ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q08193 | MLLRSLTSAFVLSAGLAQAASSSNSSTPSIEIKGNAFFNSESGERFYIRGVDYQPGGSSNLTDPLADASVCDRDVPVLKDLGINTVRVYTVDNSQDHSHCMKLLQENGIYLILDVNTPTSAISRYDPACSYNADYLQNVFATIDTFADYDNVLGFFAGNEVINSVNTTNTATYVKAVVRDMKKYIKARKYRQIPVGYSAADIVANRQLAAEYFNCGDEADARIDMFGVNDYSWCGESSFVVSGYSTKMKLYQDYSVPVFLSEFGCNQVKSSRPFTEIEAIYSTQMSSVFSGGLVYEYSNETNNYGLVQIDGDKVTKLTDFENLKNEYSKVSNPEGNGGYSTSNNYSTCPDYEKGVWEANNTLPAMPSAASAYFTSGAGSPMGTGIATQQSCDAKDDDDEEDDDTSSSSSSSSSSSSSASSSSESSSSTSKASSSSPSASETSLLKSAASATSSSQSSSKSKGAAGIIEIPLIFRALAELYNLVL | 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 biosynthesis and morphogenesis.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Sequence Mass (Da): 51870
Sequence Length: 484
Subcellular Location: Secreted
EC: 2.4.1.-
|
Q14393 | MAPSLSPGPAALRRAPQLLLLLLAAECALAALLPAREATQFLRPRQRRAFQVFEEAKQGHLERECVEELCSREEAREVFENDPETDYFYPRYLDCINKYGSPYTKNSGFATCVQNLPDQCTPNPCDRKGTQACQDLMGNFFCLCKAGWGGRLCDKDVNECSQENGGCLQICHNKPGSFHCSCHSGFELSSDGRTCQDIDECADSEACGEARCKNLPGSYSCLCDEGFAYSSQEKACRDVDECLQGRCEQVCVNSPGSYTCHCDGRGGLKLSQDMDTCEDILPCVPFSVAKSVKSLYLGRMFSGTPVIRLRFKRLQPTRLVAEFDFRTFDPEGILLFAGGHQDSTWIVLALRAGRLELQLRYNGVGRVTSSGPVINHGMWQTISVEELARNLVIKVNRDAVMKIAVAGDLFQPERGLYHLNLTVGGIPFHEKDLVQPINPRLDGCMRSWNWLNGEDTTIQETVKVNTRMQCFSVTERGSFYPGSGFAFYSLDYMRTPLDVGTESTWEVEVVAHIRPAADTGVLFALWAPDLRAVPLSVALVDYHSTKKLKKQLVVLAVEHTALALMEIKVCDGQEHVVTVSLRDGEATLEVDGTRGQSEVSAAQLQERLAVLERHLRSPVLTFAGGLPDVPVTSAPVTAFYRGCMTLEVNRRLLDLDEAAYKHSDITAHSCPPVEPAAA | 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 signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses.
PTM: Proteolytically processed after secretion to yield a N-terminal 36 kDa protein and a C-terminal 50 kDa protein including the laminin G-like domains which activates AXL.
Sequence Mass (Da): 74925
Sequence Length: 678
Subcellular Location: Secreted
|
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
|
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
|
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
|
Q6AQK1 | MKAYELSIEEAAAKLRAGDISSVELTQSCLQRIGDVEDRVKGFITVDEEGALAQAKAADKALQNGETNPLCGIPMSIKDLLAVKDLPMTCGSKMLEKFIAPYNATIVDKLQGAGAVNLGKVTMDEFAMGSTSETCAFGVPQNPWKEGYVAGGSSGGSAVTVAAQECFFSIGTDTGGSIRQPAALCGVVGMKPTYGRVSRYGLTAFASSLDQAGPLCRTVADTALVMNSICGYDPMDSTSINQEVPDYTASLVEGVKGLRIGIPKEYFAKGLDSEVEKVVRNAIAVLASAGAEIVDVSLPHTEYCVAVYYLIAPAEASTNLSRYDGALYGYRDLESKTLEDMYKDTRSAGFGDEVKKRILIGTYALSSGYYDAYYKKASQVRTLIIEDFKNAYRSCDVLLSPVTPTPAWKLGAKSDDPLAIYLSDIMTVSANLAGIPGMSVPGGFTEDGLPVGIQLQGSHFQEEILLKVAYNLEKLLAIQPGKLDF | 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-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 51681
Sequence Length: 485
EC: 6.3.5.7
|
Q72DX1 | MSALHTLSLAAIRDALARREVRAEDAVLDCLARIETTEPRIDALLHLRAEAAIEEARALDAAGPDASRPLWGVPVTVKDALTTAGTPTTAGSRILEDFVPFYDAFAVQRLREAGAIILGKNNMDEFAMGSSTENSAYKPTRNPWDTARVPGGSSGGSAASVAAGQCFASLGTDTGGSIRQPASLCGCVGLKPTYGRVSRYGLIAYGSSLDQIGPMTRTVEDAAIVMGVIAGHDKRDSTCADRPVEDFAAALASRHDLAGVRIGVPAEFWGEGLSPEVATSCRAALDAARDLGATIVDVALPHTPQSIAAYYIVASAEASSNLARYDGVRYGKRAHAPEDLMDLYVRSRSEGLGDEVQRRIMLGTYVLSSGYYDAYYRKAAQVRRRILEDYRNAFATCDVICGPVSPVTAWPLGALTADPLQMYLMDVFTLSLNLAGLPGLSLPVGLGTESGMPVGIQLLGRSFDEATLLSVGNVLSRALPPLGSPAGLR | 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-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 51637
Sequence Length: 489
EC: 6.3.5.7
|
Q54L63 | MNRLTNISKIRKSLIDGKLKVNDLVLNKIKEINKVSPNHLNTFISLQDEKSLGKQIKESQERYDNGTNKRLDGIPIGVKDNFSSKNFKTTCGSKILENYIPSFDSTVVKLLKEEGAIIIGKTNMDEFSMGSSSTSGHFGKVINPWSKPNNNNNNDNDNNNNGEVLYVAGGSSGGSAAAVASNYCVASIGSDTGGSIRQPSSYCGVVGFKPSYGLISRFGLVAYASSLDTPGVLTNNVEDAAELLDILIKKDQENDSTSIEFINNNQNQNQNNGEKRNILDEFNEKLKNKNIKDLVFGIPKDYLVKELDTDILNLWKEVVEEIEKRGGKVVSVSLPHTRYALPAYYLLATSEASSNLSRFDGVRYGYRFEEEKDENKVDNDNDDDDDVDENKIGMGLKDMYTKTRTNGFGEEVKKRIILGTMALSRSSYDNFYTKAQKIRRLVSDDFKNVFQGENKVDILITPTAPSPAFKQNEKMDPIEVYVNDIMTIPSNLAGLPACSIPLKLSNSNLPISVQLISNRLTDDNLLFAAHTIMNFDCYKDFTSLTPNYLK | 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) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 61155
Sequence Length: 550
Subcellular Location: Mitochondrion
EC: 6.3.5.7
|
Q9VE09 | MRRHLQWSIKQLTASYSDGQLSPRRVTEDALQDALRWKTLNAFVRLTPEQAGQQAQDAEQRYKLRQPISDLDGVTIAIKDNFCTKDVHTTCASRMLQDFVPPYDATVCSRLKQAGAVILGKTNMDQFAMGAGTVDSLYGPTKNIWSEDLNKDHWRIAGGSSGGSASAVAAGLCYAAIGSDTGGSTRNPASYCGVVGLKPTYGLVSRHGLIPLVNSMDVPGIFARSVSDCVAVLNTVAGPDKLDSTTIRQPFTRLHLPEVGQIDLSTVRIGIPKEYHCHGLSAEVLETWSKVADLLECSGASVRQVSLPNTAASIFVYTILNQCEVASNMARYDGIEYGHRATDERSTEQLYALSRAEGFNDVVKTRILTGNFLLLKKNYDHYFEKALRVRRLIAEDFARVFDSSAKEERVDILLTPTTLTEAPLYKDFASLTNRDQCAVQDFCTQPANMAGIPAVSIPIRLSQAGLPLSLQLMSNSLNEQLLLTVARWIEAQVEFDSLEHSQQYKASL | 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) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 55819
Sequence Length: 508
Subcellular Location: Mitochondrion
EC: 6.3.5.7
|
Q5AQN0 | MSLLLEAERYVANQSSNRMLNAFITPLCRHSGRWHDQAKDADIRGKQGKLRSRLDGRFIAFKDNICTRDFPTTCASKSLDTFTSPFNATVVQQLEDAGAIVAGKTNLDEFGMGSHSIYSSFGHVMNTRRGDDSKFLSAGGSSGGNAVAVATDQCYAALGTDTGGSIRLPAAYTGTVGFKPSYGLLSRWGVIAYANSLDTVGILAKRVSVARDVFDVLNKHDPRDPTSISPSSRSRISSKLNLPQLTSRLTSRPLRIGIPLEYNISELAPSVRQAWCHSLEYLRQQGHTIQPVSLPMTKLALSAYYVLAPAEASSNLAKYDGVRYGTRSDDSTENQSETYLYAKTRGAGFGPEVKRRIMLGAFSLSAQAIDNYFIQAQRIRRLVRHDFDAAFQAEHPLAAEIRNVELRQQAKQTGIDVLISPTAPTPPPTISDITDTSTKRSNLDAYINDVFTVPASLAGLPAISVPVSGKDNAGNQEGDILAGIQVIGQYGDDELVLKVGELLERR | 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) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 55011
