ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P47500 | MDFDKQLFFNVEKIVELTEQLEKDLNKPNLSFEQIKVINKELKHKQPLIVKFKELQKLVENANEAEQILNNSSLKELHEEAKKELEKIKASLPSLEEEIKFLLLPVDENNQKNVIVEIRPAAGGDESCIFLSDLFNMYKNYCTSKNWTVELNEIIPASVGINFVSFAVNGTDVFAKLKFESGVHRVQRVPLTEAKGRVHTSTVTVAVLPQLEEVEITINPSDLRIDTYRASGAGGQHVNRTESAVRITHLPTGIVVACQEGKSQFSNRDKAMKMLRAKLWENAQNKQLSTQADLRKSQVGSGERAEKIRTYNYPQNRITD... | 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: Cytoplas... |
A9G9L1 | MLPIAKLEAVQRRFQELEHLMCSPAVLAAPAELQRLNRERTEIEPVVVAFARMRDVERRIAEDREALSDPDLSELAQAELPELELERERLAAELEVLLLPKDPNDTRNTVIEIRSGEGGEEAALFAADLFRMLCRYAETKRWKVEVLNLSEASAGGYKEVAALITGQDVYSHLRYEGGVHRVQRVPSTETQGRIHTSTATVAVLPEADEVDVHIDEKDLEISIAASGGPGGQGVNTTNSAVQIKHLPTGMIVKCQDERSQLKNKAKAMKVLRSRLLELEQRRQEEAQSAERRTMVGTGERAQKVRTYNFPQNRVTDHRIG... | 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-al... |
P37742 | MLTCFKAYDIRGKLGEELNEDIAWRIGRAYGEFLKPKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPISGDTGLRDVQRLAEANDFPPVDETKRGRYQQINLRDAYVDHLFGYINVKNLTPLKLVINSGNGAAGPVVDAIEARFKALGAPVELIKVHNTPDGNFPNGIPNPLLPECRDDTRNAVIKHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVTAAGTPVMSKTGHAFIKERMRKEDA... | 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... |
P37755 | MTQLTCFKAYDIRGELGEELNEDIAYRIGRAYGEFLKPGKIVVGGDVRLTSESLKLALARGLMDAGTDVLDIGLSGTEEIYFATFHLGVDGGIEVTASHNPMNYNGMKLVRENAKPISGDTGLRDIQRLAEENQFPPVDPARRGTLRQISVLKEYVDHLMGYVDLANFTRPLKLVVNSGNGAAGHVIDEVEKRFAAAGVPVTFIKVHHQPDGHFPNGIPNPLLPECRQDTADAVREHQADMGIAFDGDFDRCFLFDDEASFIEGYYIVGLLAEAFLQKQPGAKIIHDPRLTWNTVDIVTRNGGQPVMSKTGHAFIKERMR... | 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... |
P26405 | MNVVNNSRDVIYSSGIVFGTSGARGLVKDFTPQVCAAFTVSFVAVMQEHFSFDTVALAIDNRPSSYGMAQACAAALADKGVNCIFYGVVPTPALAFQSMSDNMPAIMVTGSHIPFERNGLKFYRPDGEITKHDEAAILSVEDTCSHLELKELIVSEMAAVNYISRYTSLFSTPFLKNKRIGIYEHSSAGRDLYKPLFIALGAEVVSLGRSDNFVPIDTEAVSKEDREKARSWAKEFDLDAIFSTDGDGDRPLIADEAGEWLRGDILGLLCSLALDAEAVAIPVSCNSIISSGRFFKHVKLTKIGSPYVIEAFNELSRSYS... | 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-... |
P26404 | MSFLPVIMAGGTGSRLWPLSREYHPKQFLSVEGKLSMLQNTIKRLASLSTEEPVVICNDRHRFLVAEQLREIDKLANNIILEPVGRNTAPAIALAAFCALQNADNADPLLLVLAADHVIQDEIAFTKAVRHAEEYAANGKLVTFGIVPTHAETGYGYIRRGELIGNDAYAVAEFVEKPDIDTAGDYFKSGKYYWNSGMFLFRASSYLNELKYLSPEIYKACEKAVGHINPDLDFIRIDKEEFMSCPSDSIDYAVMEHTQHAVVIPMSAGWSDVGSWSSLWDISNKDHQRNVLKGDIFAHACNDNYIYSEDMFISAIGVSN... | 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-manno... |
