ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q08193 | MLLRSLTSAFVLSAGLAQAASSSNSSTPSIEIKGNAFFNSESGERFYIRGVDYQPGGSSNLTDPLADASVCDRDVPVLKDLGINTVRVYTVDNSQDHSHCMKLLQENGIYLILDVNTPTSAISRYDPACSYNADYLQNVFATIDTFADYDNVLGFFAGNEVINSVNTTNTATYVKAVVRDMKKYIKARKYRQIPVGYSAADIVANRQLAAEYFNCGDEADARIDMFGVNDYSWCGESSFVVSGYSTKMKLYQDYSVPVFLSEFGCNQVKSSRPFTEIEAIYSTQMSSVFSGGLVYEYSNETNNYGLVQIDGDKVTKLTDF... | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthe... |
Q14393 | MAPSLSPGPAALRRAPQLLLLLLAAECALAALLPAREATQFLRPRQRRAFQVFEEAKQGHLERECVEELCSREEAREVFENDPETDYFYPRYLDCINKYGSPYTKNSGFATCVQNLPDQCTPNPCDRKGTQACQDLMGNFFCLCKAGWGGRLCDKDVNECSQENGGCLQICHNKPGSFHCSCHSGFELSSDGRTCQDIDECADSEACGEARCKNLPGSYSCLCDEGFAYSSQEKACRDVDECLQGRCEQVCVNSPGSYTCHCDGRGGLKLSQDMDTCEDILPCVPFSVAKSVKSLYLGRMFSGTPVIRLRFKRLQPTRLV... | Function: Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine sig... |
P46689 | MAISKALIASLLISLLVLQLVQADVENSQKKNGYAKKIDCGSACVARCRLSRRPRLCHRACGTCCYRCNCVPPGTYGNYDKCQCYASLTTHGGRRKCP | Function: Gibberellin-regulated protein that may function in hormonal controlled steps of development such as seed germination, flowering and seed maturation.
PTM: Six disulfide bonds may be present.
Sequence Mass (Da): 10745
Sequence Length: 98
Subcellular Location: Secreted
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P46688 | MAVFRSTLVLLLIIVCLTTYELHVHAADGAKVGEGVVKIDCGGRCKDRCSKSSRTKLCLRACNSCCSRCNCVPPGTSGNTHLCPCYASITTHGGRLKCP | Function: Gibberellin-regulated protein that may function in hormonal controlled steps of development such as seed germination, flowering and seed maturation.
PTM: Six disulfide bonds may be present.
Sequence Mass (Da): 10531
Sequence Length: 99
Subcellular Location: Secreted
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P46687 | MAIFRSTLVLLLILFCLTTFELHVHAAEDSQVGEGVVKIDCGGRCKGRCSKSSRPNLCLRACNSCCYRCNCVPPGTAGNHHLCPCYASITTRGGRLKCP | Function: Gibberellin-regulated protein that may function in hormonal controlled steps of development such as seed germination, flowering and seed maturation.
PTM: Six disulfide bonds may be present.
Sequence Mass (Da): 10705
Sequence Length: 99
Subcellular Location: Secreted
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Q6AQK1 | MKAYELSIEEAAAKLRAGDISSVELTQSCLQRIGDVEDRVKGFITVDEEGALAQAKAADKALQNGETNPLCGIPMSIKDLLAVKDLPMTCGSKMLEKFIAPYNATIVDKLQGAGAVNLGKVTMDEFAMGSTSETCAFGVPQNPWKEGYVAGGSSGGSAVTVAAQECFFSIGTDTGGSIRQPAALCGVVGMKPTYGRVSRYGLTAFASSLDQAGPLCRTVADTALVMNSICGYDPMDSTSINQEVPDYTASLVEGVKGLRIGIPKEYFAKGLDSEVEKVVRNAIAVLASAGAEIVDVSLPHTEYCVAVYYLIAPAEASTNL... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-... |
Q72DX1 | MSALHTLSLAAIRDALARREVRAEDAVLDCLARIETTEPRIDALLHLRAEAAIEEARALDAAGPDASRPLWGVPVTVKDALTTAGTPTTAGSRILEDFVPFYDAFAVQRLREAGAIILGKNNMDEFAMGSSTENSAYKPTRNPWDTARVPGGSSGGSAASVAAGQCFASLGTDTGGSIRQPASLCGCVGLKPTYGRVSRYGLIAYGSSLDQIGPMTRTVEDAAIVMGVIAGHDKRDSTCADRPVEDFAAALASRHDLAGVRIGVPAEFWGEGLSPEVATSCRAALDAARDLGATIVDVALPHTPQSIAAYYIVASAEASS... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-... |
Q54L63 | MNRLTNISKIRKSLIDGKLKVNDLVLNKIKEINKVSPNHLNTFISLQDEKSLGKQIKESQERYDNGTNKRLDGIPIGVKDNFSSKNFKTTCGSKILENYIPSFDSTVVKLLKEEGAIIIGKTNMDEFSMGSSSTSGHFGKVINPWSKPNNNNNNDNDNNNNGEVLYVAGGSSGGSAAAVASNYCVASIGSDTGGSIRQPSSYCGVVGFKPSYGLISRFGLVAYASSLDTPGVLTNNVEDAAELLDILIKKDQENDSTSIEFINNNQNQNQNNGEKRNILDEFNEKLKNKNIKDLVFGIPKDYLVKELDTDILNLWKEVVE... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln... |
Q9VE09 | MRRHLQWSIKQLTASYSDGQLSPRRVTEDALQDALRWKTLNAFVRLTPEQAGQQAQDAEQRYKLRQPISDLDGVTIAIKDNFCTKDVHTTCASRMLQDFVPPYDATVCSRLKQAGAVILGKTNMDQFAMGAGTVDSLYGPTKNIWSEDLNKDHWRIAGGSSGGSASAVAAGLCYAAIGSDTGGSTRNPASYCGVVGLKPTYGLVSRHGLIPLVNSMDVPGIFARSVSDCVAVLNTVAGPDKLDSTTIRQPFTRLHLPEVGQIDLSTVRIGIPKEYHCHGLSAEVLETWSKVADLLECSGASVRQVSLPNTAASIFVYTIL... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln... |
Q5AQN0 | MSLLLEAERYVANQSSNRMLNAFITPLCRHSGRWHDQAKDADIRGKQGKLRSRLDGRFIAFKDNICTRDFPTTCASKSLDTFTSPFNATVVQQLEDAGAIVAGKTNLDEFGMGSHSIYSSFGHVMNTRRGDDSKFLSAGGSSGGNAVAVATDQCYAALGTDTGGSIRLPAAYTGTVGFKPSYGLLSRWGVIAYANSLDTVGILAKRVSVARDVFDVLNKHDPRDPTSISPSSRSRISSKLNLPQLTSRLTSRPLRIGIPLEYNISELAPSVRQAWCHSLEYLRQQGHTIQPVSLPMTKLALSAYYVLAPAEASSNLAKYD... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln... |
B1GZD3 | MDEILKTRVKDLCEKIRSGQIKSIEIVKACFKRIKETDPKVKAFLKLNEERSLKQAAQSDDKIKTGAECGSLEGVPIGIKDNIMIKGESMTSASKYLENYISPYDAAVIEKLKEAGVIFVGRTNMDEFAMGGSTETSVYQKTANPWNIDYIPGGSSGGSAAAVSSGMVPFALGSDTGGSIRQPAGFCGIVGYKPSYGLISRYGACALASSFDQIGVFSKTVKDASLLTSFIAVGDYRDPVCETGEQTNYAHGIYNPDILKTVRIGIPKQLSNYKADEEITKYFGDAVNKLKLEGAATVEIDVPAYKYVPALYEVIMCAEV... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-... |
B0TWN0 | MSYIKKLRARLDSGEVTAVELTKQYLAKIKDQDKSINSVITLCEAEALKEAENADAIISAGKQSLLTGIPILHKDLFCTKGIKTTAASKMLDNFVAPYDSTVTKNCKDQGMVTLGKLNMDEFAMGSTNEHSYYGAVSNPWDLDRVPGGSSGGSAAAVAAGFAPVSTGSDTGGSVRQPASFCGLTAMKPTYGSTSRFGMVAFASSFDQAGIFGHYAEDVAIMLDAISGECQYDSTCVGVKENHFTQDLEKDISGKVIGIDESLIKDLPAQIQEAVSKTLDNFKKLGAEIKSVKVPDLKEALSTYYIITPAEAAANLARYDG... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-... |
