSKEPSQQRVKRWGFSFDEILKDQVGRDQFLRFLESEFSSENLRFWLSVQDLKKQPLQDVAKRVEEIWQEFLAPGAPSAINLDSHSYEITSQNVKDGGRYTFEDAQEHIYKLMKSDSYARFLRSNAYQDLLLAKKKGKSLAGKRLTGLMQSS | Function: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. The RGS6/GNB5 dimer enhances GNAO1 GTPase activity.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54531
Sequence Length: 472
Domain: The RGS domain interacts avidly with Galpha and mediates the acceleration of Galpha-mediated GTP hydrolysis.
Subcellular Location: Cytoplasm
|
P49801 | LAVQDLKKQPLQDVAKRVEEIWQEFLAPGAPSAINLDSHSYEITSQNVKDGGRYTFEDAQEHIYKL | Function: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. The RGS6/GNB5 dimer enhances GNAO1 GTPase activity.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7530
Sequence Length: 66
Domain: The RGS domain interacts avidly with Galpha and mediates the acceleration of Galpha-mediated GTP hydrolysis.
Subcellular Location: Cytoplasm
|
P49802 | MAQGNNYGQTSNGVADESPNMLVYRKMEDVIARMQDEKNGIPIRTVKSFLSKIPSVFSGSDIVQWLIKNLTIEDPVEALHLGTLMAAHGYFFPISDHVLTLKDDGTFYRFQTPYFWPSNCWEPENTDYAVYLCKRTMQNKARLELADYEAESLARLQRAFARKWEFIFMQAEAQAKVDKKRDKIERKILDSQERAFWDVHRPVPGCVNTTEVDIKKSSRMRNPHKTRKSVYGLQNDIRSHSPTHTPTPETKPPTEDELQQQIKYWQIQLDRHRLKMSKVADSLLSYTEQYLEYDPFLLPPDPSNPWLSDDTTFWELEASKEPSQQRVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIKEVPSRVQEIWQEFLAPGAPSAINLDSKSYDKTTQNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQELLQAKKKSGNSMDRRTSFEKFAQNVGRNIPIFPCHKNCTPTLRASTNLL | Function: GTPase activator component of the RGS7-GNB5 complex that regulates G protein-coupled receptor signaling cascades . The RGS7-GNB5 complex acts as an inhibitor signal transduction by promoting the GTPase activity of G protein alpha subunits, such as GNAO1, thereby driving them into their inactive GDP-bound form . May play a role in synaptic vesicle exocytosis (Probable). Glycine-dependent regulation of the RGS7-GNB5 complex by GPR158 affects mood and cognition via its ability to regulate neuronal excitability in L2/L3 pyramidal neurons of the prefrontal cortex (By similarity). Modulates the activity of potassium channels that are activated by GNAO1 in response to muscarinic acetylcholine receptor M2/CHRM2 signaling .
PTM: Palmitoylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57668
Sequence Length: 495
Subcellular Location: Cytoplasm
|
P57771 | MAALLMPRRNKGMRTRLGCLSHKSDSCSDFTAILPDKPNRALKRLSTEEATRWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTRSTAKLVSKAHRIFEEFVDVQAPREVNIDFQTREATRKNLQEPSLTCFDQAQGKVHSLMEKDSYPRFLRSKMYLDLLSQSQRRLS | Function: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2 (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form . Modulates the activity of potassium channels that are activated in response to DRD2 and CHRM2 signaling (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20917
Sequence Length: 180
Subcellular Location: Cell membrane
|
Q95K68 | MAALLMPRRNKGMRTRLGCLSHKSDSCSDFTAILPDKPNRALNYLRMYKFTATELQESRRLSTEEATRWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTRSTAKLVSKAHRIFEEFVDVQAPREVNIDFQTREATRKNMQEPSLTCFDQAQGKVHSLMEKDSYPRFLRSKMYLDLLSQSQRRLS | Function: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Modulates the activity of potassium channels that are activated in response to DRD2 and CHRM2 signaling.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22939
Sequence Length: 196
Subcellular Location: Cell membrane
|
Q8FBE0 | MTTQLEQAWELAKQRFAAVGIDVEEALRQLDRLPVSMHCWQGDDVSGFENPEGSLTGGIQATGNYPGKARNASELRADLEQAMRLIPGPKRLNLHAIYLESDTPVARDQIKPEHFKNWVEWAKTNQLGLDFNPSCFSHPLSADGFTLSHADDSIRQFWIDHCKASRRVSAYFGEQLGTPSVMNIWIPDGMKDITVDRLAPRQRLLAALDEVISEKLDPAHHIDAVESKLFGIGAESYTVGSNEFYMGYATSRQTALCLDAGHFHPTEVISDKISAAMLYVPQLLLHVSRPVRWDSDHVVLLDDETQAIASEIVRHDLFDRVHIGLDFFDASINRIAAWVIGTRNMKKALLRALLEPTAELRKLEAAGDYTARLALLEEQKSLPWQAVWKMYCQRHDTPAGSEWLENVRAYEKEILSRRG | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the interconversion of L-rhamnose and L-rhamnulose.
Catalytic Activity: L-rhamnopyranose = L-rhamnulose
Sequence Mass (Da): 47241
Sequence Length: 419
Pathway: Carbohydrate degradation; L-rhamnose degradation; glycerone phosphate from L-rhamnose: step 1/3.
Subcellular Location: Cytoplasm
EC: 5.3.1.14
|
Q9KCM0 | MNYSLAVDIGASSGRLIVGECNKKIQLTEIHRFENQIIEKNGQFCWDVDALFSEIKTGLKKCREAGIEPVSMGIDTWAVDFVLLDEHDKPLTDAVSYRDPRTDGVMEEVIEQFMKERLYLETGIQFQQFNTIYQLYALKKQHPDIFKKAKSFLMIPDYFHFLLTGKKANEYTNATTTQLVNAFTKKWDKDIIEALGFNPDMFQEIKLPTESLGKLKSEWVEEVGFDLEVILPATHDTGSAVVAVPKVADTIYLSSGTWSLIGVENSFPICVTKALDYNFTNEGGMNYQFRFLKNIMGLWMIQEVRRNYDNRYSFAQLVELSKGISFKSTVDVNDPRFLKPTNMIKEIQRYCQETGQQAPELPGEVAKCVFESLAESYTSAVAEIEDIFEKDFKSINVIGGGCRNELLNQLIADRTKKDVFAGPIEATAIGNLVAQWMALGEIESIQQARKLIYDSFDVKRYVSADRE | Function: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate.
Catalytic Activity: ATP + L-rhamnulose = ADP + H(+) + L-rhamnulose 1-phosphate
Sequence Mass (Da): 53111
Sequence Length: 467
Pathway: Carbohydrate degradation; L-rhamnose degradation; glycerone phosphate from L-rhamnose: step 2/3.
EC: 2.7.1.5
|
Q8Y3I6 | MKHYVAVDIGASSGRLILGKLVNEKLQLEEIHRFKNGFTYRDGHERWEIDQLMQEIFIGLEKVKQLGISECVLGIDTWGVDYVLIGASGEKLADPISYRDKRTLNAVQNLTSEYPREYIYKKTGIQFMELNTLYQLYVEERDLLERAEKILLIPDYIGYVLTGVKVAETTNSSTTQMLNLREQLFDKDLLSHLNIDVEKFAPLTDAGTYLGEVKEDWLKMYDIPNCDVVTVATHDTASAVVGTPAEGENWAFLSSGTWSLIGMELSAPINNEVAFKENYTNEWGAYGTYRFLKNIMGLWIVQEIARMDDYKHSFAEMAEEAGNYPYFKQIINVNDARFNNPENMVDEIRLYCRETGQTVPETIGELTNCVYGSLALYYALELEKMTEITGKKIEKLYIVGGGSNVAMLNQLTAKLAGIEVFAGPSEATAIGNLVVQMINQGEIESMRAGRKIIRNSFEIGEFSCGDVRFEEIKERFTKVLEFN | Function: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate.