P26406 | MDNIDNKYNPQLCKIFLAISDLIFFNLALWFSLGCVYFIFDQVQRFIPQDQLDTRVITHFILSVVCVGWFWIRLRHYTYRKPFWYELKEIFRTIVIFAIFDLALIAFTKWQFSRYVWVFCWTFALILVPFFRALTKHLLNKLGIWKKKTIILGSGQNARGAYSALQSEEMMGFDVIAFFDTDASDAEINMLPVIKDTEIIWDLNRTGDVHYILAYEYTELEKTHFWLRELSKHHCRSVTVVPSFRGLPLYNTDMSFIFSHEVMLLRIQNNLAKRSSRFLKRTFDIVCSIMILIIASPLMIYLWYKVTRDGGPAIYGHQRV... | 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
Lo... |
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
Sequenc... |
P26401 | MLISFCIPTYNRKEYLEELLNSINNQEKFNLDIEICISDNASTDGTEEMIDVWRNNYNFPIIYRRNSVNLGPDRNFLASVSLANGDYCWIFGSDDALAKDSLAILQTYLDSQADIYLCDRKETGCDLVEIRNPHRSWLRTDDELYVFNNNLDREIYLSRCLSIGGVFSYLSSLIVKKERWDAIDFDASYIGTSYPHVFIMMSVFNTPGCLLHYISKPLVICRGDNDSFEKKGKARRILIDFIAYLKLANDFYSKNISLKRAFENVLLKERPWLYTTLAMACYGNSDEKRDLSEFYAKLGCNKNMINTVLRFGKLAYAVKN... | 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-... |
P37746 | MNTNKLSLRRNVIYLAVVQGSNYLLPLLTFPYLVRTLGPENFGIFGFCQATMLYMIMFVEYGFNLTATQSIAKAADSKDKVTSIFWAVIFSKIVLIVITLIFLTSMTLLVPEYNKHAVIIWSFVPALVGNLIYPIWLFQGKEKMKWLTLSSILSRLAIIPLTFIFVNTKSDIAIAGFIQSSANLVAGIIALAIVVHEGWIGKVTLSLHNVRRSLADGFHVFISTSAISLYSTGIVIILGFISGPTSVGNFNAANTIRNALQGLLNPITQAIYPRISSTLVLNRVKGVILIKKSLTCLSLIGGAFSLILLLGASILVKISI... | 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 ... |
Q99191 | MRKLRLVRIPRHLIIAASSWLSKIIIAGVQLVSVKFLLEILGEESYAVFTLLTGLLVWFSIADIGIGSSLQNYISELKADRKSYDAYIKAAVHILFASLIILSSTLFFLSDKLSSLYLTSFSDELKNNSGSYFFIASILFIFIGVGSVVYKILFAELLGWKANIINALSYLLGFLDVVAIHYLMPDSSITFALVALYAPVAILPIIYISFRYIYVLKAKVNFNTYKLLLSRSSGFLIFSSLSIIVLQTDYIVMSQKLSAADIIKYTVTMKIFGLMFFIYTAVLQALWPVCAELRVKMQWRKLHRIIFLNIIGGVFFIGLG... | 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 ... |
Q03583 | MKKNILLLFLVHGANYLFPFIVLPYQTRILSIETFADVAKIQAAVMLLSLIVNYGYNLSSTRAIARAVSQAEINKIYSETLIVKLLLATICLALGCVHLMYVKEYSLIYPFIISSIYLYGSALFATWLFQGLEKMKAVVIATTIAKLTGVILTFILVKSPNDIVAALFTQNIGMFISGIISIYLVRKNKYATVICFRLKNIIVSLKEAWPFFLSLAATSVYTYFNVILLSFYAGDYVVANFNAADKLRMAAQGLLIPIGQAVFPRLSKLEGYEYSSKLKIYAIRYAIFGVCISAGLVFLGPMLTTIYLGKEYSLSGEYLQ... | 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 ... |
P37748 | MIYLVISVFLITAFICLYLKKDIFYPAVCVNIIFALVLLGYEITSDIYAFQLNDATLIFLLCNVLTFTLSCLLTESVLDLNIRKVNNAIYSIPSKKVHNVGLLVISFSMIYICMRLSNYQFGTSLLSYMNLIRDADVEDTSRNFSAYMQPIILTTFALFIWSKKFTNTKVSKTFTLLVFIVFIFAIILNTGKQIVFMVIISYAFIVGVNRVKHYVYLITAVGVLFSLYMLFLRGLPGGMAYYLSMYLVSPIIAFQEFYFQQVSNSASSHVFWFFERLMGLLTGGVSMSLHKEFVWVGLPTNVYTAFSDYVYISAELSYLM... | 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 membra... |
Q00474 | MLPFPPGAILRDVLNVFFVALVLVRFVIDRKKTYFPLVFTIFSWSAVILWVIALTIFSPDKIQAIMGGRSYILFPAVFIALVILKVSYPQSLNIEKIVCYIIFLMFMVATISIIDVLMNGEFIKLLGYDEHYAGEQLNLINSYDGMVRATGGFSDALNFGYMLTLGVLLCMECFSQGYKRLLMLIISFVLFIAICMSLTRGAILVAALIYALYIISNRKMLFCGITLFVIIIPVLAISTNIFDNYTEILIGRFTDSSQASRGSTQGRIDMAINSLNFLSEHPSGIGLGTQGSGNMLSVKDNRLNTDNYFFWIALETGIIG... | 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 membra... |