Sequence Length: 506
Subcellular Location: Mitochondrion
EC: 6.3.5.7
|
B1GZD3 | MDEILKTRVKDLCEKIRSGQIKSIEIVKACFKRIKETDPKVKAFLKLNEERSLKQAAQSDDKIKTGAECGSLEGVPIGIKDNIMIKGESMTSASKYLENYISPYDAAVIEKLKEAGVIFVGRTNMDEFAMGGSTETSVYQKTANPWNIDYIPGGSSGGSAAAVSSGMVPFALGSDTGGSIRQPAGFCGIVGYKPSYGLISRYGACALASSFDQIGVFSKTVKDASLLTSFIAVGDYRDPVCETGEQTNYAHGIYNPDILKTVRIGIPKQLSNYKADEEITKYFGDAVNKLKLEGAATVEIDVPAYKYVPALYEVIMCAEVSANIATFDGIRYGYRSSNGRNLNDEYAKSRAESLGYEVKKRILFGTYVLGAKNYYRCYHQAQRVRTLLINQITDAYKKCDFIFSPATLQMPVKFGEKLSEECDIFLTAANLAGLPGITVPCTFTSSGMPMGVHFMGSRFSDAKLFQIADAFERISGFDINKYPNL | 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-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 53099
Sequence Length: 485
EC: 6.3.5.7
|
B0TWN0 | MSYIKKLRARLDSGEVTAVELTKQYLAKIKDQDKSINSVITLCEAEALKEAENADAIISAGKQSLLTGIPILHKDLFCTKGIKTTAASKMLDNFVAPYDSTVTKNCKDQGMVTLGKLNMDEFAMGSTNEHSYYGAVSNPWDLDRVPGGSSGGSAAAVAAGFAPVSTGSDTGGSVRQPASFCGLTAMKPTYGSTSRFGMVAFASSFDQAGIFGHYAEDVAIMLDAISGECQYDSTCVGVKENHFTQDLEKDISGKVIGIDESLIKDLPAQIQEAVSKTLDNFKKLGAEIKSVKVPDLKEALSTYYIITPAEAAANLARYDGIRYGYRNPEARDLDELYRKSRTDGFGEEVKRRIMIGNYVLASSQYDSYYNKAQQLRKVMTDQINQIFEQVDVIFMPAAPSEAFKKGDKLDPVSAYLSDIYTIPANISGLPAIAFPIGFANDLPVGGQFMAKAFNDNVLTQMVTQYQNSYGIEEFILEQARI | 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-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 52332
Sequence Length: 481
EC: 6.3.5.7
|
B2ATX1 | MLSRSGLRGARLRVVSLTSQRRLLNHFITHPPEPIPPPPPPAPSSSPSPKQFTLAVKDNIATTIPGLPTTCASGILSKSYVSPIEATIITQLRARGAVITGKTNLDEFGMGSHSIYSHYGPVSQDTPPETSAGGSSGGSAVAVANGEVELALGTDTGGSVRLPAAYTGIIGYKPSYGMISRYGVIPYANSLDTVGFLSKQINPLKELIIGERGLWKEHDSNDPTSLTTAARKRCAAQRRGYRSRQGQTTELEGLKFGIPLEYNIAELDPEIRDAWAAAAKRLQDAGARIVPVSLPTTKHALAAYYVIAPAEASSNLAKYDGVRYGARDAEGASDASAGGVLYASTRGKGFGEEVKRRILLGSYTLSSEAMDNYFIKAQRVRRLVRRDFNRVFALENPLQERETFELSDLPEEVEMEDKWGPEEVDFLLCPTAPTLAPKLKGVMEQQPVDAYMNDVFTVPASLAGLPAISVPMKVATEGAAGLQLIGQYWDDARLLDVADAVAKEVRT | 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) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 54516
Sequence Length: 507
Subcellular Location: Mitochondrion
EC: 6.3.5.7
|
A2BWS5 | MNFNSFRKEIKSGNASVKELINEFFLKIDSLDPKINAYTCLTKEIANSQSEQIDKLISNNEQLPPLAGIPIAIKDNICTKGVVTSCSSKMLQDFVSPYESTVSGKLWSSGGIFLGKTNLDEFAMGSSTETSVFGTTSNPWDTKRVPGGSSGGSAASVAAGLCAASIGSDTGGSIRQPASFCGVVGLKPTYGRVSRWGLIAFASSLDQIGPITNTVSDAAEILYSMSGKDPLDSTCLDKPVPNYLSDLDKSIKGLKIGIIEECFNHPGLDQEVKLSVLSAVDRLKSLGAEIHDVKCPRFNDGIATYYVIAPCEASANLARYDGVKYGYRSDGDTNLVEMISKSRAEGFGNEVQRRILIGTYALSAGYSDAYYKKAQRVRTLIRKDFDSAFDKVDVLLTPTCPTTAFLKGDFINDPLSMYLSDLLTVPANLAGLPAISIPCGFDKKGLPIGLQLIGNVLEEHRILNVANIFEKDADVMKRKPSIEI | 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-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 52120
Sequence Length: 484
EC: 6.3.5.7
|
Q2IH95 | MPISDFQVVIGLEVHAQLLTASKIFCGCSTAFGGAPNAHTCPVCLGLPGALPALNRSVVEMAVRTGLALGCEIRPKSVFARKNYFYPDLPKGYQISQYELPICEGGEVTFTLDGRDHTARLVRIHMEEDAGKNVHDVAADGSSGVDLNRAGVPLVEIVSRPDLRSAEEAVEYLKALRAILMALGVNDGNMQEGSLRCDANVSVMRKGASELGTRCEIKNMNSFRFLKQAIEFEARRQVELIEAGEPVVQETRLFDPDRGETRSMRSKEEAHDYRYFPEPDLPPVIVEAALVERLRGELPELPRAKAERYQRSLGLSAQDAGNLVADAAVSAWFDAAVAAYGAGPEAAKKVANWVIGELARLANETGEAPAAWKLTPARLAAVLRLIDAGTIGGPGAKQVVEEVFRTGAEPDAVVKAKGLAQVSDEGAIEAAVDKVLAANPGEVEKYRGGRKNLVGFFVGQVMKEMRGKGNPAVVNALLRRKLGD | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 52068
Sequence Length: 484
EC: 6.3.5.-
|
O66766 | MNEKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPVCLGMPGALPIVNKRAVEYAIRASLALNCEVHEESVFARKHYFYPDLPKGYQISQYEKPLATNGWVELNLPNGEKKKVRIRRLHIEEDAGKNIHEGDKTLVDLNRAGTPLMEIVTEPDIRTPEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRPKGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGGEVVQETRTFDPQTGKTYPMRTKEEAEDYRYFPDPDLVPLKVKKEWIEEIKKNMPELPDQRFERLIKEYGLSEYEAGILVNHKEVGDFFEEAVRHFKEPKGIVNWLINDLLGLLRDKGISIEESPVKPEHLAELVKLIKEKVISTKIGKEVIKEMVETGKTPSQIVEEKGLKQITDENQIKELVKKIFEKHPKEVERLKQGEEKLIGFFVGQVMRETRGKANPQVVNKVIRELVKEV | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 55041
Sequence Length: 478
EC: 6.3.5.-
|
Q9FV81 | MSTTLLRTIQLNQFSLLGTSLLRRRRSNNFSVRSCGSQTTTTHEAKQSSPTRVAPKNHKSNQLDEILRDYEAVIGIETHVQLSTLTKAFCSCSNNYGSYPNTSICPVCMGLPGALPVLNSKVVEFGVRLGLALNCDLSLKSKFDRKQYFYPDLPKGYQISQFDIPIASGGYVDVDIPLEFGGGHRRFGITRVHMEEDAGKLLHSDTGDYSQVDLNRAGVPLLEIVSEPDMRSGIEAAEYACEMQRIARYLGVSNGNMQEGSLRCDVNISIRPIGQAEFGTKVEIKNLNAFSAISRAIDFEISRQALLYNQGKADQIVTETRLWEEGAQKTVTMRKKEGLADYRYFPEPDLPEVILTQEYVDSIRASLPELPEAKRRRYEAMGLGMQDVLFLANDVSVAEYFDAVIGKGAEVKLAANWIMSDIAAYLKNEKLSINDIKLTPQELAELIAAIKDGTISGKIGKEILFELLAKGGTVKGMIKAKDLVQITDPAEIEKMVIQVVSENPKQLEQYRSGKTKLQGYFAGQVMKMSKGKANPGLLNKILLEKLNAKD | 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-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 60941
Sequence Length: 550
Subcellular Location: Mitochondrion
EC: 6.3.5.-
|