Catalytic Activity: ATP + L-rhamnulose = ADP + H(+) + L-rhamnulose 1-phosphate
Sequence Mass (Da): 54757
Sequence Length: 483
Pathway: Carbohydrate degradation; L-rhamnose degradation; glycerone phosphate from L-rhamnose: step 2/3.
EC: 2.7.1.5
|
Q8ESX1 | MQQCNLAVDIGASSGRVIAGYLQNGKLQLEEVHRFDNKLIDLNNYFCWDIDRIYQEILMGIKSAVDNGYQPISLGIDTWAVDFVLLDENDMRLTDAVSYRDPRTDGMMEEVFSQISKERLYLETGIQFQKFNTMYQLQALKNSNPDLIEKATSFLMIPDYLNFLLTGKKVNEYTNATTTQLVNAFTKKWDIDLIEQLGFNSNMFMDIQPPESVIGNLRPELQEELGVDFNVILPATHDTGSAVVAVPEQENSIYISSGTWSLIGVENHFPICTTKALDYNFTNEGGADYRYRFLKNIMGLWMIQEVKRNFNDEFEFADFAAMAKGESFKSIVDVDDDRFLKPENMIEEIKAYCKETNQAIPQSPSEVAKCVFNSLAVSYQQAISQIEEIYEIDFPTIYVIGGGSKNEMLNQLIADTTGKTVIAGLSEATAIGNLIVQMMAIDQIDDMQQARQIIKHSFDLYTYAKVTMEG | Function: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate.
Catalytic Activity: ATP + L-rhamnulose = ADP + H(+) + L-rhamnulose 1-phosphate
Sequence Mass (Da): 53267
Sequence Length: 470
Pathway: Carbohydrate degradation; L-rhamnose degradation; glycerone phosphate from L-rhamnose: step 2/3.
EC: 2.7.1.5
|
Q9UBD6 | MAWNTNLRWRLPLTCLLLQVIMVILFGVFVRYDFEADAHWWSERTHKNLSDMENEFYYRYPSFQDVHVMVFVGFGFLMTFLQRYGFSAVGFNFLLAAFGIQWALLMQGWFHFLQDRYIVVGVENLINADFCVASVCVAFGAVLGKVSPIQLLIMTFFQVTLFAVNEFILLNLLKVKDAGGSMTIHTFGAYFGLTVTRILYRRNLEQSKERQNSVYQSDLFAMIGTLFLWMYWPSFNSAISYHGDSQHRAAINTYCSLAACVLTSVAISSALHKKGKLDMVHIQNATLAGGVAVGTAAEMMLMPYGALIIGFVCGIISTLGFVYLTPFLESRLHIQDTCGINNLHGIPGIIGGIVGAVTAASASLEVYGKEGLVHSFDFQGFNGDWTARTQGKFQIYGLLVTLAMALMGGIIVGLILRLPFWGQPSDENCFEDAVYWEMPEGNSTVYIPEDPTFKPSGPSVPSVPMVSPLPMASSVPLVP | Function: Ammonium transporter involved in the maintenance of acid-base homeostasis. Transports ammonium and its related derivative methylammonium across the plasma membrane of epithelial cells likely contributing to renal transepithelial ammonia transport and ammonia metabolism. Postulated to primarily mediate an electroneutral bidirectional transport of NH3 ammonia species according to a mechanism that implies interaction of an NH4(+) ion with acidic residues of the pore entry followed by dissociation of NH4(+) into NH3 and H(+). As a result NH3 transits through the central pore and is protonated on the extracellular side reforming NH4(+) . May act as a CO2 channel providing for renal acid secretion .
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Sequence Mass (Da): 53179
Sequence Length: 479
Subcellular Location: Cell membrane
|
Q9QXP0 | MAWNTNLRGRLPITCLILQVTMVVLFGVFVRYDIQADAHWWLEKKRKNISSDVENEFYYRYPSFQDVHAMVFVGFGFLMTFLQRYGFSAVGFNFLLAAFGIQWALLMQGWFHYFEEGHIVLSVENIIQADFCVASSCVAFGAVLGKVSPMQLLIMTFFQVTLFTVNEFILLNLIEAKDAGGSMTIHTFGAYFGLTVTWILYRKNLDQSKQRQSSVYHSDLFAMIGTLFLWIYWPSFNSASSFHGDAQHRAALNTYLSLAASVLTTVTVSSIVHKKGKLDMVHIQNATLAGGVGVGTAAEMMLTPYGALIVGFFCGIFSTLGFAYLTPFLESRHRIQDTCGIHNLHGIPGIIGGIVGAVTAAYSSPDVYGEPGIVHSFGFGSYKMDWNKRMQGRSQIFGLLLSLAMALVGGIIVGFILKLPFWGQAADENCFEDSIYWEVHEEVNTVYIPEDLAHKHSTSLVPAMPLVLPTTSASIVPPVPPTPPVSLATSAPSAALVH | Function: Ammonium transporter involved in the maintenance of acid-base homeostasis. Transports ammonium and its related derivative methylammonium across the plasma membrane of epithelial cells likely contributing to renal transepithelial ammonia transport and ammonia metabolism. Postulated to primarily mediate an electroneutral bidirectional transport of NH3 ammonia species according to a mechanism that implies interaction of an NH4(+) ion with acidic residues of the pore entry followed by dissociation of NH4(+) into NH3 and H(+). As a result NH3 transits through the central pore and is protonated on the extracellular side reforming NH4(+) (By similarity). May act as a CO2 channel providing for renal acid secretion (By similarity).
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Sequence Mass (Da): 54972
Sequence Length: 498
Subcellular Location: Apical cell membrane
|
Q8RJP2 | MHMNKPLQAWRTPLLTLIFVLPLTATGAVKLTLDGMNSTLDNGLLKVRFGADGSAKEVWKGGTNLISRLSGAARDPDKNRSFYLDYYSGGVNEFVPERLEVIKQTPDQVHLAYIDDQNGKLRLEYHLIMTRDVSGLYSYVVAANTGSAPVTVSELRNVYRFDATRLDTLFNSIRRGTPLLYDELEQLPKVQDETWRLPDGSVYSKYDFAGYQRESRYWGVMGNGYGAWMVPASGEYYSGDALKQELLVHQDAIILNYLTGSHFGTPDMVAQPGFEKLYGPWLLYINQGNDRELVADVSRRAEHERASWPYRWLDDARYPRQRATVSGRLRTEAPHATVVLNSSAENFDIQTTGYLFSARTNRDGRFSLSNVPPGEYRLSAYADGGTQIGLLAQQTVRVEGKKTRLGQIDARQPAPLAWAIGQADRRADEFRFGDKPRQYRWQTEVPADLTFEIGKSRERKDWYYAQTQPGSWHILFNTRTPEQPYTLNIAIAAASNNGMTTPASSPQLAVKLNGQLLTTLKYDNDKSIYRGAMQSGRYHEAHIPLPAGALQQGGNRITLELLGGMVMYDAITLTETPQ | Function: Degrades the rhamnogalacturonan I (RG-I) backbone of pectin. Is required for the full virulence of E.chrysanthemi strain 3937 as it is involved in rotting of plant tissue.