B2ATX1 | MLSRSGLRGARLRVVSLTSQRRLLNHFITHPPEPIPPPPPPAPSSSPSPKQFTLAVKDNIATTIPGLPTTCASGILSKSYVSPIEATIITQLRARGAVITGKTNLDEFGMGSHSIYSHYGPVSQDTPPETSAGGSSGGSAVAVANGEVELALGTDTGGSVRLPAAYTGIIGYKPSYGMISRYGVIPYANSLDTVGFLSKQINPLKELIIGERGLWKEHDSNDPTSLTTAARKRCAAQRRGYRSRQGQTTELEGLKFGIPLEYNIAELDPEIRDAWAAAAKRLQDAGARIVPVSLPTTKHALAAYYVIAPAEASSNLAKYD... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln... |
A2BWS5 | MNFNSFRKEIKSGNASVKELINEFFLKIDSLDPKINAYTCLTKEIANSQSEQIDKLISNNEQLPPLAGIPIAIKDNICTKGVVTSCSSKMLQDFVSPYESTVSGKLWSSGGIFLGKTNLDEFAMGSSTETSVFGTTSNPWDTKRVPGGSSGGSAASVAAGLCAASIGSDTGGSIRQPASFCGVVGLKPTYGRVSRWGLIAFASSLDQIGPITNTVSDAAEILYSMSGKDPLDSTCLDKPVPNYLSDLDKSIKGLKIGIIEECFNHPGLDQEVKLSVLSAVDRLKSLGAEIHDVKCPRFNDGIATYYVIAPCEASANLARY... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-... |
Q2IH95 | MPISDFQVVIGLEVHAQLLTASKIFCGCSTAFGGAPNAHTCPVCLGLPGALPALNRSVVEMAVRTGLALGCEIRPKSVFARKNYFYPDLPKGYQISQYELPICEGGEVTFTLDGRDHTARLVRIHMEEDAGKNVHDVAADGSSGVDLNRAGVPLVEIVSRPDLRSAEEAVEYLKALRAILMALGVNDGNMQEGSLRCDANVSVMRKGASELGTRCEIKNMNSFRFLKQAIEFEARRQVELIEAGEPVVQETRLFDPDRGETRSMRSKEEAHDYRYFPEPDLPPVIVEAALVERLRGELPELPRAKAERYQRSLGLSAQDA... | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
O66766 | MNEKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPVCLGMPGALPIVNKRAVEYAIRASLALNCEVHEESVFARKHYFYPDLPKGYQISQYEKPLATNGWVELNLPNGEKKKVRIRRLHIEEDAGKNIHEGDKTLVDLNRAGTPLMEIVTEPDIRTPEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRPKGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGGEVVQETRTFDPQTGKTYPMRTKEEAEDYRYFPDPDLVPLKVKKEWIEEIKKNMPELPDQRFERLIKEYGLSEYEAGIL... | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
Q9FV81 | MSTTLLRTIQLNQFSLLGTSLLRRRRSNNFSVRSCGSQTTTTHEAKQSSPTRVAPKNHKSNQLDEILRDYEAVIGIETHVQLSTLTKAFCSCSNNYGSYPNTSICPVCMGLPGALPVLNSKVVEFGVRLGLALNCDLSLKSKFDRKQYFYPDLPKGYQISQFDIPIASGGYVDVDIPLEFGGGHRRFGITRVHMEEDAGKLLHSDTGDYSQVDLNRAGVPLLEIVSEPDMRSGIEAAEYACEMQRIARYLGVSNGNMQEGSLRCDVNISIRPIGQAEFGTKVEIKNLNAFSAISRAIDFEISRQALLYNQGKADQIVTET... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts and mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glut... |
O28164 | MDDVVIGLEVHVQLNRLRTKLFCSCPLNYHQSPPNTHVCPVCLGMPGAMPVINKEAVKAAVKVAMALNAEIQPFTVFDRKNYFYPDLPKGFQISQYDRPLALGGYVTIELDGQEKRIQLKRVHMEEDPGKLSYKGSITTAKYSLIDYNRSGAPLLEIVTEPVMNSPKEARLFLNKLRMILEYLEVFDGDLEGAMRVDANISIRGSGRVEIKNISSFKGVEKALSYEIMRQKNLLQRGRSVVRETRHFDEARNITVSLRSKEEEQDYRYFPEPDLVPVLTEEIVREVEGTLPEMPEEKRERLKRQYGIGDNFAKVLILDVK... | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
Q5P4D1 | MSRNDWEVVIGLEVHAQLNTASKIFSAASTAFGAEPNVQASAVDIALPGVLPVLNGGAVERAIRFGVAIGATVAPKSVFARKNYFYPDLPKGYQISQFELPVVQGGAITIRVGDGDKAYEKTVQLTRAHLEEDAGKSLHEDFHGMSGIDLNRAGTPLLEIVSEPDMRSSAEAVAYARALHALVRWIDICDGNMQEGSFRCDANVSVRRPGGPLGTRREIKNLNSFRFLQQAIDFEVQWQIGTIEDGGRIQQATVLFDPDTGETRMMRSKEDAHDYRYFPDPDLLPLVIPSEWIARVRSEMPELPGAMKARFINDYGLSAY... | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
P61343 | MNYQAVIGLEVHVQLKTDTKIFCGCSTTFGASPNSQTCPVCLGMPGVLPVLNKKVVEFAIRAGLATNCRIAPRSVFARKNYFYPDLPKGYQISQYELPICQNGHLDIEVDGQVKRIGITRIHMEEDAGKLVHADVPGLGSGSGVDLNRACTPLLEIVSEPDIRSADEAVAYLRKLHQIVVYLGICDGNMEEGSFRCDANVSVMPVGSTTFGTRTETKNVNSFRFVKQAIEHEIERQIELIEEGGKVVQETRLFDPNTGETRSMRGKEEAHDYRYFPDPDLVPLVISNDWVEDTRLSLPELPDARRSRYRSELGLSDYDAE... | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
Q7NI42 | MTSTAPPKVQYEAVIGLEVHVQLSTETKLFCRCSTRFGNTPNTNICPICTGQPGTLPVLNQQALDYAVLTASALNCQIHPQGLSKFDRKQYFYPDLPKNYQISQYDLPLAERGWLEIEVEGEPAKRIGITRLHMEEDAGKLVHAGADRLSGSTHSLVDFNRAGVALCEIVSEPDIRTAAEAAAYAGELRRIVRYLGVCDGNMQEGSLRFDLNISVRPAGEGKFGTKVEIKNLNSFNSLQRAVEYEFARQVDCLLSGERIVQETRLWDEATQRTISMRSKEEANDYRYFPEPDLVPIALNGTQIDAYRQRLGELPAQKRHR... | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
Q9HS93 | MSAQAAERDLTAIIGLEVHVQLETDTKIFCGCSTDTDDADPNTHTCPVCLGLPGALPTLNEGAVEAAVKLGKAIDADIPERTRFHRKNYFYPDLPKGFQITQYDAPICQDGELEVGTADDRRAIGIERAHLEEDPGSLQHVGGSIEDADYTLVDYNRAGTPLMEIVTRPDFRAAEEVRSFLAKLTSVLEYLGVFDAERDGSLRVDANISMVDSAELAGEGGPSDDVLEAANRTEVKNISSHRAAQKALAYETTRQRNQLERGMAVAQETRHWDEARGVTVSMRSKEEEKDYRYFREADIPPLEVSDWKDEIPIPELPDAR... | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
O06492 | MSRISIEEVKHVAHLARLAITEEEAKMFTEQLDSIISFAEELNEVNTDNVEPTTHVLKMKNVMREDEAGKGLPVEDVMKNAPDHKDGYIRVPSILD | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
Q6FZS8 | MSVDQETVKRVSHLARIAIHDDEIEPMTKELNVILGFVEQLNEVDVNGIEPLTSVMPMALRMREDSVTDGDKVADIVANAPVTEENFFLVSKVVE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
Q1DCA4 | MALTLEQVRHVATLARLSLTPEEEQRFTTQLSAVLDAVEQLQSLDVEAVEPTSHATLTSSRLREDVTRPSLPPEKSLANAPAKSDTSFAVPKIIE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
B2A5W6 | MKVSKEEVLHVAKLGQLDLDQEEVEMFQDKLSQILEWQEKLDELDLEGLEPTAHALERRNVTREDQVHNSLTNDKALENAPETEGNYFKVPRIIE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