O28164 | MDDVVIGLEVHVQLNRLRTKLFCSCPLNYHQSPPNTHVCPVCLGMPGAMPVINKEAVKAAVKVAMALNAEIQPFTVFDRKNYFYPDLPKGFQISQYDRPLALGGYVTIELDGQEKRIQLKRVHMEEDPGKLSYKGSITTAKYSLIDYNRSGAPLLEIVTEPVMNSPKEARLFLNKLRMILEYLEVFDGDLEGAMRVDANISIRGSGRVEIKNISSFKGVEKALSYEIMRQKNLLQRGRSVVRETRHFDEARNITVSLRSKEEEQDYRYFPEPDLVPVLTEEIVREVEGTLPEMPEEKRERLKRQYGIGDNFAKVLILDVKMADYFEEVAKLVDPKLAASWIVDVLRGELNYRDWSFAKCWEVFKPEEFAKLLKYFEEDRITEKGVVEVIRTKLDEGGEIDAIIQKKGLFAIPKEEIIKFCKEAIEENPKAVEDYLSGKRQALNFLVGQVMKKTRGRADPADTAKLIEEMLS | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 53922
Sequence Length: 471
EC: 6.3.5.-
|
Q5P4D1 | MSRNDWEVVIGLEVHAQLNTASKIFSAASTAFGAEPNVQASAVDIALPGVLPVLNGGAVERAIRFGVAIGATVAPKSVFARKNYFYPDLPKGYQISQFELPVVQGGAITIRVGDGDKAYEKTVQLTRAHLEEDAGKSLHEDFHGMSGIDLNRAGTPLLEIVSEPDMRSSAEAVAYARALHALVRWIDICDGNMQEGSFRCDANVSVRRPGGPLGTRREIKNLNSFRFLQQAIDFEVQWQIGTIEDGGRIQQATVLFDPDTGETRMMRSKEDAHDYRYFPDPDLLPLVIPSEWIARVRSEMPELPGAMKARFINDYGLSAYDAASLTAAKEIAAYYQAMLATADTKPGSQVPKLGANWVMGELAAQLNRAERDIGDSPVTPAQLAGLVQRIADGTISNNIARKVFAALWNGEGGSGADAADRIIEAQGLRQVNDSSALEPLIDEVLAANRKSVDEFRAGKEKAFNALVGQVMKASRGKANPAQVNEMLKRKLDA | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 53422
Sequence Length: 493
EC: 6.3.5.-
|
P61343 | MNYQAVIGLEVHVQLKTDTKIFCGCSTTFGASPNSQTCPVCLGMPGVLPVLNKKVVEFAIRAGLATNCRIAPRSVFARKNYFYPDLPKGYQISQYELPICQNGHLDIEVDGQVKRIGITRIHMEEDAGKLVHADVPGLGSGSGVDLNRACTPLLEIVSEPDIRSADEAVAYLRKLHQIVVYLGICDGNMEEGSFRCDANVSVMPVGSTTFGTRTETKNVNSFRFVKQAIEHEIERQIELIEEGGKVVQETRLFDPNTGETRSMRGKEEAHDYRYFPDPDLVPLVISNDWVEDTRLSLPELPDARRSRYRSELGLSDYDAEVLTATREMAEYFENCLAAGAPAKGAANWVMGEVTRALNEAGKDIAECPVAPARLTALLQLIEKGTISGKIAKTVFDEMWQSDKAPEAIVEEKGLVQVSDTGAIEKIIDEIMAANMGQVEEFRGGKEKVFGFFVGQVMRASKGKANPAVVNELLMKKLKG | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 52668
Sequence Length: 479
EC: 6.3.5.-
|
Q7NI42 | MTSTAPPKVQYEAVIGLEVHVQLSTETKLFCRCSTRFGNTPNTNICPICTGQPGTLPVLNQQALDYAVLTASALNCQIHPQGLSKFDRKQYFYPDLPKNYQISQYDLPLAERGWLEIEVEGEPAKRIGITRLHMEEDAGKLVHAGADRLSGSTHSLVDFNRAGVALCEIVSEPDIRTAAEAAAYAGELRRIVRYLGVCDGNMQEGSLRFDLNISVRPAGEGKFGTKVEIKNLNSFNSLQRAVEYEFARQVDCLLSGERIVQETRLWDEATQRTISMRSKEEANDYRYFPEPDLVPIALNGTQIDAYRQRLGELPAQKRHRYRETLGLSSYDAGVLTDEREVAEYFEQVVALGIPAKQAANFVSGAVAAHLNETRRSISQIKVTPEVSAELLALINQGIISNRIANELLPDLFEKGGSPRALVEERGLTQISDRGQLEQIVDEVLAGESDSVAAYRGGRTKLLGFFVGKVMKKTAGRADPQVVNDLLQSKLAEQPTAPPPEPESAAETPEAPPAVEDAPPEAPTEAITAEAGSAEAITAASEEPDTPVSHQDAHA | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 60533
Sequence Length: 554
EC: 6.3.5.-
|
Q9HS93 | MSAQAAERDLTAIIGLEVHVQLETDTKIFCGCSTDTDDADPNTHTCPVCLGLPGALPTLNEGAVEAAVKLGKAIDADIPERTRFHRKNYFYPDLPKGFQITQYDAPICQDGELEVGTADDRRAIGIERAHLEEDPGSLQHVGGSIEDADYTLVDYNRAGTPLMEIVTRPDFRAAEEVRSFLAKLTSVLEYLGVFDAERDGSLRVDANISMVDSAELAGEGGPSDDVLEAANRTEVKNISSHRAAQKALAYETTRQRNQLERGMAVAQETRHWDEARGVTVSMRSKEEEKDYRYFREADIPPLEVSDWKDEIPIPELPDARRERFRTEYGVGDETASKLTSRKAVADLFEELADEYDAALAATWVADNVLGELNYRDLSLDDVADRDDEFERLVELVAEDEITAKNAEEVVLRTMLDEDRAPDEIVDAEGLGKTSGDAVADAVAEAIAENPDAVADYHDGEGDALNFLVGQVMAKTGGSADPGQVNELLRDELAQA | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 54267
Sequence Length: 495
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10859
Sequence Length: 96
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10580
Sequence Length: 95
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10380
Sequence Length: 95
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 11056
Sequence Length: 95
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10602
Sequence Length: 93
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10958
Sequence Length: 96
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10479
Sequence Length: 95
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10397
Sequence Length: 99
EC: 6.3.5.-
|
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) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 21152
Sequence Length: 188
Subcellular Location: Mitochondrion
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10600
Sequence Length: 99
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 11309
Sequence Length: 96
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 11059
Sequence Length: 97
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 9957
Sequence Length: 89
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 12559
Sequence Length: 114
EC: 6.3.5.-
|
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) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 17121
Sequence Length: 149
Subcellular Location: Mitochondrion
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10777
Sequence Length: 95
EC: 6.3.5.-
|
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-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 15328
Sequence Length: 137
Subcellular Location: Mitochondrion
EC: 6.3.5.-
|
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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Mass (Da): 10840
Sequence Length: 96
EC: 6.3.5.-
|
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 not with beta-3 (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 7229
Sequence Length: 68
Subcellular Location: Cell membrane
|
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 Mass (Da): 8594
Sequence Length: 73
Subcellular Location: Cell membrane
|
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 Mass (Da): 8481
Sequence Length: 73
Subcellular Location: Cell membrane
|
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 phosphorylation by PKC is on Ser-2 or Ser-3.