Catalytic Activity: Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.
Sequence Mass (Da): 64978
Sequence Length: 578
Subcellular Location: Secreted
EC: 4.2.2.23
|
Q58DK7 | MSADDGGIRAAQDKERARETPGHGHSCQEMLSESEGTVPLGEAWESPHIKMEPEEPHPEGVSQETRAEGARGWVPLSQGTKEKVCFLPGGALPAPQTPVLSREGRTRDRQMAAALLTAWSQMPVTFEDMALYLSREEWGRLDHTQQSFYREVLQKRSGLSLGFPFSRPFWASQVQGKGEAPGSSRQLGHEEEEKRGVVEVDKEELAASLGALGDAKSFKSRMGRAQGEAPRCGQRAASGQNSGPAKDDVQPCPVKEAQLESAPPDTDLPKTQEGHFPEQPREGGTAAPESSEEGLALDSEAGKKTYKCEQCGKAFSWHSHLVTHRRTHTGEKPYACTDCGKRFGRSSHLIQHQIIHTGEKPYTCPSCWKSFSHHSTLIQHQRIHTGEKPYVCDRCAKRFTRRSDLVTHQGTHTGAKPHKCPICGKCFTQSSALVTHQRTHTGVKPYPCPECGKCFSQRSNLIAHNRTHTGEKPYHCLDCGKSFSHSSHLTAHQRTHRGVRPYSCPLCGKSFSRRSNLHRHEKIHTAGPKALAMLMLGAAGTLAAPPPAPT | Function: Transcriptional repressor involved in regulating MPV17L expression. By regulating MPV17L expression, contributes to the regulation of genes involved in H(2)O(2) metabolism and the mitochondrial apoptotic cascade.
Sequence Mass (Da): 60459
Sequence Length: 550
Domain: The KRAB domain is required for transcriptional repression.
Subcellular Location: Nucleus
|
O95201 | MSADGGGIQDTQDKETPPEVPDRGHPHQEMPSKLGEAVPSGDTQESLHIKMEPEEPHSEGASQEDGAQGAWGWAPLSHGSKEKALFLPGGALPSPRIPVLSREGRTRDRQMAAALLTAWSQMPVTFEDVALYLSREEWGRLDHTQQNFYRDVLQKKNGLSLGFPFSRPFWAPQAHGKGEASGSSRQAGDEKEWRGACTGAVEVGQRVQTSSVAALGNVKPFRTRAGRVQWGVPQCAQEAACGRSSGPAKDSGQPAEPDRTPDAAPPDPSPTEPQEYRVPEKPNEEEKGAPESGEEGLAPDSEVGRKSYRCEQCGKGFSWHSHLVTHRRTHTGEKPYACTDCGKRFGRSSHLIQHQIIHTGEKPYTCPACRKSFSHHSTLIQHQRIHTGEKPYVCDRCAKRFTRRSDLVTHQGTHTGAKPHKCPICAKCFTQSSALVTHQRTHTGVKPYPCPECGKCFSQRSNLIAHNRTHTGEKPYHCLDCGKSFSHSSHLTAHQRTHRGVRPYACPLCGKSFSRRSNLHRHEKIHTTGPKALAMLMLGAAAAGALATPPPAPT | Function: Transcriptional repressor involved in regulating MPV17L expression . By regulating MPV17L expression, contributes to the regulation of genes involved in H(2)O(2) metabolism and the mitochondrial apoptotic cascade .
Sequence Mass (Da): 60630
Sequence Length: 554
Domain: The KRAB domain is required for transcriptional repression.
Subcellular Location: Nucleus
|
Q51559 | MRRESLLVSVCKGLRVHVERVGQDPGRSTVMLVNGAMATTASFARTCKCLAEHFNVVLFDLPFAGQSRQHNPQRGLITKDDEVEILLALIERFEVNHLVSASWGGISTLLALSRNPRGIRSSVVMAFAPGLNQAMLDYVGRAQALIELDDKSAIGHLLNETVGKYLPQRLKASNHQHMASLATGEYEQARFHIDQVLALNDRGYLACLERIQSHVHFINGSWDEYTTAEDARQFRDYLPHCSFSRVEGTGHFLDLESKLAAVRVHRALLEHLLKQPEPQRAERAAGFHEMAIGYA | Function: Required for rhamnolipid surfactant production . Supplies the acyl moieties for rhamnolipid biosynthesis by competing with the enzymes of the type II fatty acid synthase (FASII) cycle for the beta-hydroxyacyl-acyl carrier protein (ACP) pathway intermediates. Catalyzes the formation of one molecule of beta-hydroxydecanoyl-beta-hydroxydecanoate from two molecules of beta-hydroxydecanoyl-ACP. Is the only enzyme required to generate the lipid component of rhamnolipid. In vitro results establish that RhlA is highly selective for 10-carbon acyl-ACP intermediates and thus functions as the molecular ruler that controls the acyl chain composition of rhamnolipids. Cannot use beta-hydroxydecanoyl-CoA as substrate . Rhamnolipid production plays an important role in swarming motility .
Catalytic Activity: 2 (3R)-hydroxydecanoyl-[ACP] + H2O = (3R)-3-[(3R)-3-hydroxydecanoyloxy]decanoate + H(+) + 2 holo-[ACP]
Sequence Mass (Da): 32963
Sequence Length: 295
Pathway: Lipid metabolism; rhamnolipid biosynthesis.
EC: 2.3.1.-
|
Q22038 | MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAKTKDGIREVFEKATQAALQQKKKKKSKCMIL | Function: Required for ventral migration of epidermal cells during ventral enclosure in the embryo and for cell elongation . Also required for ventral migration of P cells during larval development . Involved in asymmetric spindle positioning during anaphase and establishment of cell polarity during embryo development . In adults, involved in regulation of multiple processes including locomotion, pharyngeal pumping, fecundity, ovulation, defecation and body morphology . In body wall muscles, regulates organization of myosin thick filaments downstream of unc-89 . Association with the oxidase bli-3 promotes ROS production and this interaction may be modulated by memo-1, in order to control the oxidative stress response and longevity .
Location Topology: Lipid-anchor
Sequence Mass (Da): 21635
Sequence Length: 192
Subcellular Location: Cell membrane
|
P31021 | MLAFSDMNTGAGKIENGKKALKIVVVGDGAVGKTCLLLAFSKGEIPTAYVPTVFENFSHVMKYKNEEFILHLWDTAGQEEYDRLRPLSYADSDVVLLCFAVNNRTSFDNISTKWEPEIKHYIDTAKTVLVGLKVDLRKDGSDDVTKQEGDDLCQKLGCVAYIEASSVAKIGLNEVFEKSVDCIFSNKPVPKASVTTQAKSQESTQQKKKSKCLLQ | Function: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states . Involved in actin cytoskeleton remodeling . Regulates phagocytosis by modulating actin cytoskeleton dynamics through the recruitment of formin1 and profilin1 to the phagocytosis nucleation site .
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 23767
Sequence Length: 215
Domain: The switch 1 and switch 2 motifs undergo large conformational changes during GTP/GDP cycle and play important roles in the interaction with downstream effectors.
