ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q2M5Q2 | MKNLCIIPARGGSKRIPRKNIIDFLGKPLIAYSIENALNSGIFDEIVLSSDDEEIIEVALKYGAKAPFVRDKNLSDDYASSTAAVQNAIEILQSQNQIYDHVCCLYATAPLLNKNILKQAYEKFIQNQSKFLFAATEFEYPIQRAFYLNENNQVYMFDEKHYKSRSQDLTKAYHDAGAFYFGTSKAWLEEDFIFKPHSSVFVLPRNLVCDIDTMQDLEFAKILYKVNHESAF | Function: Catalyzes the final step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Mediates the activation of pseudaminic acid with CMP by forming CMP-pseudaminic acid (By similarity).
Catalytic Activity: CTP + pseudaminate = CMP-pseudaminate + diphosphate
Sequence Ma... |
Q0P8U5 | MKVLFRSDSSSQIGFGHIKRDLVLAKQYSDVSFACLPLEGSLIDEIPYPVYELSSESIYELINLIKEEKFELLIIDHYGISVDDEKLIKLETGVKILSFDDEIKPHHCDILLNVNAYAKASDYEGLVPFKCEVRCGFSYALIREEFYQEAKENREKKYDFFICMGGTDIKNLSLQIASELPKTKIISIATSSSNPNLKKLQKFAKLHNNIRLFIDHENIAKLMNESNKLIISASSLVNEALLLKANFKAICYVKNQESTATWLAKKGYEVEYKY | Function: Nucleotide sugar hydrolase that catalyzes the fourth step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Mediates the removal of UDP from C-1 of UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose forming 2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyran... |
O25094 | MKKNYSYKNIQAIDFTNLNDGEKLLVLEFRNHPNTALWMYSTFISLKTHLQFIEDLKNSPNHRYFLFKEEGVYLGVGSITKINFFHKHGYLGIYKNPFLKNGGETILKALEFIAFEEFQLHSLHLEVMENNFKAIAFYEKNHYELEGRLKGFISKDKEFIDVLLYYKDKKGYNDQSLLKL | Function: Catalyzes the third step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Mediates N-4 acetylation of UDP-4-amino-4,6-dideoxy-beta-L-AltNAc to form UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose.
Catalytic Activity: acetyl-CoA + UDP-4-amino-4,6-dideo... |
Q0P8U0 | MQIGNFNTDKKVFIIAELSANHAGSLEMALKSIKAAKKAGADAIKIQTYTPDSLTLNSDKEDFIIKGGLWDKRKLYELYESAKTPYEWHSQIFETAQNEGILCFSSPFAKEDVEFLKRFDPIAYKIASFEANDENFVRLIAKEKKPTIVSTGIATEEELFKICEIFKEEKNPDLVFLKCTSTYPTAIEDMNLKGIVSLKEKFNVEVGLSDHSFGFLAPVMAVALGARVIEKHFMLDKSIESEDSKFSLDFDEFKAMVDAVRQAESALGDGKLDLDEKVLKNRVFARSLYASKDIKKGEMFSEENVKSVRPSFGLHPKFYQ... | Function: Catalyzes the fifth step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Catalyzes the condensation of phosphoenolpyruvate with 2,4-diacetamido-2,4,6-trideoxy-beta-l-altropyranose, forming pseudaminic acid.
Catalytic Activity: 2,4-diacetamido-2,4,6-trideoxy-... |
O24980 | MLQPPKIVAELSANHNQDLNLAKESLHAIKESGADFVKLQTYTPSCMTLNSKEDPFIIQGTLWDKENLYELYQKASTPLEWHAELFELARKLDLGIFSSPFSSQALELLESLNCPMYKIASFEIVDLDLIEKAARTQKPIILSSGIATHTELQDAISLCRRVNNFDITLLKCVSAYPSKIEDANLLSMVKLGEIFGVKFGLSDHTIGSLCPILATTLGASMIEKHFILNKSLQTPDSAFSMDFNGFKSMVEAIKQSVLALGEEEPRINPKTLEKRRFFARSLFVIKDIQKGEALTENNIKALRPNLGLHPKFYKEILGQK... | Function: Catalyzes the fifth step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Catalyzes the condensation of phosphoenolpyruvate with 2,4-diacetamido-2,4,6-trideoxy-beta-l-altropyranose, forming pseudaminic acid (By similarity).
Catalytic Activity: 2,4-diacetamido... |
P55810 | MKIFAIQLQPLDDKNARKQIEQLKPFVSFEKRAAAERFRFLIDARRTLLGEVLIRHIIHEMYALPMEQIIFETEGNGKPVVRQIPSFHFNLSHSGDWVVGAVDDAPVGIDIEEIKPIDLAIAERFFSADEYQDLLSQPAERQEAYFFHLWSMKEAFIKLTGKGISYGLSSFTARLSEDGQATLRLPDHEAPCVVQTYSLDPAYQMAVCTRKPAAAEHVEILTCENMLSRLNNV | Function: Probably activates the peptidyl carrier protein (PCP) domains of surfactin synthetase by transferring the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to a serine residue. Required for the production of the lipopeptide antibiotic, surfactin.
Catalytic Activity: apo-[peptidyl-carrier protein] + CoA = aden... |
Q8MJG1 | MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKFSSQQASAKQSNASSDVEVEEKETSVSKEDTDPEEKASNEDVTKAIDITTPKAARRGRKRKAEKQVETEEAGVVTTATASANLKVSPKRGRPAATEVKIPKPRGRPKMVKQPCPSESDMITEEDKSKKKGQEEKQPKKQLKKDEEGQKEEEKPRKEPDKKEGKKEVESKRKNLAKTGVTSTSDSEEEGDDQEGEKKRKGGRNFQTAHRRNMLKGQHEKEAADRKRKQEE... | Function: Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stres... |
O75475 | MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKFSSQQAATKQSNASSDVEVEEKETSVSKEDTDHEEKASNEDVTKAVDITTPKAARRGRKRKAEKQVETEEAGVVTTATASVNLKVSPKRGRPAATEVKIPKPRGRPKMVKQPCPSESDIITEEDKSKKKGQEEKQPKKQPKKDEEGQKEEDKPRKEPDKKEGKKEVESKRKNLAKTGVTSTSDSEEEGDDQEGEKKRKGGRNFQTAHRRNMLKGQHEKEAADRKRKQEE... | Function: Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stres... |
Q99JF8 | MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKFSSQQASTKQSNASSDVEVEEKETNVSKEDTDQEEKASNEDVTKAVDITTPKAARRGRKRKAEKQVDTEEAGMVTAATASNVKASPKRGRPAATEVKIPKPRGRPKVVKQPCPSDGDMVIDEDKSKKKGPEEKQPKKQLKKEEEGQKEEEKPRKEPDKKEGKKEVESKRKNLAKPGVTSTSDSEDEDDQEGEKKRKGGRNFQAAHRRNMLKGQHEKEAGDRKRKQEEQM... | Function: Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stres... |
P0DPB1 | MNPTTATDAHERTSLLSGRPQSAANSTAPYERQVQPSRKSQCFTPVTVITIITLIYRLATTMVITTNIRVLHTVACQLWYHVNDPDVFPGGNIPEKYCALPGVDKYYAIMVSMTTVIDGLGGILGTGIASYMSSRFGRKPVLMFLLSCTMIDHLAILTVQNVYGWKQLVTFGLIMIVETIGNENTTVFLVSMYVVDVTEAERRTAALSSITGWLVLGGALAYSIGGSITTFLHSNSAVYIVSFSVTGIVLTFTAFVLPESFPAEKRDLLRLERLAETRGHSQSWTQKIKAVATVALEPMELLKPTFNPITGKANWRLVYC... | Function: Major facilitator-type transporter; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51791
Sequence Length: 471
Subcellular Location: Membrane
|
P0DPB2 | MSLERSTSPNPTERTSLLSDTASTISSRDDVEQSSLKQRRTPIPTGQLGGKVSMHSIIINAEGHLWPYINQFVNDIGVSDGNPRNVGFYSGLIESVFACGEVCSIFMLSRLSDRIGRRPVLLPSALGIAVFTALFGLSSSFTMMLTLRVCAGLLAGATPIVHSIVSELTDDTNNALVVPLYGLITPIGFAIGPLIGGTLEHAATKYPNVFGYELFRKYPYFLPSFVPCCMAIVGVTFGYFFLKETLPSLVKSKKRLERQRSSSSISSENSTLYGATEHIRDSTEETAADEEPDSKPKGITELIRDPSIRAIMASGTFLMF... | Function: Major facilitator-type transporter; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56907
Sequence Length: 523
Subcellular Location: Membrane
|
Q9LMY9 | MMKTKSEVLIFFFTLVLLLSMASSVILREDGFAPPKPSPTTHEKASTKGDRDGVECKNSDSEEECLVKKTVAAHTDYIYTQDLNLSP | Function: Promotes plant cell differentiation, organogenesis and somatic embryogenesis as well as cell proliferation.