Location Topology: Lipid-anchor
Sequence Mass (Da): 8057
Sequence Length: 72
Subcellular Location: Cell membrane
|
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 Mass (Da): 8006
Sequence Length: 72
Subcellular Location: Cell membrane
|
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 Mass (Da): 7997
Sequence Length: 72
Subcellular Location: Cell membrane
|
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 Mass (Da): 7949
Sequence Length: 67
Subcellular Location: Cell membrane
|
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 Mass (Da): 7979
Sequence Length: 67
Subcellular Location: Cell membrane
|
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 Mass (Da): 8544
Sequence Length: 74
Subcellular Location: Cell membrane
|
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 Mass (Da): 8130
Sequence Length: 70
Subcellular Location: Cell membrane
|
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 Mass (Da): 8528
Sequence Length: 74
Subcellular Location: Cell membrane
|
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-anchor
Sequence Mass (Da): 7850
Sequence Length: 71
Subcellular Location: Cell membrane
|
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, GABARAPL3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, GABARAPL3-II. ATG4B also mediates the delipidation required for GABARAPL1 recycling when autophagosomes fuse with lysosomes (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 13976
Sequence Length: 117
Subcellular Location: Cytoplasm
|
O00591 | MNYSLHLAFVCLSLFTERMCIQGSQFNVEVGRSDKLSLPGFENLTAGYNKFLRPNFGGEPVQIALTLDIASISSISESNMDYTATIYLRQRWMDQRLVFEGNKSFTLDARLVEFLWVPDTYIVESKKSFLHEVTVGNRLIRLFSNGTVLYALRITTTVACNMDLSKYPMDTQTCKLQLESWGYDGNDVEFTWLRGNDSVRGLEHLRLAQYTIERYFTLVTRSQQETGNYTRLVLQFELRRNVLYFILETYVPSTFLVVLSWVSFWISLDSVPARTCIGVTTVLSMTTLMIGSRTSLPNTNCFIKAIDVYLGICFSFVFGALLEYAVAHYSSLQQMAAKDRGTTKEVEEVSITNIINSSISSFKRKISFASIEISSDNVDYSDLTMKTSDKFKFVFREKMGRIVDYFTIQNPSNVDHYSKLLFPLIFMLANVFYWAYYMYF | 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 with other GABA(A) receptor subunits alters the sensitivity of recombinant receptors to modulatory agents such as pregnanolone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50640
Sequence Length: 440
Subcellular Location: Postsynaptic cell membrane
|
P24046 | MLAVPNMRFGIFLLWWGWVLATESRMHWPGREVHEMSKKGRPQRQRREVHEDAHKQVSPILRRSPDITKSPLTKSEQLLRIDDHDFSMRPGFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLSFPSTNNLSMTFDGRLVKKIWVPDMFFVHSKRSFIHDTTTDNVMLRVQPDGKVLYSLRVTVTAMCNMDFSRFPLDTQTCSLEIESYAYTEDDLMLYWKKGNDSLKTDERISLSQFLIQEFHTTTKLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDRRAVPARVPLGITTVLTMSTIITGVNASMPRVSYIKAVDIYLWVSFVFVFLSVLEYAAVNYLTTVQERKEQKLREKLPCTSGLPPPRTAMLDGNYSDGEVNDLDNYMPENGEKPDRMMVQLTLASERSSPQRKSQRSSYVSMRIDTHAIDKYSRIIFPAAYILFNLIYWSIFS | 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 Mass (Da): 55883
Sequence Length: 479
Subcellular Location: Postsynaptic cell membrane
|
P56476 | MPYLMRLALVLFCLMALVESRKPRRKRWTGLLETSKPSHLYKKNLDVTKMRPGKPRPLLRVEDHDFTMRPAFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWRDERLAFPSSSNKSMTFDGRLVKKIWVPDVFFVHSKRSFIHDTTTDNIMLRVFPDGHVLYSMRITVTAMCNMDFSHFPLDSQTCSLELESYAYTDEDLMLYWKNGDESLKTDEKISLSQFLIQKFHTTSRLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDHRAVPARVSLGIMTVLTMSTIITGVNASMPRVSYIRAVDIYLWVSFVFVFLSVLEYAAVNYLTTLQEQKERKFREKLPCMCGMLHSRTMMLDGSYSESEANSLAGYPRSHILPEEERPDNIVVHLALNSELTSSRKKGLLKGQMGLYIFQNTHAIDKYSRLIFPAFYIVFNLIYWSVFS | 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 protein
Sequence Mass (Da): 54231
Sequence Length: 465
Subcellular Location: Postsynaptic cell membrane
|
P47742 | MPYFMRLALFLFCLMALVESRKPRRKRWTGHLETSKPSHLYKKNLDVTKIRTGKPRPLLRVEDHDFTMRPAFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWRDERLAFPSSSNRSMTFDGRLVKKIWVPDVFFVHSKRSFTHDTTTDNIMLRVFPDGHVLYSMRITVTAMCNMDFSHFPLDSQTCSLELESYAYTDEDLMLYWKNGDESLKTDEKISLSQFLIQKFHTTSRLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDHRAVPARVSLGIMTVLTMSTIITGVNASMPRVSYIRAVDIYLWVSFVFVFLSVLEYAAVNYLTTVQEQKERKLRDKFPCTCGMLHSRTMTLDGSYSESEANSLAGYPRSHILPEEERQDKIVVHLALNSELTSSRKKGLLKGQMGLYIFQNTHAIDKYSRLIFPAFYIVFNLIYWSVFS | 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 Mass (Da): 54296
Sequence Length: 465
Subcellular Location: Postsynaptic cell membrane
|
P50573 | MVLAFWLAFFTYTWITLMLDASAVKEPHQQCLSSPKQTRIRETRMRKDDLTKVWPLKREQLLHIEDHDFSTRPGFGGSPVPVGIDVQVESIDSISEVNMDFTMTFYLRHYWKDERLSFPSTTNKSMTFDRRLIQKIWVPDIFFVHSKRSFIHDTTVENIMLRVHPDGNVLFSLRITVSAMCFMDFSRFPLDTQNCSLELESYAYNEEDLMLYWKHGNKSLNTEEHISLSQFFIEEFSASSGLAFYSSTGWYYRLFINFVLRRHIFFFVLQTYFPAMLMVMLSWVSFWIDRRAVPARVSLGITTVLTMSTIVTGVSASMPQVSYVKAVDVYMWVSSLFVFLSVIEYAAVNYLTTVEEWKQLNRRGKISGMYNIDAVQAMAFDGCYHDGETDVDQTSFFLHSEEDSMRTKFTGSPCADSSQIKRKSLGGNVGRIILENNHVIDTYSRIVFPVVYIIFNLFYWGIYV | 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: Postsynaptic cell membrane
|
Q9UN88 | MGIRGMLRAAVILLLIRTWLAEGNYPSPIPKFHFEFSSAVPEVVLNLFNCKNCANEAVVQKILDRVLSRYDVRLRPNFGGAPVPVRISIYVTSIEQISEMNMDYTITMFFHQTWKDSRLAYYETTLNLTLDYRMHEKLWVPDCYFLNSKDAFVHDVTVENRVFQLHPDGTVRYGIRLTTTAACSLDLHKFPMDKQACNLVVESYGYTVEDIILFWDDNGNAIHMTEELHIPQFTFLGRTITSKEVYFYTGSYIRLILKFQVQREVNSYLVQVYWPTVLTTITSWISFWMNYDSSAARVTIGLTSMLILTTIDSHLRDKLPNISCIKAIDIYILVCLFFVFLSLLEYVYINYLFYSRGPRRQPRRHRRPRRVIARYRYQQVVVGNVQDGLINVEDGVSSLPITPAQAPLASPESLGSLTSTSEQAQLATSESLSPLTSLSGQAPLATGESLSDLPSTSEQARHSYGVRFNGFQADDSIIPTEIRNRVEAHGHGVTHDHEDSNESLSSDERHGHGPSGKPMLHHGEKGVQEAGWDLDDNNDKSDCLAIKEQFKCDTNSTWGLNDDELMAHGQEKDSSSESEDSCPPSPGCSFTEGFSFDLFNPDYVPKVDKWSRFLFPLAFGLFNIVYWVYHMY | 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: Postsynaptic cell membrane
|
P71016 | MSQTLFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIGIEEGAKLETGGKRPEDPELQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYRNTKPAAVNWFNS | 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(+) = glycine betaine + 2 H(+) + NADH
Sequence Mass (Da): 53666
Sequence Length: 490
Pathway: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1.