Subcellular Location: Cell membrane
EC: 3.6.5.2
|
Q35638 | MSASRFIKCVTVGDGAVGKTCLLISYTSNTFPTDYVPTVFDNFSANVVVNGSTVNLGLWDTAGQEDYNRLRPLSYRGADVFILAFSLISKASYENVSKKWIPELKHYAPGVPIILVGTKLDLRDDKQFFVDHPGAVPITTAQGEELRKLINAPAYIECSSKSQQNVKAVFDAAIRVVLQPPKQKKKKSKAQKACSIL | Function: Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation (By similarity). May be involved in cell polarity control during the actin-dependent tip growth of pollen tubes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21630
Sequence Length: 197
Subcellular Location: Cytoplasm
|
Q09914 | MATELRRKLVIVGDGACGKTCLLIVFSKGTFPEVYVPTVFENYVADVEVDGRHVELALWDTAGQEDYDRLRPLSYPDSHVILICFAVDSPDSLDNVQEKWISEVLHFCSSLPILLVACKADLRNDPKIIEELSKTNQHPVTTEEGQAVAQKIGAYKYLECSAKTNEGVREVFESATRAAMLKHKPKVKPSSGTKKKKRCILL | Function: Involved in the regulation of cell wall growth and actin cytoskeleton organization. Activates (1,3)-beta-D-glucan synthase.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22523
Sequence Length: 202
Subcellular Location: Cell membrane
|
P06780 | MSQQVGNSIRRKLVIVGDGACGKTCLLIVFSKGQFPEVYVPTVFENYVADVEVDGRRVELALWDTAGQEDYDRLRPLSYPDSNVVLICFSIDLPDSLENVQEKWIAEVLHFCQGVPIILVGCKVDLRNDPQTIEQLRQEGQQPVTSQEGQSVADQIGATGYYECSAKTGYGVREVFEAATRASLMGKSKTNGKAKKNTTEKKKKKCVLL | Function: Acts as a central regulator in the cell wall integrity signaling pathway, which is regulated by the cell cycle and in response to various types of cell wall stress. Integrates signals from different cell surface sensors, and activates a set of effectors, regulating processes including beta-glucan synthesis at the site of wall remodeling, gene expression related to cell wall biogenesis, organization of the actin cytoskeleton, and protein- and secretory vesicle-targeting to the growth site. Activates the protein kinase C (PKC1) MAP kinase cascade, the beta-1,3-glucan synthase (FKS1), the formin BNI1, the exocyst component SEC3 and the transcription factor SKN7.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 23152
Sequence Length: 209
Subcellular Location: Cell membrane
EC: 3.6.5.2
|
P06781 | MSEKAVRRKLVIIGDGACGKTSLLYVFTLGKFPEQYHPTVFENYVTDCRVDGIKVSLTLWDTAGQEEYERLRPFSYSKADIILIGFAVDNFESLINARTKWADEALRYCPDAPIVLVGLKKDLRQEAHFKENATDEMVPIEDAKQVARAIGAKKYMECSALTGEGVDDVFEVATRTSLLMKKEPGANCCIIL | Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 21479
Sequence Length: 192
Subcellular Location: Cell membrane
EC: 3.6.5.2
|
O13928 | MSSCFGSKKKPIYRKIVILGDGAAGKTSLLNVFTKGYFPQVYEPTIFENYIHDIFVDGNSIELSLWDTAGQEEYDQLRSLSYSDTHVIMICFAVDSRDSLENVITKWLPEVSSNCPGVKLVLVALKCDLRGADEEQVDHSKIIDYEEGLAAAKKINAVRYLECSAKLNRGVNEAFTEAARVALAAQPRGTKDGADESHGTGCIIA | Function: Involved in controlling cell shape and septation . Regulates cell separation by modulating the function of the exocyst complex . Involved in post-Golgi vesicle transport . Involved in driving sexual development in a palmitoylation-dependent manner .
PTM: Palmitoylated by the erf2-erf4 complex.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22502
Sequence Length: 205
Subcellular Location: Cell membrane
|
Q00245 | MSFLCGSASTSNKPIERKIVILGDGACGKTSLLNVFTRGYFPEVYEPTVFENYIHDIFVDSKHITLSLWDTAGQEEFDRLRSLSYSDTQCIMLCFSIDSRDSLENVQNKWVGEITDHCEGVKLVLVALKCDLRNNENESNAITPNNIQQDNSVSNDNGNNINSTSNGKNLISYEEGLAMAKKIGALRYLECSAKLNKGVNEAFTEAARVALTAGPVATEVKSDSGSSCTIM | Function: Plays an important role in cell growth. Required to keep the uninucleated state. May be involved in the organization of the cytoskeleton which affects microtubule functions. Most likely RHO3 and RHO4 of S.cerevisiae regulate partially overlapping but different pathways.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25312
Sequence Length: 231
Subcellular Location: Cell membrane
|
P50861 | MAVKGLGKPDQVYDGSKIRVGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFVDRQAKLGKPLDVVIPIGVLIKGSTMHFEYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGIDEAHSMHNHGEDWGAAAVEMAVKFGKNAF | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 18556
Sequence Length: 169
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
Subcellular Location: Mitochondrion intermembrane space
EC: 2.5.1.78
|
O66747 | MERPYVIIVSEVSVDGKLTLYRGASSKELMSLMDEEAYKYLHEIRAKVDGIMVGCETVRTDNPSLTVRYAKGKNPVRIIPCSTANVPLDANVLNTKEAPTIIATTERAPKERLEKIKELGAEVIVVGDELVDFDKLLPELYRRGIKSLMVEGGASINWEFVRRRVVDEIRLIHLPVIVGGENVPTLVGGEGFKKLKNLLHLRLRSHFVRGKQLITEWEVVNKIR | Function: Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADPH
Sequence Mass (Da): 25257
Sequence Length: 224
Pathway: Cofactor biosynthesis; riboflavin biosynthesis.
EC: 1.1.1.302
|
O28272 | MRPYVFVNVAASLDGKISDESRKQLRISCEEDLRIVDRLRAESDAIMVGIGTVLADDPRLTVKSAELREKRQKDGKEPNPLRVVVDSRCRVPLTARILNDEARTLVAVSRIAPEEKVREVKKVAEVAVFGEERVELSALLEFLHRKGVRRLMVEGGGTLISSLISQNLVDEIRIYYGPIFIGGRDSPTVCDGESFLKKCRIEKIERIGEGFAVTARFNR | Function: Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADPH
Sequence Mass (Da): 24578
Sequence Length: 219
Pathway: Cofactor biosynthesis; riboflavin biosynthesis.
EC: 1.1.1.302
|
Q6FU96 | MLRVRDDLPPFLKNYLPDGHRNGRPFVTLTYAQSIDAKIAKQRGVRTTISHIETKEMTHYLRYFHDGILIGSGTVLADDPGLNCKWIGPNNDPDESMEEKSPRPIILDPKLKWKYSGSKMEELCNQGMGKPPIVITTKTPKVKEANVEYMIMEPDANDRISWKSILDTLRRNYDMKSVMIEGGSHVINQLLMCSDLIDSLIVTIGSIYLGSEGVTVSPPDEVKLKDISWWKGTSDVVMCSRLQN | Function: Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADPH
Sequence Mass (Da): 27568
Sequence Length: 244
Pathway: Cofactor biosynthesis; riboflavin biosynthesis.