B9LA82 | MKIDESLVKRLETLSMVEIEDKASMAKDLAEIVEFVEMLNELDTSNVDATFSTLDNSTYLREDEPIKNNVIEEILEHAPKAKDGFFIVPKIIE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
Q9JZ00 | MALTLADVDKIARLSRLHLTAEEKEKSLQELNDIFTMVEQMQTINTDGIEPMAHPHEAALRLREDEVTETDRAAEYQAGAPEVRNRLYIVPQVIEE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
Q2YC92 | MSLSLDDVKRVANLARIEISEDEARKALIQLSGIFGLIEQMQAVDVSAITPMSHAQDVMQRLRADGATEIDQRELFQSVAPQVEAGLYLVPKVIE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
Q5YRT3 | MPAISRDEVAHLARLSRLALSDAELDQFAGQLDSILSHVRTISEVAAADVPATASPDPVTNVTRPDTVVPGLTPDQALAAAPAVEEQRFMVPQILGEGE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
Q4RSW7 | MSVLRFATRRGLSWCYASRLTHQGTSVTSGEGSPGTRTSRVPARVLNLTRPLSCRAYNSKVPQSPTWEPVSEDLLPPCAQFPADLVDKLERLALVDFRTKQGLECLEKAIRFADQLHVVDTSGVEPMDSVLEDRVLYLREDEEKEGDCAEELLQLSRNTCEEYYVAPPGNIPLPTREKRAAMLKHSEF | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln... |
Q47SC4 | MSAITRDEVAHLARLARLALPEDELDQLAAQLDVIISAVAKVQEVAKGDIPPTSHALPLTNVYRPDEVKPGLTPDQALAEAPAVEDGRFRVPQILGEEG | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
Q9WY94 | MIKVTKDLVLHLENLARLELSEDQRESLMKDFQEILDYVELLNEVDVEGVEPMYTPVEDSAKLRKGDPRFFEMRDLIKKNFPEEKDGHIKVPGIHR | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
B9L146 | MRLSREIVDHVAMLARLGLTEEERELMREQLSSILEHVSRIQELDTEAIPPTAQVITLQNVWREDDVRPSLPVEAVLANAPESEDGFFRVHAVLEQS | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
Q9LCX4 | MELSPELLRKLETLAKIRLSPEEEALLLQDLKRILDFVDALPRVEEGGAEEALGRLREDEPRPSLPQAEALALAPEAEDGFFRVPPVLE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
O83982 | MAQQRITSDIFAQLLTLSHLESSECAVGLATQIEDIIQYFSVVEQFDPGPRDDPDTDNAQGRCSQGNKIDVDCCPDWVRKDVALPGLSVHDLKRLSTEFADGYFRAPRALDGSA | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
B3RYZ0 | MAVKPSANLGKAFQLPHPFNSCVYIQIPPQPTWSINEYWERNPNKQYLDESDTTYLEELTLTPIEKHQALEKLNTIISAADRLQEVDTKNVDPMYTCVDEREMYMNSGQDGETVNKEEILGNAHKIFQDYFTAPTSEKMRSSSDLNAKE | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln... |
A5CX64 | MSLSENQVSQIAHLACLSLNEAQLKDNTQNLNTITSLFEQLANIEIDGVEPMLHPLHMFQRLREDVVSEKEQLALFQSIAPKVRNGYYLVPTVIK | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
D7STK2 | MGSRALLLLKATTAETLLFTSKSTFSKALIRNSTRSFSTRSALLPPDLPRLAETARISLTPHEVEEFAPKIRQVIDWFGQLQAVDLQSIEPSIRADTEGDNLRDDSPETFENREAIIAAIPSYEEPYLKVPKVLNKD | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts and mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glut... |
Q7MSD5 | MQIDDKLLARLESLAMIEVPEEKKESIKAELGEIVNFVENLNSLEVEGLEATFTTLEGKTPMREDTPMNDEEIPALILKHAPQSAENYFIVPKIIE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
Q9CXP8 | MSSGASVSALQRLVEQLKLEAGVERIKVSQAAAELQQYCIQNACKDALLLGVPAGSNPFREPRSCALL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Interacts with beta-1 and beta-2, but no... |
Q5E9F0 | MPALHIEDLPEKEKLKMEVEQLRKEVKLQRQQVSKCSEEIKNYIEERSREDPLVKGIPEDKNPFKEKGSCIIS | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Location Topology: Lipid-anchor
Sequence... |
P61952 | MPALHIEDLPEKEKLKMEVEQLRKEVKLQRQQVSKCSEEIKNYIEERSGEDPLVKGIPEDKNPFKEKGSCVIS | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Location Topology: Lipid-anchor
Sequence... |
Q28024 | MSSKTASTNNIAQARRTVQQLRMEASIERIKVSKASADLMSYCEEHARNDPLLMGIPTSENPFKDKKTCTIL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
PTM: It is not sure whether phosphorylat... |
Q9UBI6 | MSSKTASTNNIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLIGIPTSENPFKDKKTCIIL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Location Topology: Lipid-anchor
Sequence... |
Q9DAS9 | MSSKTASTNSIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLMGIPTSENPFKDKKTCIIL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Location Topology: Lipid-anchor
Sequence... |
Q9P2W3 | MEEWDVPQMKKEVESLKYQLAFQREMASKTIPELLKWIEDGIPKDPFLNPDLMKNNPWVEKGKCTIL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Location Topology: Lipid-anchor
Sequence... |
Q9JMF3 | MEEWDVPQMKKEVESLKYQLAFKREMSSKTIPELLKWIEDGIPKDPFLNPDLMKNNPWVEKAKCTIL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Location Topology: Lipid-anchor
Sequence... |
P02698 | MPVINIEDLTEKDKLKMEVDQLKKEVTLERMLVSKCCEEFRDYVEERSGEDPLVKGIPEDKNPFKELKGGCVIS | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Location Topology: Lipid-anchor
Sequence... |
P38040 | MDVMSSSLQQQRVVVEQLRREAAIDRQTISESCAKMMKYITEHEQEDYLLTGFTSQKVNPFREKSSCTVL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Location Topology: Lipid-anchor
Sequence... |
Q61012 | MPVINIEDLTEKDKLKMEVDQLKKEVTLERMMVSKCCEEVRDYIEERSGEDPLVKGIPEDKNPFKELKGGCVIS | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Location Topology: Lipid-anchor
Sequence... |
P59768 | MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENPFREKKFFCAIL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction (By similarity).