EC: 1.2.1.8
|
P71017 | MTLNMKVESMQKFHTFEIPTVIKHGIGAIKHTGEEVAALGVSKALLVTDPGIYKAGVADPVIESLKEAGIEVVLFNKVEPNPPVRLVNEGSELYKKENCNGLVAVGGGSSMDTAKAIGVEATHEGSVLDYEAADGKKPLENRIPPLTTIPTTAGTGSEVTQWAVITDEEREFKFNTGGPLIAAHLTIIDPELHVSMPPHVTAMTGIDALAHAIECYTMKFAQPITDAVALMAIEYAAHYIKRAFADGEDLEARYGMAQAAMLAGLSYGSESAGAAHAMSQTLGGIIPVAHGQCVAAMMGPVMEYNWKGYPEKFARIAKAFGIDTSKMTTEEAAKASVNWMYDLVEDLEVPTLEEQGVSPDMIERLSKEAMKDPQTFGNPRDLNEKAYNWIYKRCFNLTPKTV | 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 choline (dehydrogenase route): step 1/1.
EC: 1.1.1.-
|
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: Phosphorylated by casein kinase II at Ser-81 in HAECs during oscillatory shear stress; phosphorylation at Ser-81 results in increased enzyme activity.
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 27903
Sequence Length: 250
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.4.16
|
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: step 1/1.
EC: 3.5.4.16
|
B1W019 | MSQITLPAFHMPFQSAGCHPGLAETREAAWEWAAAEGLDLSVPARRKMIRTRPELWISLIFPQATQAHLDLFCQWLFWAFLVDDEFDDGPAGRDPLMCERAIARLVDVFDGAAPNGPMERALAGLRDRTCRGRSPQWNRQFRRDTAAWLWTYYAEAVERAAGQVPSRAEFAKHRRDSVAMQPFLCLHEITAGIDLPDSARSLPAYIALRNAVTDHSGLCNDICSFEKEAALGYEHNAVRLIQRDRGSTLQEAVDEAGIQLARIAERVQRAERELIEEIEAAGIDGPTRTALERCVRDYRGLVRGDFDYHARAERYTRPDLVELDERDSLSRHFAA | 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, and then its conversion to (+)-caryolan-1-ol via a second cyclization and the addition of a water molecule.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (+)-(E)-beta-caryophyllene + diphosphate
Sequence Mass (Da): 37906
Sequence Length: 335
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 4.2.1.138
|
P0DPQ8 | MTFAVSVGGRRVDCEPGQTLLEAFLRGGVWMPNSCNQGTCGTCKLQVLSGEVDHGGAPEDTLSAEERASGLALACQARPLADTEVRSTADAGRVTHPLRDLTATVLEVADIARDTRRVLLGLAEPLAFEAGQYVELVVPGSGARRQYSLANTADEDKVLELHVRRVPGGVATDGWLFDGLAAGDRVEATGPLGDFHLPPPDEDDGGPMVLIGGGTGLAPLVGIARTALARHPSREVLLYHGVRGAADLYDLGRFAEIAEEHPGFRFVPVLSDEPDPAYRGGFPTDAFVEDVPSGRGWSGWLCGPPAMVEAGVKAFKRRRMSPRRIHREKFTPAS | 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 transfers electrons from NADH to the cytochrome P450 subunit GcoA. Highly prefers NADH over NADPH as the electron donor.
Catalytic Activity: NADH + 2 oxidized [cytochrome P450] = H(+) + NAD(+) + 2 reduced [cytochrome P450]
Sequence Mass (Da): 35566
Sequence Length: 334
Domain: GcoB has an unusual three-domain structure, with an N-terminal 2Fe-2S domain and a C-terminal region that consists of an FAD-binding domain followed by an NADH-binding domain.
Pathway: Aromatic compound metabolism.
EC: 1.6.2.-
|
D4B1R0 | MIVKSLSLLALAAATVEGCVRERDVGSVDILSVLSKRGHGHPHLPHLSKYESMLINSFDNTTVDSWAYYYTHGIHIAGTNQSMAQWTADKWTEFGIPSSLVSYDVYLNYPVSHSLSLTHPDGTTWEASLVEDVLKEDDTTSYPDRIPTFHGYSASGEATAEYVYVGRGQKVDFERLIQLGVDLKGKIAIARYGGPFRGLKVKNAQDQGMIGCIIFTDPADDGNVTVANGLKAYPNGPARNPSAVQRGSVQFLSMFPGDPTTPGYPSRPDSPRKDKSPVVPKIPSIPISQLDAQPILAALDGHGTPGKEVNRTRWVGALNATYATGPAPGAKLSMSNVMRDTYTPIWNSIGIINGTEQDEVVIIGNHRDAWIIGGAGDPNSGSSIMVELAKAFGKLQKAGWKPKRTIVMCSWDAEEYGLVGSTEWVEEYLPWLKASAVAYLNIDVAVSGPVPDLSATPELHKLALESMKKVIWPYKGRQDTTMYDVWNTASGGEVGVLGSGSDYTAFVHNGIASLDTGAGGDGNTDPVYHYHSNYDSYHWMATYGDPGFHTHVAMGQFLGLLGYHLATDDIIPFDVTNYGVQMTKYLDVLKKYIAASKFPDLDVSKIESAICSFNVSANAVAKLQKKAEHNVHDQQLRKHLNTIYRDFGRGFVSQGGLPDREFYRHMLYAPGLDTGYAPTTFPGVTESLDAGNRTRAVEYIERASNAIYVAAGILSSCHDCNQFVAQE | 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-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.
Sequence Mass (Da): 79197
Sequence Length: 727
Subcellular Location: Secreted
EC: 3.4.17.21
|
Q9M1S8 | MSQPLTTRPTVTGISIIPFRQPPPLCSFLFVIVLFVATFYTLHHPDAVTPPLLFSRNAYNALRLRRLFLSSASNATISSYLRELTRHPHLAGTKPSLDTLHYVFNHFQSLGLETHVAEYEALLSYPTHISVTASFSNTTTLEFDLNDVPGDSPVVRPYHAYSPSGSAQGNVVFVNHGEERDYHALESIGVSVKGCVVLARKGENLGRGAIVKIAEAKGALGVLIYAENDGGGFGGIERGTVMRGIGDPVSPGWPGVVGGEKLSLDDELVTRRFPKIPSLPLSLRNAEIILASLGGARAPLEWRNSGRVGPGQRVGPGRMVINMTFQGEMKMKKINNVVVTIRGSEEADRYVILGNHRDAWTYGAVDPNSGTSALLDISRRFALLLKSGWRPRRTILLCSWDAEEFGMIGSTEWIEENVLNLGASAVAYLNVDCAVQGSGFFAGATPQLDGLLVDVLKLVQDPDAVGLTVEETFKSQNNIIQRLSRVDSDFSGFLHHAGIPSIDMYYGADYPVYHTAFDSYDWMIHNADPLFHRHVAMAGIWGLLGILLADEPLIPFDYISYADQLQAHRDKLSKLLEGKVSVNPLSMAIQEFSLVAKEAADEAKKLKGKSYSKNDVAAAAKRRELNDRLMLVERGFLDAEGIKGKEWFKHLVYGPAAEPESKLGFFPGIADAIAMNASEGIIEHEIWRVARAIQRASKALKGGFT | 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 pathways or in a parallel pathway controlling cell and hypocotyl elongation and cellular organization . Involved in abscisic acid (ABA) signaling pathway. Plays a negative role in ABA-mediated seed germination and seedling development . Acts in association with LAMP1 to suppress ectopic stem cell niche formation in the shoot apical meristem (SAM) independently of cytokinin signaling pathway . Modulates responses to ABA, oxidative stress and abotic stress . Acts as negative regulator of the ABA signaling pathway to modulate freezing and drought stress responses. Mediates carbon and amino acid metabolism . May be involved in the acquisition and/or maintenance of seed dormancy . Involved in the regulation of response to heat shock and plant defense .