EC: 1.1.1.302
|
Q6BII9 | MSLLPLTPSLRPFLEEYLPRPCSNRPFVTLTYAQSLDSRIAAKPGEQTKISHLETKTMTHYIRSKHDGIMVGIGTVLADDPKLNCRFEAEDGNISTPRPIILDPTGKWAYHKSQLRSVCDNNKGLAPFILIDETVTPRNEDVEVLDKQDGAFVRLPLLRNADKVGNWNIILKKLFQLGIKSIMVEGGASIINDLLVYSKIIDSLIITIGPVFLGKDGVEVSPSGHAGLIDVKWWQGIQDSVLCARLT | Function: Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADPH
Sequence Mass (Da): 27372
Sequence Length: 247
Pathway: Cofactor biosynthesis; riboflavin biosynthesis.
EC: 1.1.1.302
|
Q58085 | MVMVMEKKPYIISNVGMTLDGKLATINNDSRISCEEDLIRVHKIRANVDGIMVGIGTVLKDDPRLTVHKIKSDRNPVRIVVDSKLRVPLNARVLNKDAKTIIATTEDTNEEKEKKIKILEDMGVEVVKCGRGKVDLKKLMDILYDKGIKSILLEGGGTLNWGMFKEGLVDEVSVYIAPKIFGGKEAPTYVDGEGFKTVDECVKLELKNFYRLGEGIVLEFKVKK | Function: Catalyzes an early step in riboflavin biosynthesis, the NAD(P)H-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate. The beta anomer is the authentic substrate, and the alpha anomer can serve as substrate subsequent to spontaneous anomerization. NADPH and NADH function equally well as the reductants. Does not catalyze the reduction of 5-amino-6-(5-phospho-D-ribosylamino)uracil to 5-amino-6-(5-phospho-D-ribitylamino)uracil.
Catalytic Activity: 2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADPH
Sequence Mass (Da): 25037
Sequence Length: 224
Pathway: Cofactor biosynthesis; riboflavin biosynthesis.
EC: 1.1.1.302
|
O26337 | MRPYVILNAAMTLDGKIATATGSSEISGEEDLRRVHELRRECDAIMVGINTVLADDPRLTVHRVDAAPGDNPVRVVVDSMARTPPHFRVLNDEAPTVIGVSESAPPERVAELRKRAEVVVAGTRRVDLHLLLERLHGMGIERLMLEGGSTLNYSMLTGGLVDEVRVCIAPMIVGGRDARTLVDGEGIDEMADAIRLELKRSYTLGEDLIVEYTVKG | Function: Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADPH
Sequence Mass (Da): 23576
Sequence Length: 216
Pathway: Cofactor biosynthesis; riboflavin biosynthesis.
EC: 1.1.1.302
|
P95872 | MVMKPYVIIFSTVSIDGRLATKTGYSELSCPYDKQRQHEIRSEVDAVMVGANTVRVDNPSLTVKYGKNRRNPIRVVVTRSFNLDPSYKIFTTPPSTVIYTSNYESEKVEEFIRKGVIVRKFLHLDDLLEDLYDNFNVRRLMVEGGGHLIWWFIKDNLYDEIRITISPRIFGNGVSFTQGEGFIGEDSPRLELIDAKICECGNEVHLTYKKYMT | Function: Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADPH
Sequence Mass (Da): 24561
Sequence Length: 213
Pathway: Cofactor biosynthesis; riboflavin biosynthesis.
EC: 1.1.1.302
|
Q9P7L3 | MESSQAYFPPSANKKHVLLTWAQSINGRIGYVVESPSLGQLRLSSKESFVMTHLLRTKFDGIMVGSRTAENDNPSLTAKLPDPANPDCLLPLNKQPIPIIVDSNLRLDYASLKVIRLARERLGKPPLIIVAPSIWQQVQHDSKLKEAVKLIQSVGGRCIIRNEDSPDSWSDYVALDKLLQNGVNRIMVEGGAELLAKAFGSTDIDAYVVTIVPKIFSCSNTTEIKNLNNLNLTTNSHWYPCGPDVIFTNYSDEFYESYKSLLTNSDAI | Function: Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADPH
Sequence Mass (Da): 29752
Sequence Length: 268
Pathway: Cofactor biosynthesis; riboflavin biosynthesis.
EC: 1.1.1.302
|
P33312 | MSLTPLCEDLPQFLQNYLPNAGQTENTIVPFVTLTYAQSLDARVSRGPGVRTTISHPETKTMTHYLRHHHDGILVGSGTVLADNPGLNCKWGPDPAANSPRPIIIDTKQKWRFDGSKMQELFIKRQGKPPIVVVTSEPIIKEQHVDYAICPINDTTKLVDWKKLFEILKEEFNIRSVMVEGGANVINQLLLRSDIVNSLIITIGSTFLGSSGTEVSPPQTVNLKDMSWWKGITDVVLCARLADD | Function: Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADPH
Sequence Mass (Da): 27116
Sequence Length: 244
Pathway: Cofactor biosynthesis; riboflavin biosynthesis.
EC: 1.1.1.302
|
P47924 | MSSINLSSSSPSTISLSRSRLSQSSTTLLHGLHRVTLPSNHPLSTFSIKTNTGKVKAAVISREDDLLSFTNGNTPLSNGSLIDDRTEEPLEADSVSLGTLAADSAPAPANGFVAEDDDFELDLPTPGFSSIPEAIEDIRQGKLVVVVDDEDRENEGDLVMAAQLATPEAMAFIVRHGTGIVCVSMKEDDLERLHLPLMVNQKENEEKLSTAFTVTVDAKHGTTTGVSARDRATTILSLASRDSKPEDFNRPGHIFPLKYREGGVLKRAGHTEASVDLTVLAGLDPVGVLCEIVDDDGSMARLPKLREFAAENNLKVVSIADLIRYRRKRDKLVERASAARIPTMWGPFTAYCYRSILDGIEHIAMVKGEIGDGQDILVRVHSECLTGDIFGSARCDCGNQLALSMQQIEATGRGVLVYLRGHEGRGIGLGHKLRAYNLQDAGRDTVEANEELGLPVDSREYGIGAQIIRDLGVRTMKLMTNNPAKYVGLKGYGLAIVGRVPLLSLITKENKRYLETKRTKMGHMYGLKFKGDVVEKIESESES | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Involved in riboflavin biosynthesis. Catalyzes both the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate and the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate. RIBA2 and RIBA3 together are not able to complement the loss of function of RIBA1.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 59056
Sequence Length: 543
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Subcellular Location: Plastid
|
Q6NLQ7 | MASLTLRCDSTHLLPSRDVVKGTKPFGTSLVYPRIISKKFNVRMRVIPEEGDVFSSSKSNGSSMGIELQPDLVSFGTLAAEMIPTTMDSPEVEDEEFDLDRPTDGFASIPQAIEDIRHGKMVVVVDDEDRENEGDLIMAASLATPEAMAFVVKHGTGIVCVSMKGEDLERLELPLMVTRKDNEEKLRTAFTVSVDAKKGTSTGVSARDRAQTILTLASKDSKPEDFNRPGHIFPLRYREGGVLKRAGHTEASVDLTVLAGLEPVSVLCEIVDDDGSMARLPRLRQFAQENNLKLISIADLIRYRRKRERLVEFTAVAPIPTMWGPFKAHCFKSLLDGVEHIAMVKGEIGDGKDILVRVHAECITDDIFGNSSGGKQLAIAMRLIEENGRGVFVYLRGPESKGIDLSHKPRTYNTNSDQAEGVSFPVASREYGIGAQILRDLGVREMKVMTNNPAHYVGLKGYGLSISGKVPLITTP | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Involved in riboflavin biosynthesis. Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate. RIBA2 and RIBA3 together are not able to complement the loss of function of RIBA1.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 52200