Location Topology: Lipid... |
Q9BY60 | MKFQYKEVHPFEYRKKEGEKIRKKYPDRVPLIVEKAPKARVPDLDRRKYLVPSDLTDGQFYLLIRKRIHLRPEDALFFFVNNTIPPTSATMGQLYEDSHEEDDFLYVAYSNESVYGK | Function: Ubiquitin-like modifier involved in autophagosome formation. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (By similarity).
PTM: The precursor molecule is cleaved by ATG4B to form the cytosolic form,... |
O00591 | MNYSLHLAFVCLSLFTERMCIQGSQFNVEVGRSDKLSLPGFENLTAGYNKFLRPNFGGEPVQIALTLDIASISSISESNMDYTATIYLRQRWMDQRLVFEGNKSFTLDARLVEFLWVPDTYIVESKKSFLHEVTVGNRLIRLFSNGTVLYALRITTTVACNMDLSKYPMDTQTCKLQLESWGYDGNDVEFTWLRGNDSVRGLEHLRLAQYTIERYFTLVTRSQQETGNYTRLVLQFELRRNVLYFILETYVPSTFLVVLSWVSFWISLDSVPARTCIGVTTVLSMTTLMIGSRTSLPNTNCFIKAIDVYLGICFSFVFGA... | Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. In the uterus, the function of the receptor appears to be related to tissue contractility. The binding of this pI subunit w... |
P24046 | MLAVPNMRFGIFLLWWGWVLATESRMHWPGREVHEMSKKGRPQRQRREVHEDAHKQVSPILRRSPDITKSPLTKSEQLLRIDDHDFSMRPGFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLSFPSTNNLSMTFDGRLVKKIWVPDMFFVHSKRSFIHDTTTDNVMLRVQPDGKVLYSLRVTVTAMCNMDFSRFPLDTQTCSLEIESYAYTEDDLMLYWKKGNDSLKTDERISLSQFLIQEFHTTTKLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDRRAVPARVPLGITT... | Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-1 GABA receptor could play a role in retinal neurotransmission.
Location Topology: Multi-pass membrane protein
Sequence... |
P56476 | MPYLMRLALVLFCLMALVESRKPRRKRWTGLLETSKPSHLYKKNLDVTKMRPGKPRPLLRVEDHDFTMRPAFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWRDERLAFPSSSNKSMTFDGRLVKKIWVPDVFFVHSKRSFIHDTTTDNIMLRVFPDGHVLYSMRITVTAMCNMDFSHFPLDSQTCSLELESYAYTDEDLMLYWKNGDESLKTDEKISLSQFLIQKFHTTSRLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDHRAVPARVSLGIMTVLTMSTIITGVNASMPRVSY... | Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-2 GABA receptor could play a role in retinal neurotransmission (By similarity).
Location Topology: Multi-pass membrane ... |
P47742 | MPYFMRLALFLFCLMALVESRKPRRKRWTGHLETSKPSHLYKKNLDVTKIRTGKPRPLLRVEDHDFTMRPAFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWRDERLAFPSSSNRSMTFDGRLVKKIWVPDVFFVHSKRSFTHDTTTDNIMLRVFPDGHVLYSMRITVTAMCNMDFSHFPLDSQTCSLELESYAYTDEDLMLYWKNGDESLKTDEKISLSQFLIQKFHTTSRLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDHRAVPARVSLGIMTVLTMSTIITGVNASMPRVSY... | Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-2 GABA receptor could play a role in retinal neurotransmission.
Location Topology: Multi-pass membrane protein
Sequence... |
P50573 | MVLAFWLAFFTYTWITLMLDASAVKEPHQQCLSSPKQTRIRETRMRKDDLTKVWPLKREQLLHIEDHDFSTRPGFGGSPVPVGIDVQVESIDSISEVNMDFTMTFYLRHYWKDERLSFPSTTNKSMTFDRRLIQKIWVPDIFFVHSKRSFIHDTTVENIMLRVHPDGNVLFSLRITVSAMCFMDFSRFPLDTQNCSLELESYAYNEEDLMLYWKHGNKSLNTEEHISLSQFFIEEFSASSGLAFYSSTGWYYRLFINFVLRRHIFFFVLQTYFPAMLMVMLSWVSFWIDRRAVPARVSLGITTVLTMSTIVTGVSASMPQ... | Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54031
Sequence Length: 464
Subcellular Location: Postsyn... |
Q9UN88 | MGIRGMLRAAVILLLIRTWLAEGNYPSPIPKFHFEFSSAVPEVVLNLFNCKNCANEAVVQKILDRVLSRYDVRLRPNFGGAPVPVRISIYVTSIEQISEMNMDYTITMFFHQTWKDSRLAYYETTLNLTLDYRMHEKLWVPDCYFLNSKDAFVHDVTVENRVFQLHPDGTVRYGIRLTTTAACSLDLHKFPMDKQACNLVVESYGYTVEDIILFWDDNGNAIHMTEELHIPQFTFLGRTITSKEVYFYTGSYIRLILKFQVQREVNSYLVQVYWPTVLTTITSWISFWMNYDSSAARVTIGLTSMLILTTIDSHLRDKLP... | Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71988
Sequence Length: 632
Subcellular Location: Postsyn... |
P71016 | MSQTLFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAET... | Function: Involved in the biosynthesis of the osmoprotectant glycine betaine from choline . Catalyzes the oxidation of betaine aldehyde to betaine . Shows specificity for betaine aldehyde as substrate. Can use both NAD(+) and NADP(+), but NAD(+) is strongly preferred .
Catalytic Activity: betaine aldehyde + H2O + NAD(+... |
P71017 | MTLNMKVESMQKFHTFEIPTVIKHGIGAIKHTGEEVAALGVSKALLVTDPGIYKAGVADPVIESLKEAGIEVVLFNKVEPNPPVRLVNEGSELYKKENCNGLVAVGGGSSMDTAKAIGVEATHEGSVLDYEAADGKKPLENRIPPLTTIPTTAGTGSEVTQWAVITDEEREFKFNTGGPLIAAHLTIIDPELHVSMPPHVTAMTGIDALAHAIECYTMKFAQPITDAVALMAIEYAAHYIKRAFADGEDLEARYGMAQAAMLAGLSYGSESAGAAHAMSQTLGGIIPVAHGQCVAAMMGPVMEYNWKGYPEKFARIAKAF... | Function: Involved in the biosynthesis of the osmoprotectant glycine betaine from choline.