PTM: Sulfation is important for activity and for the binding to a putative membrane receptor.
Sequence Mass (Da): 9653
Sequence Length: 87
Subcellular Location: Secreted
|
O12976 | MNDTSERRSNENSESQSNGQTQSSSQQVLEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRFDGQLIYTPFTEDTESVGQRALNSILNATIMISVIIVMTILLVVLYKYRCYKVIHGWLIISSLLLLFFFSYIYLGEVFKTYNVAVDYITLALLIWNFGVVGMICIHWKGPLLLQQAYLIMISALMALVFIKYLPEWTTWLILAVISVYDLVAVLSPKGPLRMLVETAQERNETLFPALIYSSTMIWLVNMADGDPGLKQSASTKTYNTQAPTAHPRSDSAASDDNGGFDTTWEDHRNAQIGPINST... | Function: Catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the presence of the other members of the gamma-secretase complex for protease activity. P... |
Q90X07 | MITFMNNSDSEDEPCNERTSLMSAESPPVPSYQDGLQASETREAQTHRKRQTGSSRSPNNVADEDASDSDVRVRESALENEEEELTLKYGAKHVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFSEDTPSVGQRLLNSVLNTIIMISVIVVMTVFLVVLYKYRCYKFIHGWLILSSFMLLFLFTYIYLGEVLKTYNVAMDYPTVILIIWNFGAVGMIRIHWKGPLQLQQAYLIMISALMVLVFIKYLPEWSAWVILGAISIYDLIAVLCPKGPLRMLXETAQERNQPIFPALIYSSAMIWTVGMAKPDTAAKGQ... | Function: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. Ma... |
P49810 | MLTFMASDSEEEVCDERTSLMSAESPTPRSCQEGRQGPEDGENTAQWRSQENEEDGEEDPDRYVCSGVPGRPPGLEEELTLKYGAKHVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKTYNVAMDYPTLLLTVWNFGAVGMVCIHWKGPLVLQQAYLIMISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYD... | Function: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. Ma... |
Q61144 | MLAFMASDSEEEVCDERTSLMSAESPTSRSCQEGRPGPEDGESTAQWRTQESEEDCEEDPDRYACSGAPGRPSGLEEELTLKYGAKRVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKTYNVAMDYPTLFLAVWNFGAVGMVCIHWKGPLVLQQAYLIVISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYD... | Function: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. Ma... |
O64668 | MESSILDSLGVEIIGVMAPVSICMFLVVLLTYSLSVTSDPQIRSAANLIYIENPSDSTTVKLEGSLANAIVFVVLIAAVTFILVLLFYYNFTNFLKHYMRFSAFFVLGTMGGAIFLSIIQHFSIPVDSITCFILLFNFTILGTLSVFAGGIPIVLRQCYMVVMGIVVAAWFTKLPEWTTWFILVALALYDLVAVLAPGGPLKLLVELASSRDEELPAMVYEARPTVSSGNQRRNRGSSLRALVGGGGVSDSGSVELQAVRNHDVNQLGRENSHNMDYNAIAVRDIDNVDDGIGNGSRGGLERSPLVGSPSASEHSTSVGT... | Function: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49308
Sequence Length: 453
Domain: The PAL motif is required for normal a... |
Q54ET2 | MKENEDEINKTDEKYKIKNPSNNGNNKNKNNNNNNNNNNNNNNNNNNNNNNNNNNNNNGNSNLENIEGLNKYNIYKKKKGKNESNTSLNNIYISSPNLSERSDNSIGSYCTNKTMKSENSIINIETLFRDSVSEQNSDECGSKVDKDLDEDDDDDDDETEVPELVDYSEMIVSILYPVCITMVIVVLAIRAISSSTSKNSQIVEISNDNSGGNGDSSSGADKMVFDSVVNSLIFLAVIILSTTIMVVLYKFKLMKALYAWLMGTSILLLGVFGGFLFLILLAYLNLGLDYVTFVIVVWNFSVGGIVCIFWYSPKLLNQGY... | Function: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors. Requires the other members of the gamma-secretase complex to have a protease activity (By similarity).
Location Topology: Multi-pa... |
Q9SIK7 | MDRNQRPRSILDSLGEELIAILTPVSICMFTVVLLVCILNSDPSSSSASFSSIATAAYSESDSDSSWDKFVGALLNSVVFVAAITVATFVLVLLFYLRCVKFLKFYMGFSAFIVLGNLGGEILVLLIDRFRFPIDSITFLILLFNFSVVGVFAVFMSKFSILITQGYLVWIGVLVAYFFTLLPEWTTWVLLVALALYDIAAVLLPVGPLRLLVEMAISRDEDIPALVYEARPVIRNDSRSVQRRVWREQRSSQNNANRNEVRVVESAEVEEEHVGSSERAEISVPLIDRRPEQAENSETFLEGIGLGSSGAIKLGLGDFI... | Function: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44012
Sequence Length: 397
Domain: The PAL motif is required for normal a... |
Q54DE8 | MSSDNNNDPFDLNEDGHDYFNRVSTTTSPNRQSINSSPKQSSPKSTNNNDDKNNIILDLNDNNNDNNNTNNYNDEDIDVDNKNKFENKDNTYNSNGGSNNKNKNKKKDNKSNNSSDNEEADENTSLISDSEPLLNKKEKDDEQIEIENLDGEDYDDEVSLQDFSSMIVSIIIPVSITMMAVVFFVKYLNNQTLYASTLSYTIAGGSSGGGSGADSITGNSFVDSLIVAGIVLGMIIVTTVAFVLLYKYRCLKILYGWLFLSVGMMLGSFGTTFFQAMLSAANLPLDYITFAFLIFNFTVCGIIGVFWYAHQYVNQLYLVI... | Function: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors. Requires the other members of the gamma-secretase complex to have a protease activity (By similarity).