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): 77153
Sequence Length: 705
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.4.17.21
|
P91406 | MPYVGVGAQTVSTSLTGAPMVKAYIAIAASLIFVFCIAALGVHHSERKFNKFNKVSIDDIHKSDAGVIQDNIKTENIKKYLRIFTKDPHVAGTEANKKVAYEIANAWSEAGLEDVHTLPYEVLLSYPDFENPNSVIIKSSAGKEVFKSKGVSPVIIPDEQSGKYAGHQWLAYAGNGSASADVVYINHGTANDFKNLKLMGVDIKGKIALMRYGHGFRGDKIHKAQQAGAIGAILFSDTQDVAQDGVESENVYPKKIWMPNEGVQRGSLMHGDGDALSPYYPSKKELFKGRTIEEAKEDGVLPSIPVLPVSYTTGYEILKRLSGRPAPSDWQGFVGGNLTYKLGPGFVNGEKLSINVHSELRTKRIRNVIGYIRGSEEPDSYIMLGNHFDAWVYGSIDPNSGTAVLAEVARAMMQTINETSWKPARTIVFNAWDAEEFGLIGSTEFVEEFVNILQKRAVVYINMDCIQGNISLHVDTVPILEHAVIEASKQVENPSKRERSRGRKTLYDTWMKVFPDKKAGVPKIRVPGGGSDHAPFLNFAGVPVINFTFKNYTTWDTYPLYHTMYETPFSNIHLLDTDNLSVHKAIGQYWAELAKTFADDVILPMNTTHFASVMLKTYLPQLKTTISGINVSRSDFEDIRTQYALLSKSAQDLLTMSKKFQETIHFTQHSFSQNPYDPKHVNAVNERLKSTERCFINPRGVSMHNPSARHVLFSVSDSDSYSSSLMAGVQNAINSYDLNPTKKGLREIINQISIVQYSVICVVNTLRDVI | 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: 3.4.17.21
|
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
|
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
|
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
|
Q9I137 | MTDNLNLGAIDLGTDDEFIARHIGPRAADTQAMLQRLGYDSLDTLIGNVIPDSIKGSSVLDLPAGMGEAEALASLKAIAARNRALRSFIGQGYYNCHTPAPILRNLLENPAWYTAYTPYQPEISQGRLEALLNFQTLVSDLSGLPIANASMLDEATAAAEAMTFCKRLSKNRTSQAFFASRHCHPQTLDVLRTRAEPLGIEVVVGDESTIEDFSAYFGALLQYPTCDGEIVDYRELVSRFHAVDALVAVAADLLALTLLTPPGEFGADVAIGSAQRFGVPLGFGGPHAAYFATRDAFKRDMPGRLVGVSIDRHGKPAYRLAMQTREQHIRREKATSNICTAQVLLANIASMFAVYHGPQGLLRIARRTHRLTAILAAGLERLGVAVEQKHFFDTLSLATGARTAAIHAKARAAGINLREIDAGRLGLSLDETVRQTDVETLWGLLAEEGQALPDFAALAASSGDRLPVELLRQSAILSHPIFNRHHSETELMRYLRKLADKDLALDRTMIPLGSCTMKLNAASEMIPVTWAEFGNLHPFAPAEQSEGYRQLTDELEAMLCSATGYDAVSLQPNAGSQGEYAGLLAIRAYHQSRGDSQRDICLIPSSAHGTNPATASMVGMRVVVVACDARGNVDVEDLRNKASEHKERLAALMITYPSTHGVFEEAIREICAIVHDCGGQVYIDGANMNAMVGLCAPGKFGGDVSHLNLHKTFCIPHGGGGPGVGPIGVRAHLAPFLPGHARGERKEGAVSAAPYGSASILPITWMYIRMMGGEGLKRASEMAILNANYIAHRLEEHYPVLYAGGNGLVAHECILDLRPLKDSSGISVDDVAKRLMDFGFHAPTMSFPVAGTLMIEPTESESKAELDRFCDAMIRIREEIRAVERGELDKEDNPLKNAPHTAAELLGEWNHAYSREQAAYPLASLVEAKYWPPVGRVDNVYGDRNLTCSCPPIEAYSEE | 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 Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 103919
Sequence Length: 959
EC: 1.4.4.2
|
Q88P65 | MTINLGTANEFIARHIGPRAADEQAMLTALGFDSLDAMTAAVIPDSIKGTSVLGSHDGQSEADALAALKAIAGKNQLFKSYIGQGYYNTHTPAPILRNLLENPAWYTAYTPYQPEISQGRLEALLNFQTLISDLTGLPIANASLLDEATAAAEAMTFCKRLSKNKSSHAFFASVHCHPQTLDVLRTRAEPLGIEVVVGDERELGDVSAFFGALLQYPASNGEVFDYREVVQRFHAANALVAVAADLLALTLLTPPGEFDADVAIGSAQRFGVPLGFGGPHAAYFATRDAFKRDMPGRLVGVSIDRFGKTALRLAMQTREQHIRREKATSNICTAQVLLANIASMFAVYHGPAGLKRIAERTHALTAILAAGLKALGVQVVGASAFDTLTLATGTATASLHDKARAQGINLRQIDAAHVGLSLDETSTQADVESLWQLLGGEQAQPDFTALAASTGSLLPAALLRQSAILEHPVFNRYHSETELMRYLRRLADKDLALDRSMIPLGSCTMKLNAASEMIPVTWAEFGNLHPFAPAEQSQGYLQMTTELEAMLCAATGYDAVSLQPNAGSQGEYAGLLAIRAYHRSRGEGHRDICLIPSSAHGTNPATAHMAGMRVVVTACDARGNVDVEDLRAKAIEHRERLAAIMITYPSTHGVFEEAIGEICAIIHDNGGQVYIDGANMNAMVGLCAPGKFGGDVSHLNLHKTFCIPHGGGGPGVGPIGVKSHLAPFLPGHAQLENTQGAVCAAPFGSASILPITWMYIRMMGGAGLKRASQMAILNANYIARRLEEHYPVLYTGGNGLVAHECILDLRPLKDTSGISVDDVAKRLIDFGFHAPTMSFPVAGTLMIEPTESESKEELDRFCNAMIQIREEIRAVEDGSLDKDDNPLKNAPHTAAELVGEWTHGYSREQAVYPLASLVEGKYWPPVGRVDNVFGDRNLVCACPSIESYQDA | 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 Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 101992
Sequence Length: 951
EC: 1.4.4.2
|
C1F935 | MRYLPKSPADREAMLREIGAASIDELFAIIPEEFRLTRDLAIPRQMGESEIVDHFQAAAARNANGYASFLGAGAYRHYRPVLIDTIVQRGEFLTSYTPYQAEITQGTLQAIFEFQTMICELTGMDIANASMYDGSTGAAEAVMMAIRVTGRDKVLVSRSVHPEYREVMHTYAQHQGHDAAEVEYIREGAQAGRVDLAALEAAVTEETACVLVQSPNFFGVIEDIPAIAEIAHKKGALLIVSIAEALSLGAVRPPVEADIVSLEAQSFGVALSYGGPYCGVLAAKEKYLRQMPGRLVGETKDSQGRRGFVLTLSTREQHIRREKATSNICTNQALVALMATVYMTIYGKQGIKDLALQNLAKADYAAKTLGQSGKLLFAGSPRFHEFVLETSETPAQVNERLLEEKIIGGLPLGKWYPELGHAALWCATEVTTREQIDRAAQVLAHAPALAAR | 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)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 49316
Sequence Length: 452
EC: 1.4.4.2
|
Q9YA15 | MEHPWIPNSHKAILDEMLEAIGVSSVDDLYRDIPPTILLSPEEWDSLPIGEGRPLSEAEVLARINDILSRNKYFTDPPPFVGGGVWPRYVPSVVKALITRGEFLTAYTPYQAEISQGLMQALFEYQSLVAELLEMEVVNASLYDWSSAVGEAMLMARRVTRRNRVLVPETMNPLHLETATTYAYGGGIRVEKVRVDRETGFIDLEDLESRLSQGDTAALYMEYPSSYTGVIDENVEAAGEAVHKAGGLFILGVEPVSMAILKPPGRLGADIAVGDGQPLGLGLNYGGPYLGVFAVRWDGRLVRQMPGRLIGMTVDAEGRRAFAMILQTREQHIRRAKATSNITTNEALMAIAAAVYLSLLGPQGLREVAEASWYMSHYAAKRLSELRGVEAPLLEGEFIMDFTVRLPMDAGVARRRLLEKGVLAGIPLGGFSFFSDNDMLLTVTEAHTRRHVDLLVNLLDSVLGG | 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)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 51103
Sequence Length: 465
EC: 1.4.4.2
|
Q2IQD6 | MRYHPHTPDDVRAMLDVVGAERVDDLFRSIPQALRLDRPLDLPPAADEIALFSELRRLAARNETAHPPFVGAGCYPHHVPPVVDQLLLRGEFFTAYTPYQPEISQGTLQALFEWQTFVCLLTGMDVSNASMYDGATATAEAALMAGRITGRDKVVVSAALHPEYRKVLATYLRSTGDEIVTVPFGADGRTDLAALQQAVDGRTACVILGYPNFLGVVDALPEAAAIARKAGALTVSATAEAVSLGLLQAPGALGADVAVGTFQSFGNPMSFGGPAPGFFATREKHVRQMPGRVAGATVDKQGRRGFVLTLSTREQHIRREKATSNICTNSGLCALASTVHLSLLGKRGLAELARLNHGRARMLRDAMERAGCRPVFSGPFFNEQVFDVGDAEAVVAKLAKRGIVAGAPLARWFPDAPSAKGALLCAATELHGPELIQLFAGAVRS | 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)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 47431