P0A236 | MLIISYIALCLLFIVYLYTLSVRIEGKIINVMVPYLIITVPTLYVFEGIFVYLSEVQNYTVEYLFFYTCYITYIASFVISYLYTQRKPIYNKSNTKNKPRYVFTSLLFTFLAFIIYLPVLMEFREYILSPRRIYELTRTGYGIYFYPSLMFSLVASICAFFTYKKSKLFCISIVLFNCILIFLHGNKGPIFSIFIAFILYLSYIENKKIKFMFLVKSFAVIAVIVTAFFAYTFTDGNPIENMANYSDYTRNAVLVASSNFDFMYGKLLMESEVYSRIPRAIWPDKPEDFGALYLAKVFFPDAFYRNQGAPAFGYGELYAD... | 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 membra... |
Q03584 | MTYFTGFILILFAIIIKRLTPSQSKKNIVLIANAFWGILLVGYTFNEQYFVPLSATTLFFILAFLFFFSMTYILIARSGRVVFSFGTGFIESKYIYWFAGMINIISICFGIILLYNNHFSLKVMREGILDGSISGFGLGISLPLSFCCMYLARHENKKNYFYCFTLLSFLLAVLSTSKIFLILFLVYIVGINSYVSKKKLLIYGVFVFGLFALSSIILGKFSSDPEGKIISAIFDTLRVYLFSGLAAFNLYVEKNATLPENLLLYPFKEVWGTTKDIPKTDILPWINIGVWDTNVYTAFAPWYQSLGLYAAIIIGILLGF... | 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 membra... |
P37784 | MNNINKIFITFLCIELIIGGGGRLLEPLGIFPLRYLLFVFSFILLIFNLVTFNFSITQKCVSLFIWLLLFPFYGFFVGLLAGNKINDILFDVQPYLFMLSLIYLFTLRYTLKVFSCEIFIKIVNAFALYGSLLYISYIILLNFGLLNFNLIYEHLSLTSEFFFRPDGAFFSKSFYFFGVGAIISFVDKKYLKCLIIVLAILLTESRGVLLFTTLSLLLASFKLHKLYLNTIIIILGSVLFIIMLYMVGSRSEDSDSVRFNDLYFYYKNVDLATFLFGRGFGSFILDRLRIEIVPLEILQKTGVIGVFISLVPMLLIFLKG... | 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 membra... |
Q56328 | MNGAVCVLSALIAVFTCFSCRPAVQDERAVRIAVFVPGFRHDSPVYAMLCDGVERAVTQERATGRSIGLDIIEAGPNQALWREKLAHLAAEQRYRLIVSSNPALPHVLEPILRQFPLQRFLVLDAYAPQEHSLITFRYNQWEQAYLAGHLSALVSASAMRFANADKKIGLIAGQSYPVMTQTIIPAFLAGARAVDPAFEVDVRVVGNWYDAAKSADLARILFHEGVDVMMPICGGANQGVLAAARELGFYVSWFDDNGYARAPGYVVGSSVMEQERLAYEQTLRCIRGELPSAGAWTLGVKDGYVRFIEEDPLYLQTVPE... | 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 | MMIAERGVRASARGVLSLHHIGKTYPRVMPRSKRGVWGMFGHPGRRAVDDAHTAHGPCSGARETDAAEHSVLSDVNLSFFTGEIHALLGKNGAGKSTLAHILSGFCVPTHGQLRLDGKEQRFSVPFDALRAGIGIVHQQPVFAERATVFENVVMGSAALTGVRWVRRAQVRERIDRIIAQWRMPLKKEEYVACLSADKRFFVSLLCVLFRNPRFIILDEPRCAPAQSRAVFFSHLEEFFVRSSHAPRCGGGVIVVTHRFADALRWAQRISLIEGGKACSFLRTDLLDEYCSAHQVNECIQKVSCALMSASTVTSSAVSSF... | 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 | MKRVINSCIAVLLGVAVMSAVIVLCSENPSVSLAAFFLKPFSTRGYIRALFHKAGLFVCMALGASCALKTGMINLGGDGQIYAAGFVTALLLREYWGVGFLLQWSVALLCALSVAGILACVSGILKAWLATSEMITSFLLSTACVPLIDALIITVTRDPAGNLLATAPVHSHFILQQQTSLFGVPAVLTYASLVALAVGCFFSYTRVGYQFRICGKAPEFGRFVGFPVWATYVWGMVLSGALFGLTGFFSVVGLFGTCYVGFSVGMGYAALAHALIAHAHITVLVPLAFFFAWMETASEAAVLGAHLTVNVVLFLQAAIF... | 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 | MAQEAMEYNVDEQLEHRVAEQPVPAEVVSTQGGPPPLQPLPTEVVSSQGAPPLLQPAPAEGTSSQVGPHLLQPAAQLSVDLTEEVELLGEDRVENINPGASEEHRQPSRVNRPIPVSSLDSMNSFISGLQRLHGMLEFLRPPSDHNVGPVRSRRRRGSASRRSRTVGSQRTDSARSRAPLDAYFQVSRTQPHLPSMSQDSETRNPVSEDLQVSSSSSSDSESSAEYEEVVVQAEDTRAVVSEEQGGTAAEQEVTCVGGGETLPKQSPQKTNPLLPSVSKDDEEGDTCTICFEHWTNAGDHRLSALRCGHLFGYKCISKWL... | 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, leadi... |