Location Topology: Multi-pa... |
P52166 | MPSTRRQQEGGGADAETHTVYGTNLITNRNSQEDENVVEEAELKYGASHVIHLFVPVSLCMALVVFTMNTITFYSQNNGRHLLYTPFVRETDSIVEKGLMSLGNALVMLCVVVLMTVLLIVFYKYKFYKLIHGWLIVSSFLLLFLFTTIYVQEVLKSFDVSPSALLVLFGLGNYGVLGMMCIHWKGPLRLQQFYLITMSALMALVFIKYLPEWTVWFVLFVISVWDLVAVLTPKGPLRYLVETAQERNEPIFPALIYSSGVIYPYVLVTAVENTTDPREPTSSDSNTSTAFPGEASCSSETPKRPKVKRIPQKVQIESNT... | Function: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors (lin-12 or glp-1). Provides the major presenilin function compared to hop-1 and spe-4. Required cell-autonomously for correct neuri... |
Q4FS24 | MKALEVDNAQNIRTAFFISDGTAITAETLGRAILSQFASVPFETRVLPYVDNLERAEDAVVQINTAYQRDGLLPLVFDTIVSPEIREKINSAHSCNLDMYEGLIGRVAEETGVEPDGHSGHAHDNVDSETYKERIDAVHFALDNDDGARTRHYHAADIILIGVSRSGKTPTSLYLALQFGIRAANYPLTEEDLNDNQLPKALREHKHKLFGLIIDTDRLVKIRQERRAGSRYSSYQQCQQEQRAIQGIYTSQGIPSLDVSEMSVEEIATRILQMTGLKRRIG | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: [pyruvate, water dikinase] + ADP = [pyruvate, water dikinase]-phosphate + AMP + H(+)
Sequence Mass (Da): 31554
S... |
Q9HML8 | MSDTPQSEPRRSDDRSGADDATAAAAGSTDAAAAAVSSKTGGIAGPPGGPGEVDGDEPAVARTVGESDEQLQDAWTDYEFDGDAKVSVSDLDTYYGEERALESVSLDIPAESVTALIGPSGCGKSTFLRCLNRMNDRIRGARVEGRVALDDRDVYGDGVNLVELRRQVGMVFQEPNPFPKSIRDNISYGPRKHGDLETGLLARLLGRDDRDAERDLVERALRRAALWDEVNDRLGDNALGLSGGQQQRLCIARCLAVDPDVILMDEPASALDPVATAKIEDLIEELAEEYTVVVVTHNMQQAARISDQTAVFLTGGRLAE... | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37089
Sequence Length: 345
Subcell... |
Q88YK7 | MSTILTTENLSLFYGKKEALKGINIDFDDKGITALIGPSGCGKSTFLRCLNRMNDLIPNVTITGEVNFNGHNIYAPTTDTVQLRKEIGMVFQQPNPFPFSIYENVIYGLRLAGVHDKERLDAAVEKSLKQAAIWDEVKDRLHANALSLSGGQQQRVCIARVLAVEPDIILLDEATSALDPISSRMIEETLLNLRQDYTIITVTHNMQQASRISDRTAFFLNGELIEVNDTKQIFMNPVKQETNDYISGRFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28054
Sequence Length: 251
Subcell... |
Q7U0Z9 | MACERLGGQSGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSGDVKDAKRGN | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29996
Sequence Length: 276
Subcell... |
Q3IQI3 | MTLLSTLRGISSPARQQPGTQSESRRGGDTLAERGLAVAGVSHGFDGTAVLESVTLAVDRGETVAIIGPSGTGKTTLLRLLALFSEPDDGTIGLDGTDVWRQSERQRLAARRRIGMVFQKANLFDTTVRRNVRYGLSVRRSWRERLRSWLGGRKRQESVFEALDIVGLADAASQSASSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIEEAVDAARSRGLGVAVATHDMHQARRIADRIVVLLDGQVIEAGPTERVFSDPDDARARKFINGELVY | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30827
Sequence Length: 284
Subcell... |
Q1AXT9 | MEPKETLRQRWPGRGRTEETGAMKKSDDAPAVMTVEHLNMYYGSFMALKDVSMVIRKNRITALIGPSGCGKSTFIRSLNRMHEIVPGARVEGRVTLDGEDIYAPEVDPVRVRRRVGMVFQKPNPFPTMSIYDNVIAGLKLGRKRKKSELDEIVERTLRQAALWDEVKNKLSESGTSLSGGQQQRLCIARTLALEPEVILMDEPASALDPVSTQKIEDAMLELKEQYTVVIVTHNMQQAARVSDYTGFFFIEDMGQPGQLWEFGETEKIFSNPDRKETEDYVTGRFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32322
Sequence Length: 286
Subcell... |
Q97ZT9 | MEAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVIGRIS | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29010
Sequence Length: 257
Subcell... |
Q2S081 | MRPKLRIEDLHFWYGENHALQGISMDVQPNRVTALIGPSGCGKSTLLRCLNRMNELIQGTTLEGTILADGQDIYADDTDPVMVRRRIGMVFQKPNPFPKSIYKNVAWGAEINGYTGDLDALVERSLRQAALWDEVKDQLHSSALDLSGGQQQRLCIARTLAVQPDVVLMDEPASALDPIATSKIEETITELKKDYTIVIVTHNMQQASRISDETAFLYMGRLIEMSPTDQLFTRPEKDRTEAYVTGRFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27915
Sequence Length: 249
Subcell... |
Q5Z5B7 | MAAITLLRSASLPGLSDALARDAAAVQHVCSSYLPNNKEKKRRWILCSLKYACLGVDPAPGEIARTSPVYSSLTVTPAGEAVISSEQKVYDVVLKQAALLKRHLRPQPHTIPIVPKDLDLPRNGLKQAYHRCGEICEEYAKTFYLGTMLMTEDRRRAIWAIYVWCRRTDELVDGPNASHITPSALDRWEKRLDDLFTGRPYDMLDAALSDTISKFPIDIQPFRDMIEGMRSDLRKTRYKNFDELYMYCYYVAGTVGLMSVPVMGIAPESKATTESVYSAALALGIANQLTNILRDVGEDARRGRIYLPQDELAEAGLSDE... | Function: Catalyzes the conversion of geranylgeranyl diphosphate to phytoene. Mediates the first committed step in carotenoid biosynthesis.
Catalytic Activity: 2 (2E,6E,10E)-geranylgeranyl diphosphate = 15-cis-phytoene + 2 diphosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47583
Sequence Len... |
Q8LE92 | MSFGTRLLLFLILTLPLVTSSSPNTLHVSGIVKTGTTSRFLMMTIEDYDDPSANTRHDPSVPTNAKADTTP | Function: Promotes cellular proliferation and expansion.
PTM: The sulfation and the glycosylation are required for full activity.
Sequence Mass (Da): 7694
Sequence Length: 71
Subcellular Location: Secreted
|
Q2QLV9 | MASSSSAAALWTAAPHPHGSCIRIHAIFHQRHQRRGRRPVVVASSVRPLQAASLAVATAPVAVASRRTAAEEAVYEVVLRQAALVEEATHRRGAGAPRWAEEDAVDWGLLLGDAYHRCGEVCAEYAKTFYLGTQLMTPERRKAVWAIYVWCRRTDELVDGPNSSYITPKALDRWEKRLEDLFEGRPYDMYDAALSDTVSKFPVDIQPFKDMIEGMRLDLWKSRYRSFDELYLYCYYVAGTVGLMTVPVMGIAPDSKASTESVYNAALALGIANQLTNILRDVGEDSRRGRIYLPLDELAEAGLTEEDIFRGKVTDKWRKF... | Function: Catalyzes the conversion of geranylgeranyl diphosphate to phytoene. Mediates the first committed step in carotenoid biosynthesis.
Catalytic Activity: 2 (2E,6E,10E)-geranylgeranyl diphosphate = 15-cis-phytoene + 2 diphosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 44729
Sequence Len... |
P37273 | DPDIVLPGNLGLLSEAYDRCGEVCAEYAKTFYLGTMLMTPDRRRAIWAIYVWCRRTDELVDGPNASHITPQALDRWEARLEDIFNGRPFDMLDAALSDTVSRFPVDIQPFRDMVEGMRMDLWKSRYNNFDELYLYCYYVAGTVGLMSVPIMGIAPESKATTESVYNAALALGIANQLTNILRDVGEDARRGRVYLPQDELAQAGLSDEDIFAGKVTDKWRIFMKKQIQRARKFFDEAEKGVTELSSASRWPVLASLLLYRKILDEIEANDYNNFTRRAYVSKPKKLLTLPIAYARSLVPPKSTSCPLAKT | Function: Catalyzes the reaction from prephytoene diphosphate to phytoene.
Catalytic Activity: 2 (2E,6E,10E)-geranylgeranyl diphosphate = 15-cis-phytoene + 2 diphosphate
Sequence Mass (Da): 35224
Sequence Length: 310
Pathway: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-phytoene from geranylgeranyl diphosp... |
Q8S8P7 | MGYSSSSRIGLCLFLFFTFALLSSARISLSFSENEMTVVPERSLMVSTNDYSDPTANGRHDPPRGGRGRRR | Function: Promotes cellular proliferation and expansion.
PTM: The sulfation and the glycosylation are required for full activity.
Sequence Mass (Da): 7904
Sequence Length: 71
Subcellular Location: Secreted
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B6UV92 | MMSTTTTSSAAGSPVCARRRQRVFVDVPRRRATSLARVEYAKMAPPPPPPCSVRAAGSNPIGCLEVAEPWSGAAPPPLPPLPGHLHVAAPAAEDDDDALAAAAAAVPSEQRVHDVVLKQAALAAAAPEMRRPAQLAERERVAGGLNAAFDRCGEVCKEYAKTFYLATQLMTPERRRAIWAIYVWCRRTDELVDGPNASHMSALALDRWESRLDDIFAGRPYDMLDAALSHTVATFPVDIQPFRDMIEGMRLDLTKSRYRSFDELYLYCYYVAGTVGLMTVPVMGISPDSRANTETVYKGALALGLANQLTNILRDVGEDA... | Function: Catalyzes the conversion of geranylgeranyl diphosphate to phytoene. Mediates the first committed step in carotenoid biosynthesis. May play a role in regulating carotenoid flux in response to abiotic stress in roots. May control flux to carotenoid precursors that are required for abiotic stress-induced abscisi... |
P52990 | MSSGFEFQLASYTTMPVTLLETLYSMRKKIFSDRLEWKVRVSHAFEFDEYDNAATTYLVGSWNGVPLAGLRLINTCDPYMLEGPFRSFFDCPAPKNAAMAESSRFFVDTARARSLGILHAPLTEMLLFSMHNHAALSGLQSIITVVSKAMARIVRKSGWEHHVLSTGEASPGETVLLLEMPVTADNHQRLLGNIALRQPVTDDLLRWPIALGVSGSAPQACMHSAA | Function: Required for the synthesis of OHHL (N-(3-oxohexanoyl)-L-homoserine lactone), an autoinducer molecule.