Sequence Length: 476
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Subcellular Location: Plastid
|
Q9FN89 | MMDSALYHPRIFFAHSFINGLYSSPRFANTCWRLVSRSSWEIKASENSDRNVFDENPVRKTDGSLFDSASFETVDAEITPETDDFFVSDAEGDPDCPTQGYSSIELALQALRKGKFVIVVDDETGDVEGNLIMAATLTSPKDIAFLIKNGSGIVSVGMKKENLERLSLTLMSPEMEDEDSSAPTFTITVDAKSGTSTGVSASDRAMTVLALSSLDAKPDDFRRPGHVFPLKYRDGGVLRRAGHTEASVDLMILAGLRPLSVLSAILDQEDGSMASLPYMKKLATEHDIPIVSLTDLIRYRRKRDKLVERITVSRLPTKWGLFQAYCYRSKLDGTENIALVKGNVGNGEDILVRVHSECLTGDIFGSARCDCGNQLDLAMELIEKEGRGVVVYLRGHEGRGIGLGHKLRAYNLQDEGHDTVQANVELGLSIDSREYGIGAQMLRDIGVRTMRLMTNNPAKFTGLKGYGLAVVGRVPVVTPITKENRRYMETKRKKMGHIYISDNNDQPLA | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in riboflavin biosynthesis. Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate. RIBA2 and RIBA3 together are not able to complement the loss of function of RIBA1.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (Da): 56146
Sequence Length: 509
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
Subcellular Location: Plastid
|
O84736 | MFTCEAGIASVQQAIKDVAEGKFVIVIDAASRENEGDLILAGEKVSTEKMSFLLSHTTGIVCASLSREQAKSLDLPAMVQDNQCAFKTAFTVSVDASSGVTTGVSASDRTRTVQLLADPAATAESFVRPGHVFPLISQPGGAVQRPGHTEAAMDLMRLAGMQPCGIFAELVNPDHSMMRQQQVLAFAEQHDLTVITVDDLITYRYTYDSLVTKISSARLPTKYGDFSIHVYESIIDGTQHFALVKGDIHEQEAVPVRVHSECLTGDILGSCRCDCGAQLDMAMRYIAEEGLGVIVYLRGQEGRGIGFGHKIRAYALQDLGYDTVDANLQLGFPIDAREYGMAAQVLKDLQLTSVRLITHNPRKFFELQRLGIHVLDRIILPVSISTENEGYLRTKKERMGHWLDLPVLDDVEEEYETVERMSCR | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 46675
Sequence Length: 424
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
|
O24752 | MNAPLNSAVRLDSIEEAIADIAAGKAVVVVDNEDRENEGDLIFAAELATPELVAFMVRYSSGYICVPLLPEDCKRLNLPPMMGRNEDVRGTAYTVTVDANTGTTGISATSRAETMLRLADPMSVVDDFTRPGHVVPLAARPNGVLERDGHTEAAIDLARLAGLRPAGVLCEIVSEEDPTTMARSEELRRFSDEHDLKMISIEQLIEWRRHNETQVRRTVETQLPTDFGSFTALGYKHEIDGQEHVALIAGGVEELNGAEDVFVRVHSECLTGDVFHSRRCDCGQQLHQSMEIIQEAGQGIIIYLRGHEGRGIGLLAKLKAYSLQDSGLDTVDANLEQGLPEDAREYSVAGQILRDLGIKSANLLTNNPHKGEGLRGFGVEASAHTPVEIEPNADNIDYLRTKRDRMNHDLPQVARWDAAHALK | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 46399
Sequence Length: 423
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
|
A4QEG9 | MSEHEQAHSQLDSVEEAIADIAAGKAVVVVDDEDRENEGDIIFAAELATPELVAFMVRYSSGYICAPLTAKDADRLDLPPMTAHNQDARGTAYTVTVDANTGTTGISATDRAHTLRLLADPEADRTDFTRPGHVVPLRAREGGVLVRAGHTEAAVDLARAAGLRPAGVICEVVSEEDPTGMARVPELRRFCDEHDLKLISIEQLIEWRRKNEILVERQVETVLPTDFGTFKAVGYRSIIDGTELVAIVAGDVASDGGENVLVRVHSECLTGDVFGSRRCDCGQQLHESLRLIQEAGRGVVVYMRGHEGRGIGLLAKLRAYQLQDEGADTVDANLALGLPADAREFGTSAQILYDLGVRSLNLISNNPAKKVGLEGHGISIASRTPIPVAVHEDNVRYLKTKRDRMGHDLPDVALWEQEHPEN | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 45824
Sequence Length: 422
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
|
P0A5V1 | MTRLDSVERAVADIAAGKAVIVIDDEDRENEGDLIFAAEKATPEMVAFMVRYTSGYLCVPLDGAICDRLGLLPMYAVNQDKHGTAYTVTVDARNGIGTGISASDRATTMRLLADPTSVADDFTRPGHVVPLRAKDGGVLRRPGHTEAAVDLARMAGLQPAGAICEIVSQKDEGSMAHTDELRVFADEHGLALITIADLIEWRRKHEKHIERVAEARIPTRHGEFRAIGYTSIYEDVEHVALVRGEIAGPNADGDDVLVRVHSECLTGDVFGSRRCDCGPQLDAALAMVAREGRGVVLYMRGHEGRGIGLMHKLQAYQLQDAGADTVDANLKLGLPADARDYGIGAQILVDLGVRSMRLLTNNPAKRVGLDGYGLHIIERVPLPVRANAENIRYLMTKRDKLGHDLAGLDDFHESVHLPGEFGGAL | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 46017
Sequence Length: 425
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
|
A8ME45 | MDKQVNVVNYRELKKIPYILLLLQNGVNDHDFTRISVSDLSKQMGTTPQNISKVLRRLEREGYIVRSSVKGEVSVMLSEKGSALLRNLMDLMENLLGKNITIVLRGIVVTGFGEGSYYISLEGYRRQFISKLGFDPYPGTLNVKLLDQYMKYRLYLERVPGVRIEGFSNGSRTYGGVKAFKCTISDIPCGVLLIERTSHGPEVIEIVAPVKLRDRLGLKDGDDVTINILL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Mass (Da): 25887
Sequence Length: 230
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
EC: 2.7.1.161
|
Q6FM49 | MTVRDVDVPIPEQPGAPYPIVTKCCDIVCGFGRGSSELGIPTANVPVDQLPEVVNKLELGVYFGYAKVTPVAHDLEQVEREDGRVVSYNYGSHLEEDNGDLEVLPVVLSVGKNPFYHNDFKTVEIHILHDFKSTFYGAKIKFNILGYVRPELDYTSKEALIEDIKTDIEISKQVLDTEPYRAHMAELLK | Cofactor: Zinc or magnesium.
Function: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Mass (Da): 21196
Sequence Length: 189
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.
EC: 2.7.1.26
|
A0RTV6 | MGISQQAASQHLRELEDEGLITRNAEGKGISVMVTDKGRHELLRVYNILHDSLHSRPDHVEITGTLVSGMNEGAYYMSREGYTGQFQERLGYVPFPGTLNVDTDRKHGPEIARLDGMNGTIIDGFTDGKRSYGWVKCFAGTLNGTIPCHLIRLERTHHGSSTVELISKLDIRKETGLDDGGKITIRIPLEQED | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Mass (Da): 21446
Sequence Length: 193
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
EC: 2.7.1.161
|
O76206 | MLSQLPLFAGGEIVRGFGRGSKELGIPTANFPLEVVKSLPESLPTGAYYGWANVDNGPVHKMVLSIGWNPFYNNKEKSVETHMLHDFNCDLYGQTLKICIVGYLRPERSFDSLESLIAAIRGDIEQAKAFLDEADKAKLKEAPFFTEKLCSSK | Cofactor: Zinc or magnesium.