Q6PCD5 | MAHEAMEYDVQVQLNHAEQQPAPAGMASSQGGPALLQPVPADVVSSQGVPSILQPAPAEVISSQATPPLLQPAPQLSVDLTEVEVLGEDTVENINPRTSEQHRQGSDGNHTIPASSLHSMTNFISGLQRLHGMLEFLRPSSSNHSVGPMRTRRRVSASRRARAGGSQRTDSARLRAPLDAYFQVSRTQPDLPATTYDSETRNPVSEELQVSSSSDSDSDSSAEYGGVVDQAEESGAVILEEQLAGVSAEQEVTCIDGGKTLPKQPSPQKSEPLLPSASMDEEEGDTCTICLEQWTNAGDHRLSALRCGHLFGYRCISTWL... | 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, lea... |
Q7TQ33 | MGVRAAPSCAAAPAAAGAEQSRRPGLWPPSPPPPLLLLLLLSLGLLHAGDCQQPTQCRIQKCTTDFVALTAHLNSAADGFDSEFCKALRAYAGCTQRTSKACRGNLVYHSAVLGISDLMSQRNCSKDGPTSSTNPEVTHDPCNYHSHGGVREHGGGDQRPPNYLFCGLFGDPHLRTFKDHFQTCKVEGAWPLIDNNYLSVQVTNVPVVPGSSATATNKVTIIFKAQHECTDQKVYQAVTDDLPAAFVDGTTSGGDGDVKSLHIVEKESGRYVEMHARYIGTTVFVRQLGRYLTLAIRMPEDLAMSYEESQDLQLCVNGCP... | 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.
Locati... |
Q6ZVN8 | MGEPGQSPSPRSSHGSPPTLSTLTLLLLLCGHAHSQCKILRCNAEYVSSTLSLRGGGSSGALRGGGGGGRGGGVGSGGLCRALRSYALCTRRTARTCRGDLAFHSAVHGIEDLMIQHNCSRQGPTAPPPPRGPALPGAGSGLPAPDPCDYEGRFSRLHGRPPGFLHCASFGDPHVRSFHHHFHTCRVQGAWPLLDNDFLFVQATSSPMALGANATATRKLTIIFKNMQECIDQKVYQAEVDNLPVAFEDGSINGGDRPGGSSLSIQTANPGNHVEIQAAYIGTTIIIRQTAGQLSFSIKVAEDVAMAFSAEQDLQLCVGG... | 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... |
Q7TQ32 | MGQSPSPRSPHGSPPTLSTLTLLLLLCGQAHSQCKILRCNAEYVSSTLSLRGGGSPDTPRGGGRGGLASGGLCRALRSYALCTRRTARTCRGDLAFHSAVHGIEDLMIQHNCSRQGPTAPPPARGPALPGAGPAPLTPDPCDYEARFSRLHGRAPGFLHCASFGDPHVRSFHNQFHTCRVQGAWPLLDNDFLFVQATSSPVSSGANATTIRKITIIFKNMQECIDQKVYQAEVDNLPAAFEDGSINGGDRPGGSSLSIQTANLGSHVEIRAAYIGTTIIIRQTAGQLSFSIRVAEDVARAFSAEQDLQLCVGGCPPSQRL... | 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 fr... |
Q8UBN2 | MARAERSVLLRLENISKEFPGVKALSNVHFDLRSGEVHAVCGENGAGKSTLMKIISGVYQPSEGTILHKGEKVQYASPLQSEAAGIAIIHQELNLVPHLSVAENIYLAREPRRGFLVDRKKLRLDAKRCLDRLGVDINPDQLVRSLSVAQCQMVEIAKALSLDAEVLIMDEPTSSLTEQETRLLFKVIRDLKASGVGIVYISHRLDEMAEIVDRVTILRDGRYISTDDFASITVDDIVTRMVGRSLEDKFPERTSRPTDDILFSVEGLTRNGVFSDVSFSLRRGEILGFAGLMGAGRTEVARAIFGADPLDAGKIVFNGR... | 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: Periphe... |
Q2KAW9 | MSATLQRVAPLSGGEGHRTPIDSGAGFVLEMRSITKAFPGVLALDGMSLKVRAGTVHVLVGENGAGKSTLMKILSGIYAIDGGEILFRGEKLDHQSAAAALERGISMIHQELSPVLDMTIAENIFLGREPTYSRTGVLSRFVDFDRMNSDTQTLLDRLGLKYSPQTKMRDLSIATMQLIEIVKAISREASLIIMDEPTSAISDTEVAMLFRQIADLKAAGVAIIYITHKMDEIFQIADDITVMRDGQFVAAAPASEYEPAKLISQMVGRTISSIFPKEEVPIGDIVLSVENLSRDGVFDNVGFEVRAGEIVGLSGLIGAG... | 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: Periphe... |