Catalytic Activity: a fatty acyl-[ACP] + S-adenosyl-L-methionine = an N-acyl-L-homoserine lactone + H(+) + holo-[ACP] + S-methyl-5'-thioadenosine
Sequence Mass (Da): 24946
Sequence Length: 226
EC: 2.3.1.184
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Q8IYL9 | MNSTCIEEQHDLDHYLFPIVYIFVIIVSIPANIGSLCVSFLQAKKESELGIYLFSLSLSDLLYALTLPLWIDYTWNKDNWTFSPALCKGSAFLMYMNFYSSTAFLTCIAVDRYLAVVYPLKFFFLRTRRFALMVSLSIWILETIFNAVMLWEDETVVEYCDAEKSNFTLCYDKYPLEKWQINLNLFRTCTGYAIPLVTILICNRKVYQAVRHNKATENKEKKRIIKLLVSITVTFVLCFTPFHVMLLIRCILEHAVNFEDHSNSGKRTYTMYRITVALTSLNCVADPILYCFVTETGRYDMWNILKFCTGRCNTSQRQRK... | Function: Receptor for the glycosphingolipid psychosine (PSY) and several related glycosphingolipids . Plays a role in immune response by maintaining lysosome function and supporting phagocytosis-mediated intracellular bacteria clearance . May have a role in activation-induced cell death or differentiation of T-cells (... |
P37271 | MSSSVAVLWVATSSLNPDPMNNCGLVRVLESSRLFSPCQNQRLNKGKKKQIPTWSSSFVRNRSRRIGVVSSSLVASPSGEIALSSEEKVYNVVLKQAALVNKQLRSSSYDLDVKKPQDVVLPGSLSLLGEAYDRCGEVCAEYAKTFYLGTLLMTPERRKAIWAIYVWCRRTDELVDGPNASHITPMALDRWEARLEDLFRGRPFDMLDAALADTVARYPVDIQPFRDMIEGMRMDLKKSRYQNFDDLYLYCYYVAGTVGLMSVPVMGIDPKSKATTESVYNAALALGIANQLTNILRDVGEDARRGRVYLPQDELAQAGL... | Function: Catalyzes the reaction from prephytoene diphosphate to phytoene.
Catalytic Activity: 2 (2E,6E,10E)-geranylgeranyl diphosphate = 15-cis-phytoene + 2 diphosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47487
Sequence Length: 422
Pathway: Carotenoid biosynthesis; phytoene biosynthesis;... |
P37272 | MSVALLWVVSPCDVSNGTGFLVSVREGNRIFDSSGRRNLACNERIKRGGGKQRWSFGSYLGGAQTGSGRKFSVRSAIVATPAGEMTMSSERMVYDVVLRQAALVKRQLRSTDELDVKKDIPIPGTLGLLSEAYDRCSEVCAEYAKTFYLGTMLMTPERRKAIWAIYVWCRRTDELVDGPNASHITPAALDRWEDRLEDVFSGRPFDMLDAALSDTVSKFPVDIQPFRDMIEGMRMDLRKSRYRNFDELYLYCYYVAGTVGLMSVPIMGIAPESKATTESVYNAALALGIANQLTNILRDVGEDARRGRVYLPQDELAQAG... | Function: Catalyzes the two steps reaction converting geranylgeranyl diphosphate to phytoene via prephytoene diphosphate.
Catalytic Activity: 2 (2E,6E,10E)-geranylgeranyl diphosphate = 15-cis-phytoene + 2 diphosphate
Sequence Mass (Da): 47126
Sequence Length: 419
Pathway: Carotenoid biosynthesis; phytoene biosynthesis;... |
Q9I5A5 | MHTFFIAPTGFGVGLTSISLGLLRALERAGLKVGFFKPIAQLHPGDLGPERSSELVARTHGLDTPKPLPLAQVERMLGDGQLDELLEEIISLYQRAAADKDVVIVEGMVPTRHASYAARVNFHLAKSLDAEVILVSAPENETLTELTDRIEIQAQLFGGPRDPKVLGVILNKVRGEADAANAEDGVADFARRLTEHSPLLRDDFRLIGCIPWQDELNAARTRDIADLLSARVINAGDYEQRRVQKIVLCARAVPNTVQLLKPGVLVVTPGDRDDIILAASLAAMNGVPLAGLLLCSDFPPDPRIMELCRGALQGGLPVLS... | Function: Involved in acetate metabolism. In combination with LdhA and AckA, allows fermentation of pyruvate, enhancing long-term survival under anaerobic conditions.
Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 75697
Sequence Length: 704
Domain: The N-terminal region seems to... |
Q88PS4 | MQTFFIAPTDFGVGLTSISLGLVRTLERAGLKVGFFKPIAQPHPGDTGPERSTELVARTHGIKPPVPLSLAHVERMLGDGQLDELLEEIIRLYQQACVGNDVVVVEGMVPTRHASYAARVNLHLAKSLDAEVILVSAPENEVLSELSGRVELQAQLFGGPRDPKVLGVILNKVRTDESMADFATRLREHSPLLRGNDFRLLGCIPYQPELNAPRTRDVAELLGAQVLNAGDYEQRRMSKIIICARTVANTVPLLTSGTLVVTPGDRDDIILAVSLAAINGVPLAGLLLTSDSKPDVRILGLCRGALQAGLPILSVSTGSY... | Function: Involved in acetate metabolism.
Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 74643
Sequence Length: 695
Domain: The N-terminal region seems to be important for proper quaternary structure. The C-terminal region contains the substrate-binding site (By similarity).
Pat... |
Q8CJR5 | MTRSVYVTGIDRGDGRQVVELGVMELLTRQVDRVGVFRPLVHDGPDRLFELLRARYRLSQDPATVYGMDYQEASLLQAEQGVDELVSALVDRFHLVARDYDVVLVLGTDYADTQFPDELSLNARLANEFGASVLPVVGGRKQTADSVLAETHNAFRAYDGLGCDVLAMVTNRVAREDRDEIAERLAHRLPVPCWVVPDEPALSAPTVSQIAHALGAEIVLGDDSGLARDALDFVFGGAMLPNLLAALTPGCLVITPGDRADLVIGTLAAHSAGTPPIAGVLLTLNEVPGEGILTLAARLAPGTPVLSVTGTSFPTAERLF... | Function: Involved in acetate metabolism.
Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 74047
Sequence Length: 697
Domain: The N-terminal region seems to be important for proper quaternary structure. The C-terminal region contains the substrate-binding site (By similarity).
Pat... |
P73662 | MTSSLYLSTTEARSGKSLVVLGILDLILKKTTRIAYFRPIIQDPVNGKHDNNIILVLENFRLQQTYTDSFGLYFHEAVSLASDGAIDQVLDRILAKYRHLADQVDFILCEGSDYLGEESAFEFDLNTTIAKMLNCPILLLGNAMGNTIADSLQPIDMALNSYDQESCQVVGVIINRVQPELATEIQAQLEQRYGDRPMVLGTIPQDIMLKSLRLREIVSGLNAQVLSGADLLDNLVYHHLVVAMHIAHALHWLHEKNTLIITPGDRGDIILGVMQAHRSLNYPSIAGILLTADYHPEPAIMKLIEGLPDAPPLLLTSTHT... | Function: Involved in acetate metabolism.
Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 76477
Sequence Length: 697
Domain: The N-terminal region seems to be important for proper quaternary structure. The C-terminal region contains the substrate-binding site (By similarity).
Pat... |
Q7CJ96 | MSRTIMLIPTGTSVGLTSVSLGVIRSMEQKGVSLSVFKPIAQPRAGNDAPDQTTTIIRANSSITAAEPLNMNYVETLLSSNQQDVLMEEIVARYHENTKDAEVVLVEGLVPTRKHQFANALNYEIAKTLNAEIVFVIALGNDSPDQLKERIELARSSFGGSKNKNITGVIINKLNAPVDEQGRTRPDLSEIFDDSTKASVANIDPSQLFANSPIPVLGCVPWSFELIATRAIDMAKHLNARIINEGDIKTRRVKSVTFCARSIPHMLEHFRPGSLLVTSADRPDVLVSACLAAMNGVEIGAILLTGGYAIDDRINNLCER... | Function: Involved in acetate metabolism.
Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 77402
Sequence Length: 717
Domain: The N-terminal region seems to be important for proper quaternary structure. The C-terminal region contains the substrate-binding site (By similarity).