Function: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN).
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Mass (Da): 16986
Sequence Length: 153
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.1.26
|
Q5AW61 | MRPSNPRPPVTGPDSGPEAPFPIRLSGPVIKGFGRGSKELGIPTANIPVDGLEEVLPKELGVGVYYGVVALDPATAPAPSSSDSTSGDAAPILPAVLSIGYNPYYKNKTRSIEIHIMPSLTLPSPTAPSEEKEKVKFHKLPDFYGTKLNLLMLGYIRPEYDYVSMEALVEDIRIDCEVARASLLRPAYRVYLDGNEDETVSAQRDWLRSF | Cofactor: Zinc or magnesium.
Function: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Mass (Da): 22916
Sequence Length: 210
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.
EC: 2.7.1.26
|
Q5UY62 | MRTRGSRNWRSRASSGSGTRSWSIEATDRNLSQQCDVAEHVRQRVKLYPAQTVKRAFRTNPVSVSLRSKSGMHSTFGMLIRRESLLQRMAESTGQGVGRDELATLKLLALDGALDESTKVSCADLAERLDASNQTASRRLQRLEDAGLLARDIVSDGQEVELTGDGERRLQSEYADYRRIFESDASVDLTGVVTSGMGEGRHYITLPGYMEQFIERLGYEPFAGTLNLELTAESVRKRARMSAIEPVTIEGWEDDERTYGPAYCYPASIEGSDSEYEPAHVIAPERTHHGEEQLEVIAPEKLREVLELADGDEVIVHVSE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Mass (Da): 35682
Sequence Length: 320
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
EC: 2.7.1.161
|
Q9HNF4 | MSGATSTGDVGYDELAVLKLLALDGAHRGEVKVSCGDLASRLDASSQTASRRLQALDDADHVTRDLVSDGQWITVTDAGRHALKHEYEDYRRIFEDPGELALAGTVTSGMGEGRHYISLPGYNRQFAEKLGYEPYPGTLNVDLPPDGQRARAGIQALDGVDIDAWEDEDRTYGSATCYACTVVGDGTDFDGAHVIIPDRTHHDDDQLEIIAPVKLRERLGLLDDDEVTIRVEA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Mass (Da): 25356
Sequence Length: 233
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
EC: 2.7.1.161
|
Q18FC4 | MAESTTAVGHDELAALKFVALEGAHSEPIKISCSELSDRLDASSQTASRRLQRLEAAGYLDRDVVTDGQWVSLTKAGETALHKEYTQYQEIFGDNSSVVELTGTVTSGMGEGRHYISLSGYMKQFRERLGYEPFPGTLNIDLDDDSTRTRVAVSSLTGIQIDGWEDDERTFGPATCYPAEIILAEQTAEAAHIIVPERTHHDETQLEVIAPERLRDSLELTDGQRITVQLKPKE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Mass (Da): 25870
Sequence Length: 234
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
EC: 2.7.1.161
|
Q969G6 | MRHLPYFCRGQVVRGFGRGSKQLGIPTANFPEQVVDNLPADISTGIYYGWASVGSGDVHKMVVSIGWNPYYKNTKKSMETHIMHTFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRLELPEHLKIKEDNFFQVSKSKIMNGH | Cofactor: Zinc or magnesium.
Function: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), hence rate-limiting enzyme in the synthesis of FAD. Essential for TNF-induced reactive oxygen species (ROS) production. Through its interaction with both TNFRSF1A and CYBA, physically and functionally couples TNFRSF1A to NADPH oxidase. TNF-activation of RFK may enhance the incorporation of FAD in NADPH oxidase, a critical step for the assembly and activation of NADPH oxidase.
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Mass (Da): 17623
Sequence Length: 155
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.1.26
|
A2BK57 | MENGAVQQLQLLGKRVKGFGVGGRYVAHPYYSGRFRELLGCTPFPGTLNFDANLDWRELASMCEPQVIPGTVWDGVRLGAVYVWKAKIMTRHGYVDCAVIRPLLSGHPPTVLEIVACEKLEPILENNPDKTVIVTIACKRGDALRWRRY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Mass (Da): 16712
Sequence Length: 149
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
EC: 2.7.1.161
|
A8A9X7 | MLAALYYVLKGDPYKALKEDLESLKKAKLLTEDLRITEKGMELIQQLISKPISLKGKVVSGDGEGRYYLSLEGYRRQVREKLGFDPFPGTLNVLLDPTSTEKKSTLMFKRPIILKGFTENGKRYGEVLAFPARVSGVEAALVIPLKTHHPPEIIELISPVELRKALKLKDGDEVEVLVY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Mass (Da): 20113
Sequence Length: 179
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
EC: 2.7.1.161
|
A5E1A0 | MTRPETIIPEKPTSPYPIHTTAPIISGFGRGSSELGIPTANIPINAQLNSLPTGIYYGWCKIHPVSDQNDETRTRPDGQLILFNHGNKLQANELVVHPMVMSIGWNPFYQNKEKAAEIHIMSKFERDFYGAELEFIVLGYVRPELDYTTKEALIEDILTDIRISRDILENKEEYTKYKKELE | Cofactor: Zinc or magnesium.
Function: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Mass (Da): 20838
Sequence Length: 182
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.
EC: 2.7.1.26
|
A4QQ05 | MATARPSIVGPDSGPESPFPYKMEGKVISGFGRGSKELGIPTANLPVDATISPWISSISSGVYYGWASLQLPPSHPESPSSSSCSPYVVFPMVMSIGYNPFYNNTERSAEVHILHKFTADFYDAPMRLLILGFIRDEKNYDSLEALVKDINTDCDVARTSLDRKAWVPQGGLLHPAVDVREKQGDLDGSWLVRPNDSPSA | Cofactor: Zinc or magnesium.
Function: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Mass (Da): 21834
Sequence Length: 200
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.
EC: 2.7.1.26
|
A6UVI4 | MLNKLFGRVVSGKGEGKHYMSLPPYKEKFKNILGFEPYEGTLNVKLGYIINLNELNPIEVDDFYYKNNKYYGVKLIPVRICIKDYCVNGAIVYPKKTEHPNNVIELIAPIKLRKYLSLKNNYMVKIRL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Mass (Da): 14934
Sequence Length: 128
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
EC: 2.7.1.161
|
Q0W6F7 | MRSIMEVETLKRLALMGANKEQVSLSSSIFATSLGMSPQTAARRLSALEEDGYITRVVTPEGQKVRITEKGITCLKSEYRDYCSIFEDGGAPVMRGKVVTGLGEGQYYISLDGYRNQFNDKLGFDPYPGTLNVRLTEPFIPAEHEAVVIAGFKGENRTFGGCKCYPVRIKGVRAAIIRPDRTSYPPNLIEIIAPIKLRESLGLRDGDEVEVTLE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Mass (Da): 23670
Sequence Length: 214
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
EC: 2.7.1.161
|
Q8IXN7 | MCSQLWFLTDRRIREDYPQVQILRALRQRCSEQDVRFRAVLMDQIAVTIVGGHLGLQLNQKALTTFPDVVLVRVPTPSVQSDSDITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEPLGYPVVVKSTRGHRGKAVFLARDKHHLSDICHLIRHDVPYLFQKYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCSLGGVGVKCPLTEQGKQLAIQVSNILGMDFCGIDLLIMDDGSFVVCEANANVGFLAFDQACNLDVGGIIADYTMSLLPNRQTGKMAVLPGLSSPREKNEPDGCASAQGVAESVYTINSGSTSSESEPELGEIRDSSASTMGAPPSMLPEPGYNINNRIASELKLK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Catalyzes the synthesis of N-acetyl-L-aspartyl-L-glutamate (NAAG) and N-acetyl-L-aspartyl-L-glutamyl-L-glutamate.