Q92MP8 | MTVLVSLSGISKNFSGVQALKGVDFDLRAGEVHALVGENGAGKSTLMRVLAGEMKPTSGTVSIHGETMQHSGPRGAAGRGISVIHQELALAPDLTVAENIFLGRLPRIVNHRRLRKAASEILERLGFDIDPAIHAGRLTVAHQQVVEIAKALSNRARIIVFDEPTAVLANTDAERLLAIIRELRAGGTGAVYISHRLNEVFDLSDRITVMKDGSHVETLETSATDVDAVIARMVGRQMSALFPSKAGRVPGEVVVRVRNVSRGRKVRDVSFSVRAGEVVGLGGLVGSGRTEVARLVFGADKMDSGTVELNGKPLHLSSPR... | 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: Periphe... |
Q8U9B0 | MTATASALRMRGISKIFPGVKALSNVNFTVEYGRIHAVVGENGAGKSTLMKILSGSYAPTTGTTEIAGVEVQMRRPADAQKLGIRMVHQELNLVPDLTVAENIYLGRMPHRRFLVDRQAMLRKAAAVLKELEAAIDPKARLGDLPISQQQLVEIAKSYSADPRIIVLDEPTSSLSEHETTALFSILRKMKSQGIAIIYISHRLKEVLDIADDVTILRDGSMIDTRPAAGITAAEMIRLMVGREVANVFPKTPSKIGPVAFKVTGLSDGEKFHDVGFDVRSGEILGLTGLVGAGRTEVAQAIFGLAPLATGRIEINGKAVT... | 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: Periphe... |
P49758 | MAQGSGDQRAVGVADPEESSPNMIVYCKIEDIITKMQDDKTGGVPIRTVKSFLSKIPSVVTGTDIVQWLMKNLSIEDPVEAIHLGSLIAAQGYIFPISDHVLTMKDDGTFYRFQAPYFWPSNCWEPENTDYAIYLCKRTMQNKARLELADYEAENLARLQRAFARKWEFIFMQAEAQVKIDRKKDKTERKILDSQERAFWDVHRPVPGCVNTTEMDIRKCRRLKNPQKVKKSVYGVTEESQAQSPVHVLSQPIRKTTKEDIRKQITFLNAQIDRHCLKMSKVAESLIAYTEQYVEYDPLITPAEPSNPWISDDVALWDIE... | 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
Sequ... |
Q9Z2H2 | MAQGSGDQRAVGIADPEESSPNMIVYCKIEDIITKMQDDKTGGVPIRTVKSFLSKIPSVVTGTDIVQWLMKNLSIEDPVEAIHLGSLIAAQGYIFPISDHVLTMKDDGTFYRFQAPYFWPSNCWEPENTDYAIYLCKRTMQNKARLELADYEAENLARLQRAFARKWEFIFMQAEAQVKIDRKKDKTERKILDSQERAFWDVHRPVPGCVNTTEMDIRKCRRLKNPQKVKKSVYGVTDETQSQSPVHIPSQPIRKTTKDDIRKQITFLNAQIDRHCLKMSKVAESLIAYTEQYVEYDPFITPAEPSNPWISDDITLWDIE... | 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
Seque... |
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
Seque... |
P49802 | MAQGNNYGQTSNGVADESPNMLVYRKMEDVIARMQDEKNGIPIRTVKSFLSKIPSVFSGSDIVQWLIKNLTIEDPVEALHLGTLMAAHGYFFPISDHVLTLKDDGTFYRFQTPYFWPSNCWEPENTDYAVYLCKRTMQNKARLELADYEAESLARLQRAFARKWEFIFMQAEAQAKVDKKRDKIERKILDSQERAFWDVHRPVPGCVNTTEVDIKKSSRMRNPHKTRKSVYGLQNDIRSHSPTHTPTPETKPPTEDELQQQIKYWQIQLDRHRLKMSKVADSLLSYTEQYLEYDPFLLPPDPSNPWLSDDTTFWELEASK... | 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... |
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 fo... |
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 th... |
Q8FBE0 | MTTQLEQAWELAKQRFAAVGIDVEEALRQLDRLPVSMHCWQGDDVSGFENPEGSLTGGIQATGNYPGKARNASELRADLEQAMRLIPGPKRLNLHAIYLESDTPVARDQIKPEHFKNWVEWAKTNQLGLDFNPSCFSHPLSADGFTLSHADDSIRQFWIDHCKASRRVSAYFGEQLGTPSVMNIWIPDGMKDITVDRLAPRQRLLAALDEVISEKLDPAHHIDAVESKLFGIGAESYTVGSNEFYMGYATSRQTALCLDAGHFHPTEVISDKISAAMLYVPQLLLHVSRPVRWDSDHVVLLDDETQAIASEIVRHDLFDR... | 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.