Pat... |
P37439 | MFKNAFANLQKVGKSLMLPVSVLPIAGILLGVGSANFSWLPAVVSHVMAEAGGSVFANMPLIFAIGVALGFTNNDGVSALAAVVAYGIMVKTMAVVAPLVLHLPAEEIAAKHLADTGVLGGIISGAIAAYMFNRFYRIKLPEYLGFFAGKRFVPIISGLAAIFTGVVLSFVWPPIGTAIQAFSQWAAYQNPVVAFGIYGFIERCLVPFGLHHIWNVPFQMQIGEYTNAAGQVFHGDIPRYMAGDPTAGMLSGGFLFKMYGLPAAAIAIWHSAKPENRAKVGGIMISAALTSFLTGITEPIEFSFMFVAPILYIIHAILAG... | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in... |
Q9XS65 | MGALCTLWLGLVLLGVLGALQTSAQAQVSLQPNFQQDKFLGRWFTSGLASNSSWFREKKNVLSMCMSVVAPTADGGLNLTSTFLRKDQCETRTLLLRPAGTPGCYSYTSPHWGSTHDVWVVATNYEEYALLYTAGSKGLGQDFHMATLYSRTQTPKAEIKEKFSTFAKTQGFTEDAIVFLPQTDKCMEENK | Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. B... |
P41222 | MATHHTLWMGLALLGVLGDLQAAPEAQVSVQPNFQQDKFLGRWFSAGLASNSSWLREKKAALSMCKSVVAPATDGGLNLTSTFLRKNQCETRTMLLQPAGSLGSYSYRSPHWGSTYSVSVVETDYDQYALLYSQGSKGPGEDFRMATLYSRTQTPRAELKEKFTAFCKAQGFTEDTIVFLPQTDKCMTEQ | Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation . Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. ... |
O09114 | MAALRMLWMGLVLLGLLGFPQTPAQGHDTVQPNFQQDKFLGRWYSAGLASNSSWFREKKAVLYMCKTVVAPSTEGGLNLTSTFLRKNQCETKIMVLQPAGAPGHYTYSSPHSGSIHSVSVVEANYDEYALLFSRGTKGPGQDFRMATLYSRTQTLKDELKEKFTTFSKAQGLTEEDIVFLPQPDKCIQE | Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. B... |
P22057 | MAALPMLWTGLVLLGLLGFPQTPAQGHDTVQPNFQQDKFLGRWYSAGLASNSSWFREKKELLFMCQTVVAPSTEGGLNLTSTFLRKNQCETKVMVLQPAGVPGQYTYNSPHWGSFHSLSVVETDYDEYAFLFSKGTKGPGQDFRMATLYSRAQLLKEELKEKFITFSKDQGLTEEDIVFLPQPDKCIQE | Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. B... |
Q95L14 | MPPSGLELMNGQVLPAFLLCSALLVIKMYVVAVITGQVRLRKKAFANPEDAQRHGGLQYCRNDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPFVARMHFLVFFLGRMVHTVAYLGKLRAPTRSLAYTLAQLPCASMALQIVWEAARHL | Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (By similarity). Plays a key role in inflammation respo... |
O14684 | MPAHSLVMSSPALPAFLLCSTLLVIKMYVVAIITGQVRLRKKAFANPEDALRHGGPQYCRSDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPFVAWMHFLVFLVGRVAHTVAYLGKLRAPIRSVTYTLAQLPCASMALQILWEAARHL | Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli . Plays a key role in inflammation response, fever and ... |
Q6PWL6 | MPAHSLAMSSPALPAFLLCSTLLVIKMYVVAIITGQVRLRKKAFANPEDALRHGGPQYCRSDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPFVAWMHFLVFLLGRVVHTVAYLGKLRAPIRSVTYTLAQLPCASMALQILWEAARHL | Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (By similarity). Plays a key role in inflammation respo... |
Q181A2 | MYVVVGLGNPGKKYEKTRHNVGFDVIDILAKEYNISVTKIKHKALIGEGRVGTEKVLLVKPQTYMNLSGETLIDIYKYYKVDLSNIVVVYDDIDLEVGKIRIRKKGSGGTHNGMKSITKCLGSNDFPRVRVGVSKPEAGQDLADFVLSRFRKEESDNINEALEKAADAIDSIIRENIDMSMNKYNG | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20773
Sequence Length: 186
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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A0PXL3 | MFLIVGLGNPGKEYEHTRHNVGFDIIDVISEKYNIDLNKKKFKGMYGDGTIANEKVILLKPLTYMNLSGESIKEVTDFYKIPKENVIVIYDDISLEVGRMRIREKGSAGGHNGIKNIIAHFGSDVFPRIKVGVGQPVQRDLVSHVLGKFNKDDREILSKVFEAASDAAENIIEKGTAEAMNKFNGFKA | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20960
Sequence Length: 188
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q899I4 | MFLLVGLGNPGKEYEKTRHNIGFEAVDKISYEYNIPIKRERFKGVFGDGRISNEKVILLKPTTYMNLSGESLREIIEYYNIPITNVIVIYDDVDLEVGRLRIRTKGSAGGHNGIKSIIYNLNSEDFIRLRIGVGKPQRDMVSHVLGKFAKEDEKNIEEVLKIIPELAYTIINQGPQEAMNKYNNFRAE | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21510
Sequence Length: 188
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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B5Y8L1 | MLLIVGLGNPGIEYEKTRHNIGWWVLDLLRTKLTGLNLRLLCYSRVYELKHELKKEVDFIVYPLTYMNNSGKAVKCLYEPRMDLVVIHDDLDLTVGKTRVRFGGSSAGHKGVSSIIDALGTDSFWRVKVGIGRPFSKQEVINYVLGEPQKNEKEVLIRAADYIADQLCLLITDRNFSRFQQNINSFNSNENN | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21936
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q6NI78 | MTSPYLIVGLGNLGPEYTKTRHNIGYMAIDELLTRTSPMPATLTVHKKTNTLVAETRLGTQKVIVAKPRAFMNVTGPSVRKLADFFTVDRNRIVVLYDDLDLEFGAIKFRHGGGDHGHNGLKSITQALGTKDYIRGGIGIGRPPGRMAPKSFVLKPFSKIEQSELPIVCADAADEVEKITTSEL | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20122
Sequence Length: 184
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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B6J9D9 | MSGGVKLIAGLGNPGDQYARTRHNVGAWFLETLAQQRNQSLAKENKFHGFVAKCNDYWLLKPTTFMNESGQAVAALARFYKIKPSEILIAHDELDFPAGDIRLKEGGGHGGHNGLRNIIQHLGSSDFYRLRIGINHPGYKDRVTPYVLSPPSENDRIAILAAIEKGLRLIPELVQGDFQKVMRELHS | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20816
Sequence Length: 187
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q1H3J3 | MNGIRLFVGLGNPGAQYEDTRHNAGFWWIDQLCAQTASKTTLEAKFFGLSGRLNGHADTWLLKPTTFMNASGRAVAALARFYKIPAEQILVVHDELDLPPGAARLKKGGGHSGHNGLKDIAAQLGTNDFWRLRLGIGHPGDRSAVVNYVLNAPLRDEMQQIAYAMDDSMLVLPQLLEGKFEEAMLKLHTKTK | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21124
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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B3E0Q7 | MGVFHIVVGLGNPGQEYEKTRHNIGWRVVEELVKRQNLSFKIDKKAKSKVAFKEKLVFVLPLTYMNLSGQALSYLLQKEKCSSKDILVILDDISLPLGKLRFRPKGSSGGHKGLESIIEELHTEDIPRLRLGIGPLPEGEQLADYVLKPFLEEEKDKVEEMILKAIQFFECLQKEGIEIALNKLSA | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21044
Sequence Length: 186
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q60363 | MKMVVVIRNDLGMGKGKMVAQGGHAIIEAFLDAKRKNPRAVDEWLREGQKKVVVKVNSEKELIDIYNKARSEGLPCSIIRDAGHTQLEPGTLTAVAIGPEKDEKIDKITGHLKLL | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 12670
Sequence Length: 115
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q8TV04 | MYKQVIVVRGDLKLSRGKLAAQVAHASLGAFLRAKESGAPVEEWLREGQKKVVLKCKDKEELLELHELAKRRGLPSFLVRDAGLTELEPGTVTCLGIGPEREEEIDRVTGDLPLLR | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 12871
Sequence Length: 116
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q8Q0M4 | MSEYKQCIVTRDDLKLSKGKFAVQVAHAALSAAEWASKGDLEKWKEGGQKKIVLKVPSIKELYELKEKARREGLPTALIQDAGLTEIPPGTVTVLGIGPAKEELIDKITKDLKLV | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 12612
Sequence Length: 115
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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B8IFN4 | MRLFVGLGNPGSRYAGNRHNIGFMALDAIARRHRAAPWRRKFQGEASEAVLGSERVLLLKPETYMNESGRAVAEAQRFYKIALDDVVVFHDELDLGPTKVRVKRGGGNAGHNGLRSITALCGNEYWRVRLGIGHPGDKALVHAYVLNDFAKAERPWVDDLCDALADHAALLAAGEDAAFQNKVHLALQGRGWDDVRRVGDKQA | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 22363
Sequence Length: 203
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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A2SKU1 | MIRLMVGLGNPGPEYEATRHNAGFWWVDAVARQLKASLHAERAYHGLVARVNTPVGPVWLLEPQTYMNVSGKSVAALARFFKIAPEEILVAHDELDLPPGEMKLKQGGGHAGHNGLRDIHAQLGSTDYWRLRLGIGHPGVKAEVANYVLGKPMREHREAIDACIVRSLTAVDALLSGDMSKATLRLHTSKPPRPKPPRPVAVAGTGVPAAADAPRAPDIAGSAPATTQGDPP | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 24771