Catalytic Activity: choline + NAD(+) = betaine aldehyde + H(+) + NADH
Sequence Mass (Da): 43421
Sequence Length: 402
Pathway: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choli... |
A3DHH6 | MIDKERIKAAVRELLIGIGEDPDREGLLETPDRVARMCEEIFAGLHQDPKSVVKVFQEENHEEMVMVKDIPIYSICEHHLLPFIGVAHVVYIPRKGKIMGLSKLARIVDIIARKPQLQERLGSEVANVIMESINPLGVAVVVEAEHLCMTMRGIKKAGSKTVTSALRGIIKTDARTRAEVMALINGR | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 20811
Sequence Length: 187
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
|
P30793 | MEKGPVRAPAEKPRGARCSNGFPERDPPRPGPSRPAEKPPRPEAKSAQPADGWKGERPRSEEDNELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS | Function: Positively regulates nitric oxide synthesis in umbilical vein endothelial cells (HUVECs). May be involved in dopamine synthesis. May modify pain sensitivity and persistence. Isoform GCH-1 is the functional enzyme, the potential function of the enzymatically inactive isoforms remains unknown.
PTM: Phosphorylat... |
A2BL58 | MPIDKAKIEKAVRMILEAIGEDPEREGLRETPRRVADMFEELLEGYDFTEEYTWFTEATDLVVVSGIRFYSLCEHHLLPFFGVAHVAYLPRGKVIGLSKIVRIVNKYSRRLQIQERMTKQIADEISKATGSPDVMVITEAVHLCMAMRGVRNGAPTVVAAVRGEFERDQSLKEEVYRIIEPHRLSRVIALSFF | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 22099
Sequence Length: 193
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
|
Q0BXB5 | MDAVTPKKDIPRPDSVRRPSQQEAEEAVRTLIAWAGDDPAREGLIDTPKRVVNAYKEWFEGYGEDPVKYLSRTFEDVQGYDDIVMLRNIEVESHCEHHIAPFIGKAFIAYKPSTAVVGISKLARVVEIFAKRLQTQETMTAQICDAITESLAPMGTAVFIEAEHQCMSTRGVHHKHVTTITTQFTGVFKSDADLRNRFLNMCGQTV | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 23141
Sequence Length: 206
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
|
A6SZ52 | MKQPIHTDPAKPDDFSTEDWRRLLTHLGENADRQGLRETPQRVEKAWKHWTSGYDQDPAEILKVFEDGAEQYNELIVVRGIPVYSHCEHHLAPFFGTATIGYTPNGKIVGLSKLTRLVDCFAKRLQVQERLTIQIADTLMEHVQPLSVGVVIRCRHMCMESRGIRTPGEETVTSALLGEMRTNLGLRNEFLMLAREKD | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 22608
Sequence Length: 198
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
|
Q88ST4 | MIDEKNQAKIEHAVREILSAVGEDPDRPGLVETPARVARMYAEVFATKTAAPFDNYKLFKVEHPTEMVLLKDIPFYSMCEHHLLPFFGTVQVAYVPQHEQVIGLSKIPRLIDYCSQQPNVQERLTVSIATELQRILDPAGIAVSITARHMCMEMRGVSKPGVHTESSYYSGQFKTDLDLKREFLQRIAK | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 21461
Sequence Length: 189
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
|
Q38WN0 | MIEQANQQIEKDVRDILKQVGDDPERAGVLETPQRVAKMYGEVLAYQGETIFKDYKLFETEETDDDQMVMMQDIPFYSMCEHHMLPFFGQVSVAYLPANGQIIGLSKIPRLVDFVSKRLSVQENLTRDIGQILNQILKPYGVAVQVTARHMCVEMRGIKKANSQTHTTFYSGNFKTDRQLRSEFLQLLK | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 21753
Sequence Length: 189
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
|
Q6ACQ1 | MTGFDRARIEAAVAEILAAVGEDPSRPGLSATPSRVADAYAEFFAGLGRDAEAELGEPVPLEQGQAETVILREISFRSVCEHHLLPFIGVAHVAYLPGEAVIGLGRIPRVIDTLAARPQVQERLTEQIADTFEAGAGARGVLVVLSAEHGCVTARGPRQVAATTVTLAARGEFAEPAARAELIALIGCGAA | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 19874
Sequence Length: 191
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
|
Q2T7N4 | MNLMNPEFVMPDVQSTVDTRQMPIQRVGVRAVRHPLTVRTAEGETQATVGTWNLDVHLPADQKGTHMSRFVALLEESGGPLTADAFRAMLATMLEKLEAQAGRIEVSFPYFVNKTAPVSGVRSLLDYEVTLTGDVRDGLTRVFAKVLVPVTSLCPCSKKISQYGAHNQRSHVTIDAELAADVPVEDLIRIAEEEASCELWGLLKRPDEKFVTERAYENPKFVEDLVRDVARRLDADERIVAYVLEAENFESIHNHSAYALIERDKRRRA | Function: Converts GTP to 7,8-dihydroneopterin triphosphate.
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 30188
Sequence Length: 269
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: st... |
B1W019 | MSQITLPAFHMPFQSAGCHPGLAETREAAWEWAAAEGLDLSVPARRKMIRTRPELWISLIFPQATQAHLDLFCQWLFWAFLVDDEFDDGPAGRDPLMCERAIARLVDVFDGAAPNGPMERALAGLRDRTCRGRSPQWNRQFRRDTAAWLWTYYAEAVERAAGQVPSRAEFAKHRRDSVAMQPFLCLHEITAGIDLPDSARSLPAYIALRNAVTDHSGLCNDICSFEKEAALGYEHNAVRLIQRDRGSTLQEAVDEAGIQLARIAERVQRAERELIEEIEAAGIDGPTRTALERCVRDYRGLVRGDFDYHARAERYTRPDL... | Cofactor: Binds 3 Mg(2+) ions per subunit. To a lesser extent, can also use Mn(2+) instead of Mg(2+). Cannot use Fe(2+), Co(2+), Zn(2+), Ni(2+), or Cu(2+).
Function: Sesquiterpene cyclase that first catalyzes the cyclization of farnesyl diphosphate (FPP) to the bicyclic sesquiterpene (+)-beta-caryophyllene intermediate... |
P0DPQ8 | MTFAVSVGGRRVDCEPGQTLLEAFLRGGVWMPNSCNQGTCGTCKLQVLSGEVDHGGAPEDTLSAEERASGLALACQARPLADTEVRSTADAGRVTHPLRDLTATVLEVADIARDTRRVLLGLAEPLAFEAGQYVELVVPGSGARRQYSLANTADEDKVLELHVRRVPGGVATDGWLFDGLAAGDRVEATGPLGDFHLPPPDEDDGGPMVLIGGGTGLAPLVGIARTALARHPSREVLLYHGVRGAADLYDLGRFAEIAEEHPGFRFVPVLSDEPDPAYRGGFPTDAFVEDVPSGRGWSGWLCGPPAMVEAGVKAFKRRRM... | Cofactor: Binds 1 FAD per subunit.