S... |
Q9KCM0 | MNYSLAVDIGASSGRLIVGECNKKIQLTEIHRFENQIIEKNGQFCWDVDALFSEIKTGLKKCREAGIEPVSMGIDTWAVDFVLLDEHDKPLTDAVSYRDPRTDGVMEEVIEQFMKERLYLETGIQFQQFNTIYQLYALKKQHPDIFKKAKSFLMIPDYFHFLLTGKKANEYTNATTTQLVNAFTKKWDKDIIEALGFNPDMFQEIKLPTESLGKLKSEWVEEVGFDLEVILPATHDTGSAVVAVPKVADTIYLSSGTWSLIGVENSFPICVTKALDYNFTNEGGMNYQFRFLKNIMGLWMIQEVRRNYDNRYSFAQLVEL... | 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
Sequenc... |
Q8Y3I6 | MKHYVAVDIGASSGRLILGKLVNEKLQLEEIHRFKNGFTYRDGHERWEIDQLMQEIFIGLEKVKQLGISECVLGIDTWGVDYVLIGASGEKLADPISYRDKRTLNAVQNLTSEYPREYIYKKTGIQFMELNTLYQLYVEERDLLERAEKILLIPDYIGYVLTGVKVAETTNSSTTQMLNLREQLFDKDLLSHLNIDVEKFAPLTDAGTYLGEVKEDWLKMYDIPNCDVVTVATHDTASAVVGTPAEGENWAFLSSGTWSLIGMELSAPINNEVAFKENYTNEWGAYGTYRFLKNIMGLWIVQEIARMDDYKHSFAEMAEE... | 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
Sequenc... |
Q8ESX1 | MQQCNLAVDIGASSGRVIAGYLQNGKLQLEEVHRFDNKLIDLNNYFCWDIDRIYQEILMGIKSAVDNGYQPISLGIDTWAVDFVLLDENDMRLTDAVSYRDPRTDGMMEEVFSQISKERLYLETGIQFQKFNTMYQLQALKNSNPDLIEKATSFLMIPDYLNFLLTGKKVNEYTNATTTQLVNAFTKKWDIDLIEQLGFNSNMFMDIQPPESVIGNLRPELQEELGVDFNVILPATHDTGSAVVAVPEQENSIYISSGTWSLIGVENHFPICTTKALDYNFTNEGGADYRYRFLKNIMGLWMIQEVKRNFNDEFEFADFA... | 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
Sequenc... |
Q9UBD6 | MAWNTNLRWRLPLTCLLLQVIMVILFGVFVRYDFEADAHWWSERTHKNLSDMENEFYYRYPSFQDVHVMVFVGFGFLMTFLQRYGFSAVGFNFLLAAFGIQWALLMQGWFHFLQDRYIVVGVENLINADFCVASVCVAFGAVLGKVSPIQLLIMTFFQVTLFAVNEFILLNLLKVKDAGGSMTIHTFGAYFGLTVTRILYRRNLEQSKERQNSVYQSDLFAMIGTLFLWMYWPSFNSAISYHGDSQHRAAINTYCSLAACVLTSVAISSALHKKGKLDMVHIQNATLAGGVAVGTAAEMMLMPYGALIIGFVCGIISTLG... | 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 elec... |
Q9QXP0 | MAWNTNLRGRLPITCLILQVTMVVLFGVFVRYDIQADAHWWLEKKRKNISSDVENEFYYRYPSFQDVHAMVFVGFGFLMTFLQRYGFSAVGFNFLLAAFGIQWALLMQGWFHYFEEGHIVLSVENIIQADFCVASSCVAFGAVLGKVSPMQLLIMTFFQVTLFTVNEFILLNLIEAKDAGGSMTIHTFGAYFGLTVTWILYRKNLDQSKQRQSSVYHSDLFAMIGTLFLWIYWPSFNSASSFHGDAQHRAALNTYLSLAASVLTTVTVSSIVHKKGKLDMVHIQNATLAGGVGVGTAAEMMLTPYGALIVGFFCGIFSTL... | 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 elec... |
Q8RJP2 | MHMNKPLQAWRTPLLTLIFVLPLTATGAVKLTLDGMNSTLDNGLLKVRFGADGSAKEVWKGGTNLISRLSGAARDPDKNRSFYLDYYSGGVNEFVPERLEVIKQTPDQVHLAYIDDQNGKLRLEYHLIMTRDVSGLYSYVVAANTGSAPVTVSELRNVYRFDATRLDTLFNSIRRGTPLLYDELEQLPKVQDETWRLPDGSVYSKYDFAGYQRESRYWGVMGNGYGAWMVPASGEYYSGDALKQELLVHQDAIILNYLTGSHFGTPDMVAQPGFEKLYGPWLLYINQGNDRELVADVSRRAEHERASWPYRWLDDARYPR... | 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 rhamnogal... |