Catalytic Activity: ATP + L-glutamate + N-acetyl-L-aspartate = ADP + H(+) + N-acetyl-L-aspartyl-L-glutamate + phosphate
Sequence Mass (Da): 42864
Sequence Length: 391
Subcellular Location: Cytoplasm
EC: 6.3.2.41
|
Q66HZ2 | MCSRVWFITDRRISQEYPQIQILRALKERCVEDDVEFRYLLMDEIVLTITDGQLGLRVGQEIVTSYPQVAVVRVPTPWVQSDSDITVLRHLEKMGCRLVNRPQAILNCVNKFWTFQELAGHGVPLPDTYSYGGHDNFRKMIDEAEPLGYPVVVKNARGHRGKAVFLARDKHHLSDLCHLIRHEAPYLFQEYVKESHGRDVRVVLVGGRVIGSMLRCSTDGRMQSNCSLGGVGMMCPLSEQGKQLAVQVCNILGMDVCGIDLLQKNDGSFVVCEANANVGFIAFDQACGMDVAGIVADFVLSLLPSRLSRKMSLLSVVSSTSETSSEPEVCIPTEVIIPSEVCIPNEICPLGTTCPIPDAMSTMSTSSTSSESEADLTETGPTPVGANPAYNINSLLASEMKLLTE | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Catalyzes the synthesis of beta-citryl-L-glutamate and N-acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized more efficiently than N-acetyl-L-aspartyl-L-glutamate.
Catalytic Activity: ATP + citrate + L-glutamate = ADP + beta-citrylglutamate + H(+) + phosphate
Sequence Mass (Da): 44500
Sequence Length: 405
Subcellular Location: Cytoplasm
EC: 6.3.1.17
|
Q80WS1 | MCSSVTGKLWFLTDRRIREDYPQKEILRALKAKCCEEELDFRAVVMDEMVLTVEQGNLGLRISGELISAYPQVVVVRVPTPWVQSDSDITVLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEAEVLEFPMVVKNTRGHRGKAVFLARDKHHLADLSHLIRHEAPYLFQKYIKESHGRDVRVIVVGGRVVGTMLRCSTDGRMQSNCSLGGVGMMCSLSEQGKQLAIQVSNILGTDVCGIDLLMKDDGSFCVCEANANVGFIAFDKACNLDVAGIIADYAASLLPAGRLTRRMSLLSVVSTASETSEPELGPPASAAVDNMSASSSSVDSDPESTTEREMLTKLPGGLFNMNQLLANEIKLLVE | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Catalyzes the synthesis of beta-citryl-L-glutamate and N-acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized more efficiently than N-acetyl-L-aspartyl-L-glutamate.
Catalytic Activity: ATP + citrate + L-glutamate = ADP + beta-citrylglutamate + H(+) + phosphate
Sequence Mass (Da): 42528
Sequence Length: 387
Subcellular Location: Cytoplasm
EC: 6.3.1.17
|
A4WNX8 | MTRTDRLCVGAIAGAFGVKGEVRLKSFCAEPSDIASYGPLFTEDGGRSFRVTLTRPVAGALGARLSGVATKEEADALRGVQLYADRDRLPSLGDDEFYHADLIGLEVRDTGGALLGRVHAVHNHGAGDILEVTGAGRREALLLPFTRAVVPTVDLSIGRIVADPPEGLE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 17822
Sequence Length: 169
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
Q11CR1 | METHMAKPKAPAGIENPVQLAVIGAAHGIKGEVRVKTFTEDPMALGSYGPLHMVDGRVLQVAAIRPAKEVVIVRFKGVDGRNAAEALNGEALFVDRSALPEKLEEEEFYYADLIGMAVLDEKGENLGRVVAVHNFGAGDLLEFRENSGPTVIIPFTRDAVPDIDLSNNTIRIDSITAGLDNAELSGEEDEAEGPESARGSRPRGPKSAGEPR | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 22668
Sequence Length: 212
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
A9WEK5 | MLWVVMDDLLYIGALGAPFGVRGQIRLHSISSHPEHLIRHLRTVFIGPKRVPHQVSRLYMHKPGLLIIQLQTITDRDAAADLRGEEVYIAAADAAPLAADEFFYHDVIGMQAVTDSGEDIGEVRDILETGAGEIVVITRRGRPDALVPMVRDFIVAIDVGERRLVIRPIAGLLD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19232
Sequence Length: 174
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
Q3B4A2 | MELWLTGIVLKPRGLKGEVKVKPVTDYPEKFLSRKSYWVGGSPGDAVPLAVKHASLAGGFAWLFLEGVDSREKAEALAGRQLFIEASEAEPRKDDRAWLHELEGMKVLGAGRKEVGVLKEVLSMPAHEVYEIISGGRSVLVPAIEEFVEEISLEGRYIHVPRFDEFL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18557
Sequence Length: 167
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
Q8KD89 | MELFLTGVVLKPKGLKGELKVKPVTDFPESFLTRREYYIGKTPEDAVLRKVQSARFHQGFAWLVFEGAGSREGAEALVGCGLYVTRDALVAMPDDRAYIHELIGLDVFDETEGRVGKISDVLQMPAHDVYEVDTGDRKVLIPAVEDFITETDLEKGMVRLKRFKEFL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18810
Sequence Length: 167
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
Q1QT49 | MSHETGGADTAQDDEHVVLGRLTSPYGVKGWLKVYSYTSPIEGIFEHAEWVLSKRGERRACKLSQGRPHGKGLVASLEGISSRELAEQWAGADILLPKQALPALAPGDYYWYQLEGLRVETLDGECLGQVNYLFETGANDVLVIRPSEASLDERERLLPFLPDDVIRQVDLDAGRMIVDWDPEF | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 20513
Sequence Length: 184
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
Q7NRV6 | MRDEDLVVMGFVRGAFGIKGWVKIHADTEYADGLFDYPTWWLGKNGSWKPYAFENGAVQPKALAAKLEGVDDRDAAEALRGTQIAIPRSELPEAGDGEYYWADLIGLSVVNQQGETLGKVDSLLETGANDVLVVKGGDGQQRLIPFVDQYVLEVVPAEGRILVDWGLDY | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18546
Sequence Length: 169
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
A8ANE1 | MSKQLTAQAPVEPIVLGKMGSSYGIRGWLRVFSSTEDAESIFDYQPWFIQKAGQWQQVQLESWKHHNQDLIIKLKGVDDRDSANLLTNCEIVVDSSQLPALEDGSYYWKDLMGCQVVTTEGYDLGKVVDMMETGSNDVIVIKANLKDAFGIKERLVPFLDGQVIKKVDLATRTIEVDWDPGF | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 20502
Sequence Length: 182
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.