Function: Part of a two-component P450 system that efficiently O-demethylates diverse aromatic substrates such as guaiacol and a wide variety of lignin-derived monomers. Is likely involved in lignin degradation, allowing Amycolatopsis sp. ATCC 39116 to catabolize plant biomass. GcoB t... |
D4B1R0 | MIVKSLSLLALAAATVEGCVRERDVGSVDILSVLSKRGHGHPHLPHLSKYESMLINSFDNTTVDSWAYYYTHGIHIAGTNQSMAQWTADKWTEFGIPSSLVSYDVYLNYPVSHSLSLTHPDGTTWEASLVEDVLKEDDTTSYPDRIPTFHGYSASGEATAEYVYVGRGQKVDFERLIQLGVDLKGKIAIARYGGPFRGLKVKNAQDQGMIGCIIFTDPADDGNVTVANGLKAYPNGPARNPSAVQRGSVQFLSMFPGDPTTPGYPSRPDSPRKDKSPVVPKIPSIPISQLDAQPILAALDGHGTPGKEVNRTRWVGALNA... | Cofactor: Binds 2 Zn(2+) ions per subunit. Required for NAALADase activity.
Function: Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity (By similarity). Also exhibits a dipeptidyl-peptidase IV type activity (By similarity).
Catalytic Activity: Release of an unsubstituted, C... |
Q9M1S8 | MSQPLTTRPTVTGISIIPFRQPPPLCSFLFVIVLFVATFYTLHHPDAVTPPLLFSRNAYNALRLRRLFLSSASNATISSYLRELTRHPHLAGTKPSLDTLHYVFNHFQSLGLETHVAEYEALLSYPTHISVTASFSNTTTLEFDLNDVPGDSPVVRPYHAYSPSGSAQGNVVFVNHGEERDYHALESIGVSVKGCVVLARKGENLGRGAIVKIAEAKGALGVLIYAENDGGGFGGIERGTVMRGIGDPVSPGWPGVVGGEKLSLDDELVTRRFPKIPSLPLSLRNAEIILASLGGARAPLEWRNSGRVGPGQRVGPGRMV... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: May modulate the level of one or more small signaling molecules that have a role in regulating meristem function. May play a role in balancing and restricting the meristem-promoting activity of auxin signaling . Involved in ethylene and giberellin (GA) signaling path... |
P91406 | MPYVGVGAQTVSTSLTGAPMVKAYIAIAASLIFVFCIAALGVHHSERKFNKFNKVSIDDIHKSDAGVIQDNIKTENIKKYLRIFTKDPHVAGTEANKKVAYEIANAWSEAGLEDVHTLPYEVLLSYPDFENPNSVIIKSSAGKEVFKSKGVSPVIIPDEQSGKYAGHQWLAYAGNGSASADVVYINHGTANDFKNLKLMGVDIKGKIALMRYGHGFRGDKIHKAQQAGAIGAILFSDTQDVAQDGVESENVYPKKIWMPNEGVQRGSLMHGDGDALSPYYPSKKELFKGRTIEEAKEDGVLPSIPVLPVSYTTGYEILKR... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 85501
Sequence Length: 770
Subcellular Location: Membrane
EC: 3.4.... |
P20821 | MALRAVRSVRAAVGGLRAISAPSAPCLPRPWGLRAGAVRELRTGPALLSVRKFTEKHEWVTTENGVGTVGISNFAQEALGDVVYCSLPEVGTKLNKQEEFGALESVKAASELYSPLSGEVTEINKALAENPGLVNKSCYEDGWLIKMTFSNPSELDELMSEEAYEKYIKSIEE | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The glycine cleavage system catalyzes the degradation of glycine. The H protein (GCSH) shuttles the methylamine group of glycine from the P protein (GLDC) to the T protein (GCST).
Sequence Mass (Da): 18791
Sequence Length: 173
Subcellular Location: Mitochondrion
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A2Z9B8 | MALRLWASSAANALKISCSGATRAAPAYSISRYFSTVLDGLKYSSSHEWVKNDGSVATIGITDHAQGHLGEVVFVELPEAGAKVSQGGAFGNVESVKATSDINSPISGEVVEVNDKLSETPGLINSSPYEDGWMIKVKPSSPSELDALLDPAKYTKHCEEEDAH | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity).
Sequence Mass (Da): 17367
Sequence Length: 164
Subcellular Location: Mitochondrion
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P16048 | MALRMWASSTANALKLSSSSRLHLSPTFSISRCFSNVLDGLKYAPSHEWVKHEGSVATIGITDHAQDHLGEVVFVELPEPGVSVTKGKGFGAVESVKATSDVNSPISGEVIEVNTGLTGKPGLINSSPYEDGWMIKIKPTSPDELESLLGAKEYTKFCEEEDAAH | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Sequence Mass (Da): 17688
Sequence Length: 165
Subcellular Location: Mitochondrion
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Q9I137 | MTDNLNLGAIDLGTDDEFIARHIGPRAADTQAMLQRLGYDSLDTLIGNVIPDSIKGSSVLDLPAGMGEAEALASLKAIAARNRALRSFIGQGYYNCHTPAPILRNLLENPAWYTAYTPYQPEISQGRLEALLNFQTLVSDLSGLPIANASMLDEATAAAEAMTFCKRLSKNRTSQAFFASRHCHPQTLDVLRTRAEPLGIEVVVGDESTIEDFSAYFGALLQYPTCDGEIVDYRELVSRFHAVDALVAVAADLLALTLLTPPGEFGADVAIGSAQRFGVPLGFGGPHAAYFATRDAFKRDMPGRLVGVSIDRHGKPAYRL... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity).
Catalytic Acti... |
Q88P65 | MTINLGTANEFIARHIGPRAADEQAMLTALGFDSLDAMTAAVIPDSIKGTSVLGSHDGQSEADALAALKAIAGKNQLFKSYIGQGYYNTHTPAPILRNLLENPAWYTAYTPYQPEISQGRLEALLNFQTLISDLTGLPIANASLLDEATAAAEAMTFCKRLSKNKSSHAFFASVHCHPQTLDVLRTRAEPLGIEVVVGDERELGDVSAFFGALLQYPASNGEVFDYREVVQRFHAANALVAVAADLLALTLLTPPGEFDADVAIGSAQRFGVPLGFGGPHAAYFATRDAFKRDMPGRLVGVSIDRFGKTALRLAMQTREQ... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity).