Q58DK7 | MSADDGGIRAAQDKERARETPGHGHSCQEMLSESEGTVPLGEAWESPHIKMEPEEPHPEGVSQETRAEGARGWVPLSQGTKEKVCFLPGGALPAPQTPVLSREGRTRDRQMAAALLTAWSQMPVTFEDMALYLSREEWGRLDHTQQSFYREVLQKRSGLSLGFPFSRPFWASQVQGKGEAPGSSRQLGHEEEEKRGVVEVDKEELAASLGALGDAKSFKSRMGRAQGEAPRCGQRAASGQNSGPAKDDVQPCPVKEAQLESAPPDTDLPKTQEGHFPEQPREGGTAAPESSEEGLALDSEAGKKTYKCEQCGKAFSWHSH... | 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 transcript... |
O95201 | MSADGGGIQDTQDKETPPEVPDRGHPHQEMPSKLGEAVPSGDTQESLHIKMEPEEPHSEGASQEDGAQGAWGWAPLSHGSKEKALFLPGGALPSPRIPVLSREGRTRDRQMAAALLTAWSQMPVTFEDVALYLSREEWGRLDHTQQNFYRDVLQKKNGLSLGFPFSRPFWAPQAHGKGEASGSSRQAGDEKEWRGACTGAVEVGQRVQTSSVAALGNVKPFRTRAGRVQWGVPQCAQEAACGRSSGPAKDSGQPAEPDRTPDAAPPDPSPTEPQEYRVPEKPNEEEKGAPESGEEGLAPDSEVGRKSYRCEQCGKGFSWH... | 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 transcri... |
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-hyd... |
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 ... |
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 =... |
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 grow... |
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... |
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 Topolo... |
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
Sequenc... |
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 = ... |
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... |
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... |
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... |
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... |
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 ... |
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... |
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... |
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... |
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... |
P47924 | MSSINLSSSSPSTISLSRSRLSQSSTTLLHGLHRVTLPSNHPLSTFSIKTNTGKVKAAVISREDDLLSFTNGNTPLSNGSLIDDRTEEPLEADSVSLGTLAADSAPAPANGFVAEDDDFELDLPTPGFSSIPEAIEDIRQGKLVVVVDDEDRENEGDLVMAAQLATPEAMAFIVRHGTGIVCVSMKEDDLERLHLPLMVNQKENEEKLSTAFTVTVDAKHGTTTGVSARDRATTILSLASRDSKPEDFNRPGHIFPLKYREGGVLKRAGHTEASVDLTVLAGLDPVGVLCEIVDDDGSMARLPKLREFAAENNLKVVSIA... | 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... |
Q6NLQ7 | MASLTLRCDSTHLLPSRDVVKGTKPFGTSLVYPRIISKKFNVRMRVIPEEGDVFSSSKSNGSSMGIELQPDLVSFGTLAAEMIPTTMDSPEVEDEEFDLDRPTDGFASIPQAIEDIRHGKMVVVVDDEDRENEGDLIMAASLATPEAMAFVVKHGTGIVCVSMKGEDLERLELPLMVTRKDNEEKLRTAFTVSVDAKKGTSTGVSARDRAQTILTLASKDSKPEDFNRPGHIFPLRYREGGVLKRAGHTEASVDLTVLAGLEPVSVLCEIVDDDGSMARLPRLRQFAQENNLKLISIADLIRYRRKRERLVEFTAVAPIP... | 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.