Sequence Length: 232
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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B8EK40 | MILLVGLGNPGKAYAGNRHNIGFMALDQIARDYSAPPFRSKFNGLISEITLAGERCVLLAPQTYMNDSGRSVGEAARYLKIEPKDIVVLHDELDLPAGKVRVKTGGGNAGHNGLKSITAHIGNEYRRVRLGIGHPGDRALVHNYVLGDFAKSEAAWVEALCKAVAASAPLLAKGEDDAFQTKIFKDMEAALGKNVP | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20992
Sequence Length: 196
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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P69814 | MTNLFVRSGISFVDRSEVLTHIGNEMLAKGVVHDTWPQALIAREAEFPTGIMLEQHAIAIPHCEAIHAKSSAIYLLRPTNKVHFQQADDDNDVAVSLVIALIVENPQQQLKLLRCLFGKLQQPDIVETLITLPETQLKEYFTKYVLDSDE | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of GatA, GatB and GatC is invo... |
P68910 | MSSPRERRPASQAPRLSRRPPAHQTSRSSPDTTAPTGSGLSNRFVNDNGIVTDTTASGTNCPPPPRAAARRASSPGESPQLVIFDLDGTLTDSARGIVSSFRHALNHIGAPVPEGDLATHIVGPPMHETLRAMGLGESAEEAIVAYRADYSARGWAMNSLFDGIGPLLADLRTAGVRLAVATSKAEPTARRILRHFGIEQHFEVIAGASTDGSRGSKVDVLAHALAQLRPLPERLVMVGDRSHDVDGAAAHGIDTVVVGWGYGRADFIDKTSTTVVTHAATIDELREALGV | Function: Required for growth within macrophages. Catalyzes the phosphorylation of PtpA on the tyrosine residues at positions 128 and 129, thereby increasing PtpA phosphatase activity and promoting pathogenicity.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[... |
P0A436 | MKRKIIVACGGAVATSTMAAEEIKELCQSHNIPVELIQCRVNEIETYMDGVHLICTTARVDRSFGDIPLVHGMPFVSGVGIEALQNKILTILQG | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The enzyme II complex composed of GatA, GatB and GatC is involved in ... |
P37188 | MKRKIIVACGGAVATSTMAAEEIKELCQNHNIPVELIQCRVNEIETYMDGVHLICTTAKVDRSFGDIPLVHGMPFISGIGIEALQNKILTILQG | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The enzyme II complex composed of GatA, GatB and GatC is involved in ... |
P53433 | MTYRVCFVCTGNICRSPMAEAVFRARVEDAGLGHLVEADSAGTGGWHEGEGADPRTEAVLADHGYGLDHAARQFQQSWFSRLDLVVALDAGHLRALRRLAPTERDAAKVRLLRSYDPAVAGGDLDVPDPYYGGRDGFEECLEMVEAASTGLLAAVREQVEGRAA | Function: Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. May be involved in the regulation of sulfur amino acid metabolism.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 17690
Sequence Length: 16... |
P42909 | MTSPNILLTRIDNRLVHGQVGVTWTSTIGANLLVVVDDVVANDDIQQKLMGITAETYGFGIRFFTIEKTINVIGKAAPHQKIFLICRTPQTVRKLVEGGIDLKDVNVGNMHFSEGKKQISSKVYVDDQDLTDLRFIKQRGVNVFIQDVPGDQKEQIPD | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in N-acetylgalactosamine transport.
... |
P42904 | MPNIVLSRIDERLIHGQVGVQWVGFAGANLVLVANDEVAEDPVQQNLMEMVLAEGIAVRFWTLQKVIDNIHRAADRQKILLVCKTPADFLTLVKGGVPVNRINVGNMHYANGKQQIAKTVSVDAGDIAAFNDLKTAGVECFVQGVPTEPAVDLFKLL | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in N-acetylgalactosamine transport.
... |
I6WXK4 | MAVRELPGAWNFRDVADTATALRPGRLFRSSELSRLDDAGRATLRRLGITDVADLRSSREVARRGPGRVPDGIDVHLLPFPDLADDDADDSAPHETAFKRLLTNDGSNGESGESSQSINDAATRYMTDEYRQFPTRNGAQRALHRVVTLLAAGRPVLTHCFAGKDRTGFVVALVLEAVGLDRDVIVADYLRSNDSVPQLRARISEMIQQRFDTELAPEVVTFTKARLSDGVLGVRAEYLAAARQTIDETYGSLGGYLRDAGISQATVNRMRGVLLG | Function: Essential virulence factor that promotes mycobacterial survival within host macrophages . Acts as a phosphatase that possesses triple substrate specificity toward phosphotyrosine, phosphoserine/threonine and phosphoinositides . Supports mycobacteria survival during infection by modulating the normal host sign... |
Q2FF13 | MKILFVCTGNTCRSPLAESIAKEVMPNHQFESRGIFAVNNQGVSNYVEDLVEEHHLAETTLSQQFTEADLKADIILTMSYSHKELIEAHFGLQNHVFTLHEYVKEAGEVIDPYGGTKEMYVHTYEELVSLILKLKDIIC | Function: Dephosphorylates the phosphotyrosine-containing proteins.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 15788
Sequence Length: 139
EC: 3.1.3.48
|
Q15256 | MRRAVCFPALCLLLNLHAAGCFSGNNDHFLAINQKKSGKPVFIYKHSQDIEKSLDIAPQKIYRHSYHSSSEAQVSKRHQIVNSAFPRPAYDPSLNLLAMDGQDLEVENLPIPAANVIVVTLQMDVNKLNITLLRIFRQGVAAALGLLPQQVHINRLIGKKNSIELFVSPINRKTGISDALPSEEVLRSLNINVLHQSLSQFGITEVSPEKNVLQGQHEADKIWSKEGFYAVVIFLSIFVIIVTCLMILYRLKERFQLSLRQDKEKNQEIHLSPITLQPALSEAKTVHSMVQPEQAPKVLNVVVDPQGRGAPEIKATTATS... | Function: Sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs bind to a dephosphorylated kinase interacting motif, phosphorylation of which by the protein kinase A complex releases the MAPKs for activation and translocation into the nucleu... |
Q62132 | MRRAVGFPALCLLLNLHAAGCFSRNNDHFLAIRQKKSWKPVFIYDHSQDIKKSLDIAQEAYKHNYHSPSEVQISKHHQIINSAFPRPAYDPSLNLLAESDQDLEIENLPIPAANVIVVTLQMDITKLNITLLRIFRQGVAAALGLLPQQVHINRLIEKKNQVELFVSPGNRKPGETQALQAEEVLRSLNVDGLHQSLPQFGITDVAPEKNVLQGQHEADKIWSKEGFYAVVIFLSIFIIIVTCLMIIYRLKERLQLSLRQDKEKNQEIHLSPIARQQAQSEAKTTHSMVQPDQAPKVLNVVVDPQGQCTPEIRNSTSTSV... | Function: Sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs bind to a dephosphorylated kinase interacting motif, phosphorylation of which by the protein kinase A complex releases the MAPKs for activation and translocation into the nucleu... |
Q84K35 | MASSLAQSRISNLQNHLSPLEANNKLRSLVKISPQVSEALSNGRAVVALESTIISHGMPYPQNLQTAKEVESIVRENGAIPATIAILNGVPCIGLSEEELERLASLGKSVQKTAGRDIANVVATRGNGATTVSATLFFASMVGIQVFVTGGIGGVHRHANHSMDISSDLTALGRTPIAVISAGVKSILDIPKTLEYLETQEVYVAAYKSDEFPAFFTEKSGCKAPSRVNSPEDCARVIDANMKLNRQAGILFAIPIPKHHSAAGNLIESATQRALTEAREQNVTGNAETPFLLARVNELTGGTSLAANIALVKNNALIGS... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil . Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway . Acts together with the pseudouridine kinase PUKI in the peroxi... |
D2Y3X2 | MAFALPSSLVSVCNKSFIKPSSLTPSTLRFHKLSFIDQSLSNMYIPCAFFYPKVQQRLEDSKNSDELSHIAHLLQTSLSQTLVSYYPYAGKLKDNATVDCNDMGAEFLSVRIKCSMSEILDHPHASLAESIVLPKDLPWANNCEGGNLLVVQVSKFDCGGIAISVCFSHKIGDGCSLLNFLNDWSSVTRDRTTTTLVPSPRFVGDSVFSTQKYGSLITPQILSDLNQCVQKRLIFPTDKLDALRAKVAEESGVKNPTRAEVVSALLFKCATKASSSMLPSKLVHFLNIRTMIKPRLPRNAIGNLSSIFSIEATNMQDMEL... | Function: Participates in the biosynthesis of capsaicinoids in pungent cultivars of Capsicum annuum . Capsaicinoids, the alkaloids responsible for the heat or pungency of chili pepper, are synthesized from phenylpropanoid intermediates in the placental tissue of chili peper fruit (Probable). Can transfer an acyl from (... |
O13729 | MGMGFNPIKALFTGIGTVCVGVGALLSILCIINQTQHNIAFQNIYFIQLNTTSIFSVANQTAVVNNTSNLLNELTGTLVDTLETYIDQGATDLIEQVEQEMKDVSELPDWYSIGLWNYCQGNSSDYTNPTYCSTPSPSYYFNPLTMLETSINNATGSQINITLPSEVDLGLKVLKGACYAMRAMYILGFIFFALTIVSIVISCLPFFGPLFLNVFSFFATIFTFIAAVIAVATYRIAISELEKNIEILNIPIVLGKKIYAYSFLSAAAGLAACILYFIGNLTSGYSPL | Function: Contributes to the wild-type cellular response to nitrogen stress through signaling pathways that regulate the expression of genes involved in amino acid biosynthesis. Required for wild-type filamentous growth, cell growth, and cell-cell adhesion (By similarity).