Catalytic Acti... |
C1F935 | MRYLPKSPADREAMLREIGAASIDELFAIIPEEFRLTRDLAIPRQMGESEIVDHFQAAAARNANGYASFLGAGAYRHYRPVLIDTIVQRGEFLTSYTPYQAEITQGTLQAIFEFQTMICELTGMDIANASMYDGSTGAAEAVMMAIRVTGRDKVLVSRSVHPEYREVMHTYAQHQGHDAAEVEYIREGAQAGRVDLAALEAAVTEETACVLVQSPNFFGVIEDIPAIAEIAHKKGALLIVSIAEALSLGAVRPPVEADIVSLEAQSFGVALSYGGPYCGVLAAKEKYLRQMPGRLVGETKDSQGRRGFVLTLSTREQHIR... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-l... |
Q9YA15 | MEHPWIPNSHKAILDEMLEAIGVSSVDDLYRDIPPTILLSPEEWDSLPIGEGRPLSEAEVLARINDILSRNKYFTDPPPFVGGGVWPRYVPSVVKALITRGEFLTAYTPYQAEISQGLMQALFEYQSLVAELLEMEVVNASLYDWSSAVGEAMLMARRVTRRNRVLVPETMNPLHLETATTYAYGGGIRVEKVRVDRETGFIDLEDLESRLSQGDTAALYMEYPSSYTGVIDENVEAAGEAVHKAGGLFILGVEPVSMAILKPPGRLGADIAVGDGQPLGLGLNYGGPYLGVFAVRWDGRLVRQMPGRLIGMTVDAEGRR... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-l... |
Q2IQD6 | MRYHPHTPDDVRAMLDVVGAERVDDLFRSIPQALRLDRPLDLPPAADEIALFSELRRLAARNETAHPPFVGAGCYPHHVPPVVDQLLLRGEFFTAYTPYQPEISQGTLQALFEWQTFVCLLTGMDVSNASMYDGATATAEAALMAGRITGRDKVVVSAALHPEYRKVLATYLRSTGDEIVTVPFGADGRTDLAALQQAVDGRTACVILGYPNFLGVVDALPEAAAIARKAGALTVSATAEAVSLGLLQAPGALGADVAVGTFQSFGNPMSFGGPAPGFFATREKHVRQMPGRVAGATVDKQGRRGFVLTLSTREQHIRRE... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-l... |
O67193 | MSYIPHSEEETKEILSKLGLESLEDLFSHIPKELFAKDFSFPEPKSEEELRRIFERACEDTELPLYFIGAGAYDRIIPSVIWQILSRGEFLTPYTPYQAEASQGTLQAIFEYQSLICELTGMDVANASMYDGASALAEAVLMARAIKGKGDTVVLSKALNPLYRRTVKTYLRGYEDKIVEVPYTEEGTTDLNNLEEVLKESEVHALAVQYPNFFGFVEPLKEIGELCKKYEVPFVVFVDPIALSILKPPAEFGADIVVGEGQQMGIPLSFGGPYVGFFATKKEHVRKMPGRLVGMGEDIEGKRAFTLVLQTREQHIRRER... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-l... |
P54377 | MSNQDQALIFELSREGRIGYSLPELDVPEIELGDLLSDTYIRDEDAALPEVSELDIMRHYTALSKRNHGVDSGFYPLGSCTMKYNPKINEKIARIPGFAAIHPLQDEDTVQGALELLYDLSKHLEEITGMDEVTLQPAAGAHGEWTGLMMIRAYHEARGDFKRTKVIVPDSAHGTNPASATVAGFETVTVKSNEKGLVDLEDLKRAVNEETAALMLTNPNTLGLFEEQITEMAEIVHQAGGKLYYDGANLNAVLSKARPGDMGFDVVHLNLHKTFTGPHGGGGPGSGPVGVKQDLIPYLPKPVLVKKEGRFTFDYDRPHA... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity).
Catalytic Acti... |
Q9A354 | MNNVGRPTRPEAANDAANGHETLTGARGLLQDEALIFELDGWNKTGVDLPPVTAAPSSDLNGLLRDAPIGLPGLSEPETVRHYVRLSQKNHAIDLALYPLGSCTMKHNPRLNEKMARLPGFSDIHPLQPQSTVQGALELMDRLAHWLKTLTGMPAVALTPKAGAHGELCGLLAIRAAHEAAGNGHRKTVLAPTSAHGTNPATAAFVGYTVVEIAQTEDGRVDLADLESKLGDHVAAIMVTNPNTCGLFERDVVEIARLTHAAGAYFYCDGANFNAIVGRVRPGDLGVDAMHINLHKTFSTPHGGGGPGAGPVVLSEALAP... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-l... |
Q8KAN3 | MKEQLIFDLSRSGRKGYSLSPLDIPERPADELLPSKFLRKEPAELPEMAESEVVRHFIRLSNLNYHVDKNMYPLGSCTMKYNPKINDYTCDLPGFASMHPLQPESTSQGALQLMYELAEMLKEIAGMKAVTLQPAAGAHGELTGILLIKKYHEKLGNKRHKLLVVDSAHGTNPASAALGGYECVSVKCDESGCTDMGDLRAKLDGEVAALMLTNPNTVGIFEKQIPEIEKLVHGNGSLLYMDGANMNALLGITRPGDMGFDVMHYNLHKTFSAPHGGGGPGSGPVGVSERLVEFLPVPVIEKFEKDGQTRYRLNSSKPNT... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-l... |
A4J2F9 | MTEKLIFELGSPGRQGVLFPANDVPEIPPHELLPRDLIREQEVPLPEVSEGDAVRHFVRLSRMNFGVDVGFYPLGSCTMKYNPKVAEDAAGLSGFANIHPYQPDEISQGALQLMYETQQDLAEITGMDAFTLQPAAGAQGELTGMLIIKAYLESKGETGRNKVIVPDSAHGTNPATAALCGFKVVEVKSDQRGGVDLAALKQLLGPDVAALMLTNPSTLGLFEDNITEIAALVHQAGGLLYYDGANLNAIMGYARPGDMGFDVVHLNLHKTFGTPHGGGGPGSGPVGVKAELAPFLPKPVIIQREGNYLPDYHRPQSIGR... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-l... |
A7HLP1 | MTIFEKSTSGRKGYELPEYELPSVDCGIPEHLVRKEKPLLPEVSEVDVVRHYTELASKNYSVDKGFYPLGSCTMKYNPKINEDMAMLFTQLHPMQPRETIQGAIDLMGHLKEMLCEITGTDDMTLQPAAGAHGELTGLLVARAYFEDKGELDKRRKVLVPDSAHGTNPASAAMAGFEVVELKSGKDGCVNLEELKAHLDENVAVIMLTNPNTLGLFEKDILTIAKMAHEVGALLYYDGANLNAIMGRTRPGDMGFDIVHLNLHKTFSTPHGMGGPGSGPIGVKKHLAPYLPVPVIRKAGEKYDLDYNLPKSIGMVRSFYG... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-l... |
Q7VET8 | MSDHSTFADRHIGLDSQAVATMLAVIGVDSLDDLAVKAVPAGILDTLTDTGAAPGLDSLPPAASEAEALAELRALADANTVAVSMIGQGYYDTHTPPVLLRNIIENPAWYTAYTPYQPEISQGRLEALLNFQTLVTDLTGLEIANASMLDEGTAAAEAMTLMHRAARGPVKRVVVDADVFTQTAAVLATRAKPLGIEIVTADLRAGLPDGEFFGAIAQLPGASGRITDWSALVQQAHDRGALVAVGADLLALTLIAPPGEIGADVAFGTTQRFGVPMGFGGPHAGYLAVHAKHARQLPGRLVGVSVDSDGTPAYRLALQT... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-l... |
B8ZSN5 | MSVPNSSNKQTCFTARHIGPNSEDVATMLAVIGVESLDDLAAKAVPSDILDNVTDTGVAPGLDRLPPPATESETLAELGALARANTVAVSMIGQGYYDTLTPAVLSRNILENPAWYTPYTPYQPEISQGRLEALLNFQTLVSDLTGLEIANASMLDEGTAAAEAMTLMYRAARSTASRVVVDVDVFAQTVAVFATRAKPLGIDIVVADLREGLPDGEFFGVITQLPGASGRITDWTALIAQAHSRGALVAVGADLLALTLITPPGEIGADVAFGTTQRFGVPMGFGGPHAGYLALHTKHARQLPGRLVGVSVDSDGTPAY... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-l... |
Q3AET7 | MENLKRTPLYEEHIKLGAKMVPFGGWEMPVQYTGILEEHMAVRTDVGMFDVSHMGEIEITGKQAERFVNYLITNDVSRLNSGDVIYTTMCYPDGGTVDDLLAYKYSTERYLLVVNAANKDKDLAHILQYRWDDVTVTDLSDETAEIALQGPRAQEILQKLTAFDLNQIKYFGFAEIEVAGVPCLVSRTGYTGEDGFEIYFAPNLATKIWNELLNLGVKPAGLGARDTLRFEACLPLYGHELSAEITPLEAGLGWAVKFNKEDFIGKEALLAQKNAGLKRKIVGLEMIGAGIPRQGYEIVFNQRGVGFVTSGTFAPFLKKN... | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 40036
Sequence... |
P28337 | MLRAGCRAALARRHLSSAPEGLKQTPLDALHRARGGRMVPFAGWSLPVQYGRGHLESHLHTRRHCSLFDVSHMLQTRVYGRDRVRFLESLVVGDIAELRPGQGTLTLLTNERGDIVDDLIVTNTAEDHLYVVSNAGCADKDRAVMEGRAAELRAAGGDVHLEVSGQRAAGVQGPSMAQVLQAGLPDDLTKLTFMTSTATTVFGVPGCRVTRCGYTGEDGVEISVPAGRAVELAERLLGCPEVWPAGLAARDSLRLEAGLCLYGNDIDESTTPVEAGLLWTLGKRRRTAMDFPGAAIIMEQVKEKPKRKRVGLTSVGPPLR... | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 42058
Sequence... |
B2KSJ5 | MSSQVSNFPASIMKTNDIPDVKRSLANFHPNIWKEHFLSFTFDDALKIDEGMKERTEKLKEEIRMMMIAYVENQLIKLNLVDSIQRLGVSYHFEDEVDEFLEHIYVSYNNSLLLSNKNSNGEDLHITALLFRLLRQQGYRISCDIFLKFMDDNGKFKESLVEDERGLLSLYEASHMMGHGEALLEEALEFTTTHLQTYIHRYSNINPSFASEVSNALKLPIRKSVPRIKAREYLEIYQQHPSHNETLLEFSKLDFNILQKLHQKELSEICRWWKDLDVPTKFPFARDRIVECYFWTLGAYFEPQYSVGRKMLTKVIAIAS... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Sesquiterpene synthase producing mainly delta- and gamma-cadinene with traces of several other sesquiterpenoids, including alpha-copaene. Associated with the production of sesquiterpenes responsible for the aroma of the fruit.