Sequence Length: 445
EC: 1.4.4.2
|
O67193 | MSYIPHSEEETKEILSKLGLESLEDLFSHIPKELFAKDFSFPEPKSEEELRRIFERACEDTELPLYFIGAGAYDRIIPSVIWQILSRGEFLTPYTPYQAEASQGTLQAIFEYQSLICELTGMDVANASMYDGASALAEAVLMARAIKGKGDTVVLSKALNPLYRRTVKTYLRGYEDKIVEVPYTEEGTTDLNNLEEVLKESEVHALAVQYPNFFGFVEPLKEIGELCKKYEVPFVVFVDPIALSILKPPAEFGADIVVGEGQQMGIPLSFGGPYVGFFATKKEHVRKMPGRLVGMGEDIEGKRAFTLVLQTREQHIRRERATSNICTNQNLMALANLLYMVLLGKEGMKKVAVQSLSKALYFKKELMKKGFEEVFTGKHLWEFPLRHESLKAIYRKLLKEKIVLGLPLDRFYEDLKNTTLIAVTEKRTKEEIDSVLALL | 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)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 49722
Sequence Length: 439
EC: 1.4.4.2
|
P54377 | MSNQDQALIFELSREGRIGYSLPELDVPEIELGDLLSDTYIRDEDAALPEVSELDIMRHYTALSKRNHGVDSGFYPLGSCTMKYNPKINEKIARIPGFAAIHPLQDEDTVQGALELLYDLSKHLEEITGMDEVTLQPAAGAHGEWTGLMMIRAYHEARGDFKRTKVIVPDSAHGTNPASATVAGFETVTVKSNEKGLVDLEDLKRAVNEETAALMLTNPNTLGLFEEQITEMAEIVHQAGGKLYYDGANLNAVLSKARPGDMGFDVVHLNLHKTFTGPHGGGGPGSGPVGVKQDLIPYLPKPVLVKKEGRFTFDYDRPHAIGRVKPYYGNFGINVRAYTYIRSMGPDGLKAVTENAVLNANYMMRKLAPYYDLPFDRHCKHEFVLSGKRQKKLGVRTLDIAKRLLDFGYHPPTIYFPLNVEECIMIEPTETESKETLDAFIDAMIQIAKEAEENPELVQEAPHTTIVKRMDETKAARHPVLRYEAEER | 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 Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 54427
Sequence Length: 488
EC: 1.4.4.2
|
Q9A354 | MNNVGRPTRPEAANDAANGHETLTGARGLLQDEALIFELDGWNKTGVDLPPVTAAPSSDLNGLLRDAPIGLPGLSEPETVRHYVRLSQKNHAIDLALYPLGSCTMKHNPRLNEKMARLPGFSDIHPLQPQSTVQGALELMDRLAHWLKTLTGMPAVALTPKAGAHGELCGLLAIRAAHEAAGNGHRKTVLAPTSAHGTNPATAAFVGYTVVEIAQTEDGRVDLADLESKLGDHVAAIMVTNPNTCGLFERDVVEIARLTHAAGAYFYCDGANFNAIVGRVRPGDLGVDAMHINLHKTFSTPHGGGGPGAGPVVLSEALAPFAPTPWLTHGDNGFELAEHAGDDDAKTAFGRMSAFHGQMGMYVRAYAYMLSHGADGLRQVAEDAVLNANYIKAQLKDVMSPAFPEGPCMHEALFDDSWLEGTGVTTLDFAKAMIDEGFHPMTMYFPLVVHGAMLIEPTETESKHELDRFIAALRALAGAAKAGDTERFKGAPFHAPLRRLDETQAARKPRLRWKPVAAAPLAAE | 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)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 55993
Sequence Length: 524
EC: 1.4.4.2
|
Q8KAN3 | MKEQLIFDLSRSGRKGYSLSPLDIPERPADELLPSKFLRKEPAELPEMAESEVVRHFIRLSNLNYHVDKNMYPLGSCTMKYNPKINDYTCDLPGFASMHPLQPESTSQGALQLMYELAEMLKEIAGMKAVTLQPAAGAHGELTGILLIKKYHEKLGNKRHKLLVVDSAHGTNPASAALGGYECVSVKCDESGCTDMGDLRAKLDGEVAALMLTNPNTVGIFEKQIPEIEKLVHGNGSLLYMDGANMNALLGITRPGDMGFDVMHYNLHKTFSAPHGGGGPGSGPVGVSERLVEFLPVPVIEKFEKDGQTRYRLNSSKPNTIGRMMNFYGNFSVLVRAYTYIRMLGADGLRRVSENAIINANYLLQRLVEHYALPYPRPVMHEFCLSGDRQKKEHGVRTLDIAKRLLDYGYHAPTVYFPLIVSEALMIEPTETEAKETLNAFADAMIAIAEEAKSNPDLIKSAPTTTPVKRLDEAQASRQLNICCQH | 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)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 53810
Sequence Length: 486
EC: 1.4.4.2
|
A4J2F9 | MTEKLIFELGSPGRQGVLFPANDVPEIPPHELLPRDLIREQEVPLPEVSEGDAVRHFVRLSRMNFGVDVGFYPLGSCTMKYNPKVAEDAAGLSGFANIHPYQPDEISQGALQLMYETQQDLAEITGMDAFTLQPAAGAQGELTGMLIIKAYLESKGETGRNKVIVPDSAHGTNPATAALCGFKVVEVKSDQRGGVDLAALKQLLGPDVAALMLTNPSTLGLFEDNITEIAALVHQAGGLLYYDGANLNAIMGYARPGDMGFDVVHLNLHKTFGTPHGGGGPGSGPVGVKAELAPFLPKPVIIQREGNYLPDYHRPQSIGRVKAFFANFSVIVKAYTYLRSLGGKGLKEVSEHAVLNANYLMKQLSDHFRVPYQRTCMHEFVVSPPEDMKEQGIKTLDIAKRLLDYGYHPPTVYFPLIVEEALMFEPTETESKETLDEFAHNLIKVLAEARENPDKLRNAPYTTPIRRLDEVMAARKPLVGWFPE | 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)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 53106
Sequence Length: 484
EC: 1.4.4.2
|
A7HLP1 | MTIFEKSTSGRKGYELPEYELPSVDCGIPEHLVRKEKPLLPEVSEVDVVRHYTELASKNYSVDKGFYPLGSCTMKYNPKINEDMAMLFTQLHPMQPRETIQGAIDLMGHLKEMLCEITGTDDMTLQPAAGAHGELTGLLVARAYFEDKGELDKRRKVLVPDSAHGTNPASAAMAGFEVVELKSGKDGCVNLEELKAHLDENVAVIMLTNPNTLGLFEKDILTIAKMAHEVGALLYYDGANLNAIMGRTRPGDMGFDIVHLNLHKTFSTPHGMGGPGSGPIGVKKHLAPYLPVPVIRKAGEKYDLDYNLPKSIGMVRSFYGNFTVMVKAYTYILTMGNKGLKHVSDMAVLNANYLRAKLSKIYKVAYDRICMHEFVIDNEEFVKKTGVKTLDIAKRLLDYGLHAPTVYFPLIVHEAMMIEPTETESKRTLDEFIDAMEKIYNEAIENPELVKKAPYKTPIRRLDDVNATKYPVFRYKK | 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)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 53430
Sequence Length: 477
EC: 1.4.4.2
|
Q7VET8 | MSDHSTFADRHIGLDSQAVATMLAVIGVDSLDDLAVKAVPAGILDTLTDTGAAPGLDSLPPAASEAEALAELRALADANTVAVSMIGQGYYDTHTPPVLLRNIIENPAWYTAYTPYQPEISQGRLEALLNFQTLVTDLTGLEIANASMLDEGTAAAEAMTLMHRAARGPVKRVVVDADVFTQTAAVLATRAKPLGIEIVTADLRAGLPDGEFFGAIAQLPGASGRITDWSALVQQAHDRGALVAVGADLLALTLIAPPGEIGADVAFGTTQRFGVPMGFGGPHAGYLAVHAKHARQLPGRLVGVSVDSDGTPAYRLALQTREQHIRRDKATSNICTAQVLLAVLAAMYASYHGAGGLTAIARRVHAHAEAIAGALGDALVHDKYFDTVLARVPGRADEVLARAKANGINLWRVDADHVSVACDEATTDTHVAVVLDAFGVAAAAPAHADIATRTSEFLTHPAFTQYRTETSMMRYLRALADKDIALDRSMIPLGSCTMKLNAAAEMESITWPEFGRQHPFAPASDTAGLRQLVADLQSWLVLITGYDAVSLQPNAGSQGEYAGLLAIHEYHASRGEPHRDICLIPSSAHGTNAASAALAGMRVVVVDCHDNGDVDLDDLRAKVGEHAERLSALMITYPSTHGVYEHDIAEICAAVHDAGGQVYVDGANLNALVGLARPGKFGGDVSHLNLHKTFCIPHGGGGPGVGPVAVRAHLAPFLPGHPFAPELPKGYPVSSAPYGSASILPITWAYIRMMGAEGLRAASLTAITSANYIARRLDEYYPVLYTGENGMVAHECILDLRGITKLTGITVDDVAKRLADYGFHAPTMSFPVAGTLMVEPTESESLAEVDAFCEAMIGIRAEIDKVGAGEWPVDDNPLRGAPHTAQCLLASDWDHPYTREQAAYPLGTAFRPKVWPAVRRIDGAYGDRNLVCSCPPVEAFA | 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)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 99453