Location Topology: Multi-pass membrane protein... |
Q06991 | MRNFFTLFFAAIFSLGALILAIVACAGSTKNYSPINKIYCAELDLSQMKVSTVLPSLSSATLSSLGLPSYINIGLWSYCTVDSSHNIQSCSSPHGIQNFNLSSLVYDNINNNEALELMDSVASVVLPEKLKSKMTYYNNLVKCMFITILIGIVLTFVNLVFNVLRWIIHIRPLTWFGAFFSFFAFAALLVSIGSCLGTYSYIKYILKHNYSDYGISMSIGRNYQGLMWGAVVGALLNFILWCSVRSRPTVIYANAPIEEKPLI | Function: Contributes to the wild-type cellular response to nitrogen stress through signaling pathways that regulate the expression of genes involved in amino acid biosynthesis. Required for wild-type filamentous growth, cell growth, and cell-cell adhesion.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane pr... |
P46354 | MKDRIERAAAFIKQNLPESPKIGLILGSGLGILADEIENPVKLKYEDIPEFPVSTVEGHAGQLVLGTLEGVSVIAMQGRFHFYEGYSMEKVTFPVRVMKALGVEALIVTNAAGGVNTEFRAGDLMIITDHINFMGTNPLIGPNEADFGARFPDMSSAYDKDLSSLAEKIAKDLNIPIQKGVYTAVTGPSYETPAEVRFLRTMGSDAVGMSTVPEVIVANHAGMRVLGISCISNAAAGILDQPLSHDEVMEVTEKVKAGFLKLVKAIVAQYE | Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
Catalytic Activ... |
P81989 | TTTTPPSTPPLDDPATDPFLVARAAADHIAQATGVEGHDMALVLGSGWGGAAELLGEVVAEVPTHEIPGFSAPAVAGHLSVTRSIRVERADGSVRHALVLGSRTHLYEGKGVRAVVHGVRTAAATGAETLILTNGCGGLNQEWGAGTPVLLSDHINLTARSPLEGPTFVDLTDVYSPRLRELAHRVDPTLPEGVYAQFPGPHYETPAEVRMAGILGADLVGMSTTLEAIAARHCGLEVLGVSLVTNLAAGISPTPLSHAEVIEAGQAAGPRISALLADIAKR | Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
Catalytic Activ... |
P77834 | MNRTAIEQAAQFLKEKFPTSPQIGLILGSGLGVLADEIEQAIKIPYSDIPNFPVSTVEGHAGQLVYGQLEGATVVVMQGRFHYYEGYSFDKVTFPVRVMKALGVEQLIVTNAAGGVNESFEPGDLMIISDHINNMGGNPLIGPNDSALGVRFPDMSEAYSKRLRQLAKDVANDIGLRVREGVYVANTGPAYETPAEIRMIRVMGGDAVGMSTVPEVIVARHAGMEVLGISCISNMAAGILDQPLTHDEVIETTEKVKADFLRFVKAIVRNMAKN | Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
Catalytic Activ... |
P46862 | MTYTLLDPDELARRAAQVIGERTGILKHDVAVVLGSGWSSAVAALGSSRAVFPQAELPGFITPNAAGHTGELLSVRIGAHRVLVLAGRIHPYEGHDLRHVVHPVRTACAAGARIIVLTNAAGGLRADMAVGQLVLISDHLNLTTRSPLVGTHFVDLTNAYTTRLRKLASDTDPTLTEGVYAAQPGPHYETPAEIRMLRMLGADLVGMSTVHETIAARAAGAEVLGVSLVTNLAAGITGKPLNHAEVLAAGTASANRIGSLLADIIARF | Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
Catalytic Activ... |
J9VYP5 | MPEITAFPQPKSDLSILLLGAGGREHALAFKLAQSSRVARIVVCPGNGGTALMGGKVSNLALPWGAPPAFRSIVEWAQKENIDLVVPGPEQPLVDGVEGAFKKVGIPVFGPSPAAAMLEGSKSLSKEFMARHNIPTAAFRSFTSTQYEDAVAYIKSKPFTSGRSVIKASGLAAGKGVLIPETDEEAFAALKSVMVDKEFGDAGDEVVVEEYLSGPEISVLAFSDGYTIVPMPAAQDHKRIGEGDTGLNTGGMGAYAPAPIATKEIMERCVKDVLEPTIKGMREDGYPFVGMLFTGFMITADGPRVLEYNVRFGDPETQAL... | Cofactor: Binds two magnesium or manganese ions per subunit.
Function: Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway; contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities.
Catalytic Activity: 2-formamido-N(1)-(5-O-pho... |
Q9RUF5 | MKVLVIGSGGREHAIVDACARAGHEVLCTPGNPGIAAQARLLASPQDAPTLADLAVREGADVVIVGPEAYLAAGVVDECERRGVPAFGPSQAASRLEGDKAWSKAFMVRHGIPTAQHRSFDTLDAALSHAATQTPPIVVKDAGLKAGKGVTIAHSVAEAEAALREIFTQTGAQAVIEDFMTGQEVSILALTDGKRYALTPPSQDHKTIYEGDTGPMTGGMGVICPFPVGEEQLNIIRRDIVEKTLAGMRAEGIPFRGVLYAGLMLTPQGPKVVEFNARFGDPEAEAVLPLLESDLAQHALDAARGQLDPAQVRFRDGASA... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 43351
Sequence Length: 415
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-r... |
Q54GJ2 | MTIKNNILVIGSGSREHAITWKLLESNQVDKVILVPGNASSSTMERVITVECSKIDAESISNICKEHNVEYVFVGPEVPLVDGIVDGLKRKGISCFGPTKKAAQLEGSKVFCKDFMARNNIPSARYQTFTDYNKAKQYIESLNYKIVLKASGCAAGKGVLIPNNKEEELEGLKRIMVDKEFGSAGDEIVIEEFLDGEECSLMCFSDGYSLVVMPPAQDHKRIFDGDKGANTGGMGAYAPAPFIVDCNNNATTDKSKSKSSFGTIIDRCVETILKPTINGMRKEGKPFVGVLFAGLMVSSSSSTTNDKVINVLEFNCRMGD... | Cofactor: Binds no magnesium or manganese ion per subunit.