Catalytic Activity: (2E,6E)-farnesyl dip... |
Q8GY54 | MVLWVFGYGSLIWNPGFDFDEKLIGYIKDYKRVFDLACIDHRGTPEHPARTCTLEQSTGAICWGAAYCVRGGPEKEKLAMEYLERRECEYDSKTLVEFYTENDTSTPIVTGVIVFTSTPDKVSNKYYLGPAPLEEMARQIATASGPCGNNREYLFKLEKAMFDIEHEEEYVIELANEVRKQLDLPEEVKALLKPIVSHVSVKSQAHVSTRQRVFAS | Cofactor: Binds 2 Mn(2+) ions per subunit.
Function: Catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and plays a significant role in glutathione (GSH) homeostasis. Converts both GSH and gamma-glutamyl-L-alanine to 5-oxoproline in vitro. Plays a role in detoxification of heavy metals and metalloid... |
Q84MC1 | MVMWVFGYGSLVWNPGFHYDEKVLGFIKGYKRVFDLACIDHRGTPEHPARTCTLEKAEEAICWGTAFCVRGGPEKERLAMEYLERRECEYDLKTSVDFYKEDDPLKPAVTGVIVFTSTPDKVSNKYYLGPAPLEDMARQIATANGPCGNNRDYLFLLEKAMHDIGHEEDYVIELANEVRKVLAESSTKKVTPVKESRASRVANKSKNNVPTAHQILPHHPEAVATTI | Cofactor: Binds 2 Mn(2+) ions per subunit.
Function: Catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and plays a significant role in glutathione (GSH) homeostasis. Converts GSH to 5-oxoproline and cysteine-glycine (Cys-Gly) dipeptide in vitro. Possesses low activity towards gamma-glutamyl-L-alani... |
Q84QC1 | MAMWVFGYGSLIWKTGFPFDESLPGFIKGYRRVFHQGSTDHRGTPDFPGRTVTLEAAHEEVCCGVAYKITKEEDKRDALLHLEVREKQYDQKEYLDFFTDSNASEPAVAGVMVYIASPDKKSNNNYLGPAPLEDIAKQIVKAKGPSGPNRDYLFNLEEALAQLGFKDKHVTDLANQVRHILSESEELDIDATAATANNV | Cofactor: Binds 2 Mn(2+) ions per subunit.
Function: Catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and plays a significant role in glutathione (GSH) homeostasis. Converts GSH to 5-oxoproline and cysteine-glycine (Cys-Gly) dipeptide in vitro. Possesses low activity towards gamma-glutamyl-L-alani... |
Q59111 | MSKVMTLKDAIAKYVHSGDHIALGGFTTDRKPYAAVFEILRQGITDLTGLGGAAGGDWDMLIGNGRVKAYINCYTANSGVTNVSRRFRKWFEAGKLTMEDYSQDVIYMMWHAAALGLPFLPVTLMQGSGLTDEWGISKEVRKTLDKVPDDKFKYIDNPFKPGEKVVAVPVPQVDVAIIHAQQASPDGTVRIWGGKFQDVDIAEAAKYTIVTCEEIISDEEIRRDPTKNDIPGMCVDAVVLAPYGAHPSQCYGLYDYDNPFLKVYDKVSKTQEDFDAFCKEWVFDLKDHDEYLNKLGATRLINLKVVPGLGYHIDMTKEDK | Function: Catalyzes the transfer of the CoA moiety from acetyl-CoA to (R)-2-hydroxyglutarate and related compounds like glutaconate.
Catalytic Activity: acetyl-CoA + trans-glutaconate = (2E)-glutaconyl-CoA + acetate
Sequence Mass (Da): 35722
Sequence Length: 320
Pathway: Amino-acid degradation; L-glutamate degradation ... |
Q59112 | MADYTNYTNKEMQAVTIAKQIKNGQVVTVGTGLPLIGASVAKRVYAPDCHIIVESGLMDCSPVEVPRSVGDLRFMAHCGCIWPNVRFVGFEINEYLHKANRLIAFIGGAQIDPYGNVNSTSIGDYHHPKTRFTGSGGANGIATYSNTIIMMQHEKRRFMNKIDYVTSPGWIDGPGGRERLGLPGDVGPQLVVTDKGILKFDEKTKRMYLAAYYPTSSPEDVLENTGFDLDVSKAVELEAPDPAVIKLIREEIDPGQAFIQVPTEAK | Function: Catalyzes the transfer of the CoA moiety from acetyl-CoA to (R)-2-hydroxyglutarate and related compounds like glutaconate.
Catalytic Activity: acetyl-CoA + trans-glutaconate = (2E)-glutaconyl-CoA + acetate
Sequence Mass (Da): 29166
Sequence Length: 266
Pathway: Amino-acid degradation; L-glutamate degradation ... |
O18836 | MQKLQISVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACLWRENTTSSRLEAIKIQILSKLRLETAPNISKDAIRQLLPKAPPLLELIDQFDVQRDASSDGSLEDDDYHARTETVITMPTESDLLTQVEGKPKCCFFKFSSKIQYNKLVKAQLWIYLRPVKTPATVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPEPGEDGLTPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQK... | Function: Acts specifically as a negative regulator of skeletal muscle growth.
PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide linked C-terminal dimer, which is the biologically active molecule. The circulating form consists of a late... |
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