Sequence Length: 941
EC: 1.4.4.2
|
B8ZSN5 | MSVPNSSNKQTCFTARHIGPNSEDVATMLAVIGVESLDDLAAKAVPSDILDNVTDTGVAPGLDRLPPPATESETLAELGALARANTVAVSMIGQGYYDTLTPAVLSRNILENPAWYTPYTPYQPEISQGRLEALLNFQTLVSDLTGLEIANASMLDEGTAAAEAMTLMYRAARSTASRVVVDVDVFAQTVAVFATRAKPLGIDIVVADLREGLPDGEFFGVITQLPGASGRITDWTALIAQAHSRGALVAVGADLLALTLITPPGEIGADVAFGTTQRFGVPMGFGGPHAGYLALHTKHARQLPGRLVGVSVDSDGTPAYRLALQTREQHIRRDKATSNICTAQVLLAVMAAMYASYHGAEGLTGIARRVHAQARALAAGLSAAGVEVVHQAFFDTVLARVPGRTVQIQGAAKERGINVWLVDGDHVSVACDEATTDEHITAVLAAFAATPARASFAGPDIATRTSAFLTHPTFTKYRTETSMMRYLRALADKDIALDRSMIPLGSCTMKLNAAAEMESITWQEFTRQHPFAPVSDTPGLRRLISDLESWLVQITGYDAVSLQPNAGSQGEYAGLLAIHDYHVSRGEPHRNVCLIPSSAHGTNAASAALVGMRVVVVGCHDNGDVDLDDLRIKLSEHANRLSVLMITYPSTHGVYEHDIAEICAAVHDAGGQVYVDGANLNALVGLARPGKFGGDVSHLNLHKTFCIPHGGGGPGVGPVAVRSHLVSFLPGHPFAPELPQGQPVSSAPYGSASLLPITWAYIRMMGADGLRTASLTAIASANYIARRLDKYFPVLYTGENGMVAHECILDLRPITKSVGVTVDDVAKRLADYGFHAPTMSFPVPGTLMVEPTESESLAEIDAFCEAMIAIRGEIARVGAGEWSVEDNPLRGAPHTAECLLASDWDHPYTREEAAYPLGKAFRPKVWPPVRRIDGVYGDRNLVCSCLPVEAFV | 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)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 101283
Sequence Length: 952
EC: 1.4.4.2
|
Q3AET7 | MENLKRTPLYEEHIKLGAKMVPFGGWEMPVQYTGILEEHMAVRTDVGMFDVSHMGEIEITGKQAERFVNYLITNDVSRLNSGDVIYTTMCYPDGGTVDDLLAYKYSTERYLLVVNAANKDKDLAHILQYRWDDVTVTDLSDETAEIALQGPRAQEILQKLTAFDLNQIKYFGFAEIEVAGVPCLVSRTGYTGEDGFEIYFAPNLATKIWNELLNLGVKPAGLGARDTLRFEACLPLYGHELSAEITPLEAGLGWAVKFNKEDFIGKEALLAQKNAGLKRKIVGLEMIGAGIPRQGYEIVFNQRGVGFVTSGTFAPFLKKNLAMAMVDLEAAEIGTEVDVIIRGKGVRARVISRPFYKRGK | 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 Length: 360
EC: 2.1.2.10
|
P28337 | MLRAGCRAALARRHLSSAPEGLKQTPLDALHRARGGRMVPFAGWSLPVQYGRGHLESHLHTRRHCSLFDVSHMLQTRVYGRDRVRFLESLVVGDIAELRPGQGTLTLLTNERGDIVDDLIVTNTAEDHLYVVSNAGCADKDRAVMEGRAAELRAAGGDVHLEVSGQRAAGVQGPSMAQVLQAGLPDDLTKLTFMTSTATTVFGVPGCRVTRCGYTGEDGVEISVPAGRAVELAERLLGCPEVWPAGLAARDSLRLEAGLCLYGNDIDESTTPVEAGLLWTLGKRRRTAMDFPGAAIIMEQVKEKPKRKRVGLTSVGPPLRPPAAILGPEGTPVGTVTSGCPSPSLGKNIAMGYVQAAHSRPGTTLTVEVRKKQHPALVTKMPFVPTHYYMAK | 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 Length: 392
Subcellular Location: Mitochondrion
EC: 2.1.2.10
|
B2KSJ5 | MSSQVSNFPASIMKTNDIPDVKRSLANFHPNIWKEHFLSFTFDDALKIDEGMKERTEKLKEEIRMMMIAYVENQLIKLNLVDSIQRLGVSYHFEDEVDEFLEHIYVSYNNSLLLSNKNSNGEDLHITALLFRLLRQQGYRISCDIFLKFMDDNGKFKESLVEDERGLLSLYEASHMMGHGEALLEEALEFTTTHLQTYIHRYSNINPSFASEVSNALKLPIRKSVPRIKAREYLEIYQQHPSHNETLLEFSKLDFNILQKLHQKELSEICRWWKDLDVPTKFPFARDRIVECYFWTLGAYFEPQYSVGRKMLTKVIAIASILDDIYDAYGTFEELQVLTPAIQRWDRSMVHTLPLYMKPFYVAMLELYEEIGKEIDKDQNSLHLQVAIGGIKRLSESYFEEAKWLNKEYKPSFKEYMELALKTTGYTMLISISFLGLGDHIVTNEVLQWLSNGPQIIKASTIICRLMDDIASHKFEQEREHVASAVECYMKQYDCSEEEACIELHKEVVDAWKDTNEAFYRPFNVPVPVLMRVLNFSRVINLLYLDEDGYTNAKSGTKFLIKSLLVDPLPC | 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 diphosphate = (+)-gamma-cadinene + diphosphate
Sequence Mass (Da): 66633
Sequence Length: 571
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.2.3.13
|
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 metalloids by recycling glutamate and maintaining GSH homeostasis.
Catalytic Activity: an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline + an L-alpha-amino acid
Sequence Mass (Da): 24573
Sequence Length: 216
Subcellular Location: Cytoplasm
EC: 4.3.2.9
|
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-alanine. Has no activity towards gamma-glutamyl-L-cysteine.
Catalytic Activity: an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline + an L-alpha-amino acid
Sequence Mass (Da): 25607
Sequence Length: 227
Subcellular Location: Cytoplasm
EC: 4.3.2.9
|
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-alanine. Has no activity towards gamma-glutamyl-L-cysteine.
Catalytic Activity: an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline + an L-alpha-amino acid
Sequence Mass (Da): 22229
Sequence Length: 199
Subcellular Location: Cytoplasm
EC: 4.3.2.9
|
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 via hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step 3/5.
Subcellular Location: Cytoplasm
EC: 2.8.3.12
|
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 via hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step 3/5.
Subcellular Location: Cytoplasm
EC: 2.8.3.12
|
O18836 | MQKLQISVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACLWRENTTSSRLEAIKIQILSKLRLETAPNISKDAIRQLLPKAPPLLELIDQFDVQRDASSDGSLEDDDYHARTETVITMPTESDLLTQVEGKPKCCFFKFSSKIQYNKLVKAQLWIYLRPVKTPATVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPEPGEDGLTPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGEGQIIYGKIPAMVVDRCGCS | 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 latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in a latent, inactive state. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase.
Sequence Mass (Da): 42551
Sequence Length: 375
Subcellular Location: Secreted
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.