Catalyti... |
Q9FN89 | MMDSALYHPRIFFAHSFINGLYSSPRFANTCWRLVSRSSWEIKASENSDRNVFDENPVRKTDGSLFDSASFETVDAEITPETDDFFVSDAEGDPDCPTQGYSSIELALQALRKGKFVIVVDDETGDVEGNLIMAATLTSPKDIAFLIKNGSGIVSVGMKKENLERLSLTLMSPEMEDEDSSAPTFTITVDAKSGTSTGVSASDRAMTVLALSSLDAKPDDFRRPGHVFPLKYRDGGVLRRAGHTEASVDLMILAGLRPLSVLSAILDQEDGSMASLPYMKKLATEHDIPIVSLTDLIRYRRKRDKLVERITVSRLPTKWG... | 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: G... |
O84736 | MFTCEAGIASVQQAIKDVAEGKFVIVIDAASRENEGDLILAGEKVSTEKMSFLLSHTTGIVCASLSREQAKSLDLPAMVQDNQCAFKTAFTVSVDASSGVTTGVSASDRTRTVQLLADPAATAESFVRPGHVFPLISQPGGAVQRPGHTEAAMDLMRLAGMQPCGIFAELVNPDHSMMRQQQVLAFAEQHDLTVITVDDLITYRYTYDSLVTKISSARLPTKYGDFSIHVYESIIDGTQHFALVKGDIHEQEAVPVRVHSECLTGDILGSCRCDCGAQLDMAMRYIAEEGLGVIVYLRGQEGRGIGFGHKIRAYALQDLG... | 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
Sequ... |
O24752 | MNAPLNSAVRLDSIEEAIADIAAGKAVVVVDNEDRENEGDLIFAAELATPELVAFMVRYSSGYICVPLLPEDCKRLNLPPMMGRNEDVRGTAYTVTVDANTGTTGISATSRAETMLRLADPMSVVDDFTRPGHVVPLAARPNGVLERDGHTEAAIDLARLAGLRPAGVLCEIVSEEDPTTMARSEELRRFSDEHDLKMISIEQLIEWRRHNETQVRRTVETQLPTDFGSFTALGYKHEIDGQEHVALIAGGVEELNGAEDVFVRVHSECLTGDVFHSRRCDCGQQLHQSMEIIQEAGQGIIIYLRGHEGRGIGLLAKLKA... | 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
Sequ... |
A4QEG9 | MSEHEQAHSQLDSVEEAIADIAAGKAVVVVDDEDRENEGDIIFAAELATPELVAFMVRYSSGYICAPLTAKDADRLDLPPMTAHNQDARGTAYTVTVDANTGTTGISATDRAHTLRLLADPEADRTDFTRPGHVVPLRAREGGVLVRAGHTEAAVDLARAAGLRPAGVICEVVSEEDPTGMARVPELRRFCDEHDLKLISIEQLIEWRRKNEILVERQVETVLPTDFGTFKAVGYRSIIDGTELVAIVAGDVASDGGENVLVRVHSECLTGDVFGSRRCDCGQQLHESLRLIQEAGRGVVVYMRGHEGRGIGLLAKLRAY... | 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
Sequ... |
P0A5V1 | MTRLDSVERAVADIAAGKAVIVIDDEDRENEGDLIFAAEKATPEMVAFMVRYTSGYLCVPLDGAICDRLGLLPMYAVNQDKHGTAYTVTVDARNGIGTGISASDRATTMRLLADPTSVADDFTRPGHVVPLRAKDGGVLRRPGHTEAAVDLARMAGLQPAGAICEIVSQKDEGSMAHTDELRVFADEHGLALITIADLIEWRRKHEKHIERVAEARIPTRHGEFRAIGYTSIYEDVEHVALVRGEIAGPNADGDDVLVRVHSECLTGDVFGSRRCDCGPQLDAALAMVAREGRGVVLYMRGHEGRGIGLMHKLQAYQLQD... | 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
Sequ... |
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 fro... |
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 ... |
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 fro... |
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): s... |
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 ... |
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 fro... |
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 fro... |
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 fro... |
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... |
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 fro... |
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 fro... |
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 ... |
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 ... |
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 fro... |
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 fro... |
Q8IXN7 | MCSQLWFLTDRRIREDYPQVQILRALRQRCSEQDVRFRAVLMDQIAVTIVGGHLGLQLNQKALTTFPDVVLVRVPTPSVQSDSDITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEPLGYPVVVKSTRGHRGKAVFLARDKHHLSDICHLIRHDVPYLFQKYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCSLGGVGVKCPLTEQGKQLAIQVSNILGMDFCGIDLLIMDDGSFVVCEANANVGFLAFDQACNLDVGGIIADYTMSLLPNRQTGKMAVLPGLSSP... | 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... |
Q66HZ2 | MCSRVWFITDRRISQEYPQIQILRALKERCVEDDVEFRYLLMDEIVLTITDGQLGLRVGQEIVTSYPQVAVVRVPTPWVQSDSDITVLRHLEKMGCRLVNRPQAILNCVNKFWTFQELAGHGVPLPDTYSYGGHDNFRKMIDEAEPLGYPVVVKNARGHRGKAVFLARDKHHLSDLCHLIRHEAPYLFQEYVKESHGRDVRVVLVGGRVIGSMLRCSTDGRMQSNCSLGGVGMMCPLSEQGKQLAVQVCNILGMDVCGIDLLQKNDGSFVVCEANANVGFIAFDQACGMDVAGIVADFVLSLLPSRLSRKMSLLSVVSST... | 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-citrylgl... |
Q80WS1 | MCSSVTGKLWFLTDRRIREDYPQKEILRALKAKCCEEELDFRAVVMDEMVLTVEQGNLGLRISGELISAYPQVVVVRVPTPWVQSDSDITVLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEAEVLEFPMVVKNTRGHRGKAVFLARDKHHLADLSHLIRHEAPYLFQKYIKESHGRDVRVIVVGGRVVGTMLRCSTDGRMQSNCSLGGVGMMCSLSEQGKQLAIQVSNILGTDVCGIDLLMKDDGSFCVCEANANVGFIAFDKACNLDVAGIIADYAASLLPAGRLTRRMSLLS... | 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-citrylgl... |
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 ... |
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 ... |
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 ... |
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 ... |
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 ... |
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 ... |
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 ... |
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 ... |
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