Function: Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway; contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities.
Catalytic Activity: 5-phospho-beta-D-ribosylami... |
Q8FB69 | MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPALQNVAIGVTDIPALLDFAQNEKVDLTIVGPEAPLVKGVVDTFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHNIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVRDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVTDEVHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQGNPKVIEFNCRFGDPETQPIMLRMKSDLVELCLAACEGKLD... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 45946
Sequence Length: 429
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-r... |
P15640 | MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPALQNVAIGVTDIPALLDFAQNEKIDLTIVGPEAPLVKGVVDTFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVTDDVHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQGNPKVIEFNCRFGDPETQPIMLRMKSDLVELCLAACESKLD... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the reversible conversion of phosphoribosylamine to glycinamide ribonucleotide, an enzymatic step in purine biosynthesis pathway.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycin... |
Q9KF52 | MNVLVIGSGGREHTIAWKFAQSEKVERVYVAPGNDGMSDVATCVAISEQDHDQLVAFAKENKIGLTFVGPEVPLLAGIVDRFQEEGLRVFGPSKRAAEIEGSKSYAKQVMKTYNIPTGSYEVFTSFDEAKAYVEAEGVPIVIKADGLAAGKGVVVALTNEEAIAALDDMLNQDKFGGAGARVVIEEYLEGEELSLMAFVHGETVIPMVGAQDHKRAFDGDQGPNTGGMGAYSPVPQFSDVQLKQAVNEILIPTARALMQEERSFTGILYAGLMMTADGPKVIEFNARFGDPETQVVLPRLKSDLVNVIESLLDGQEPELE... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 46304
Sequence Length: 428
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-r... |
O25817 | MKDNNNYNVLIVGNKGREYALAQRLQQDERVNALYFCLGNGGTQDLGENLECEHYEHIVELALKKQIHLAIISEEEFLVLGLTEMLEKAGILVFGASKEAAKLEASKSYMKAFVKECGIKSASYFETNDLKEALSYIQNASFPLVIKALNKNTSIVYQEEEAIKILEDAFKQSNEPVIIEPFLEGFELSVTALIANDDFILLPFCQNYKRLLEGDNGVNTGGMGAIAPANFFSNELEEKIKNHIFKPTLEKLQADNTPFKGVLLAEIVIIEEKGVLEPYLLDFSVRFKDIECQTILPLLESSLLDLCLATAKGELHSLEL... | Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 47504
Sequence Length: 424
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-d... |
P22102 | MAARVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTAISISDHTALAQFCKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAFGAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAPQVSNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGL... | Cofactor: Binds 1 magnesium or manganese ion per subunit.
Function: Trifunctional enzyme that catalyzes three distinct reactions as part of the 'de novo' inosine monophosphate biosynthetic pathway.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamid... |
Q9ZF44 | MKILVIGSGGREHALAKKFMESPQVEEVFVAPGNSGMEKDGIQIVDISELSNDKLVKFAQNQNIGLTFVGPETALMNGVVDAFIKAELPIFGPNKMAAELEGSKDFAKSIMKKYGVPTADYATFDSLEPALAYLDEKGVPLVIKADGLAAGKGVTVAFDIETAKSALADIFSGSQGKVVIEEFLDGEEFSLFSFIHDGKIYPMPIAQDHKRAFDGDKGPNTGGMGAYSPVLHISKEVVNEALEKVVKPTVAGMIEEGKSFTGVLYAGLILTEDGVKTIEFNARFGDPETQVVLPRLKSDLAQAIIDILAGNEPTLEWLES... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 44289
Sequence Length: 412
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-r... |
Q88U30 | MANVLVVGGGGREHAIAKAMMASPQVSTVYCAPGNPGMIRDGIRTLAIDEMDFAGLVNFARANTVTLTFVGPEVPLAAGIVDYFQAAGLAIFGPNQAAAQLESSKVFAKAFMSRHHIPTADYRQFHELDSALAYSHEQAVPQVIKVDGLAAGKGVTVATSHEQAAAAIKTAFKTSSTVLIEDYVAGFEFSQMVLVGGEHYALLPTAQDHKRLQDHDRGPNTGGMGAYSPVPQITPAVIDQTIATIIEPTIAGLKADGLSFEGVIYVGGILTATGVQVIEYNLRLGDPETQILLPQLQSDFYQVIVDLLQHRQPHAQWQTT... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 43463
Sequence Length: 413
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-r... |
Q6ACE6 | MKILVLGSGAREHAIITALLAERAGHDIVAAPGNAGIAADVAVEPGLDTLNGAAVTAFAIENGFELVVIGPEAPLVAGVADPLRRRGIPVFGPGRAAAQLEGSKTFAKRIMDEAGVPTGRAVRAATLAEAGSALDEFGAPYVVKADGLAAGKGVIVTEDRAAALAHAARYLTHGSVLVEEFLDGEEVSLFLVSDGHTVLPLSPAQDYKRLLDGDAGPNTGGMGAYSPLTWLPETFVDEVIDTVAMPTVRQLAAEQTPFIGLLYCGLIVTAKGIRVIEFNARFGDPETQVVLPRLVTPLSTLLFAAATGTLSGMPRPEFAP... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 43135
Sequence Length: 417
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-r... |
Q8EZT7 | MQVKLKVLLIGSGGRESAIAFYLRKSVLLSELKVFPGNGGFPDQELLPPDSFQVLDKNSVQSFLKQNPFDLIVVGPEDPLVAGFADWAAELNIPVFGPDSFCAQVEGSKDFAKSLMTEAKIPTAEYKTFSEYSDSLKYLESKSIPIVIKADGLAAGKGVTVATSKEMAQTALKEIFKDKKFGSSGNQVVIEEFMEGQEASIFAISDGDSYFLLPAAQDHKRAFDGDQGPNTGGMGAYCPAPVISESILQKVKEQIFDPMFDLFRKKGHPYRGLLYAGLMISPNGEPKVVEFNCRFGDPETQCVLAMLDGDLLELLYRAST... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 46244
Sequence Length: 426
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-r... |
Q0TTB2 | MLTYKEAGVNIEEGYRSVKLIKEYAKKTMSEYVLNGLGSFAGMVELPEGYKKPVLVSGTDGVGTKLDIACKKRKFDTVGIDCVAMCVNDILCHGAKPLFFLDYIACGKLEAEVSSDLVKGVAEGCIESQCSLIGGETAEMPGMYKEGDYDIAGFAVGIVDKDKIINGKDIKSGDKLIGIASSGVHSNGYSLIRKVFKNLDEDFNGKAIWEELLTPTKIYVKPVLSLLEKFNIKGMAHVTGGGFYENLPRMLSKEGLSIVINKNSYEIPEIFKKLMELGVKEEEMYNTFNMGIGFVLCVEEDEVEEVLKELSKQGEKAFEI... | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 36440
Sequence Length: 333
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-... |
Q0K769 | MSASPTAGQAGLSYRDAGVDIDAGDALVDRIKPFAKRTMREGVMAGIGGFGALFELSKKFQEPVLVSGTDGVGTKLKLAFQLNRHDTVGQDLVAMSVNDILVQGAEPLFFLDYFACGKLDVDTAATVIQGIARGCELAGCALIGGETAEMPSMYPDGEYDLAGFAVGAVEKKKIIDGSTITPGDVVLGLASSGAHSNGYSLVRKIIEVARPDLNADFHGQRLQDAIMAPTRIYVKPLLSLIETLPVKGMAHITGGGLTENVPRVLAQDVTAVLKRDAWTLPPLFQWLQAQGRVADDEMHRVFNCGIGMVVIVAKEDAERA... | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 37258
Sequence Length: 350
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-... |
Q5LRF9 | MTSGKNGITYAEAGVDIDAGNALVDRIKPAAKRTNRPGVASGLGGFGALFDLKAAGYQDPVLVAATDGVGTKLRIAIDTGLVDGVGIDLVAMCVNDLVCQGAEPLFFLDYFATGKLETDTAARIIEGIAEGCVQSGCALIGGETAEMPGMYPAGDFDLAGFAVGAMERGTALPEGVVEGDVLLGLASNGVHSNGYSLVRKLVEISGNTWESDCPFGDGKLGQALLTPTRLYVRQVLAAIRAGGVHALAHITGGGLTENLPRVLPEGMGATIDLDTWDLPPVFGWMAETGGIAEAEMLKTFNCGIGMIVVCAADRAEALAE... | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 35663
Sequence Length: 348
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-... |
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