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GCST_YEAST
ID   GCST_YEAST              Reviewed;         400 AA.
AC   P48015; D6VS05;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 181.
DE   RecName: Full=Aminomethyltransferase, mitochondrial;
DE            EC=2.1.2.10;
DE   AltName: Full=Glycine cleavage system T protein;
DE            Short=GCVT;
DE   AltName: Full=Glycine decarboxylase complex subunit T;
DE   Flags: Precursor;
GN   Name=GCV1; OrderedLocusNames=YDR019C; ORFNames=YD9335.05C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9047339; DOI=10.1016/s0378-1119(96)00670-1;
RA   McNeil J.B., Zhang F.R., Taylor B.V., Pearlman R.E., Bognar A.L.;
RT   "Cloning, and molecular characterization of the GCV1 gene encoding the
RT   glycine cleavage T-protein from Saccharomyces cerevisiae.";
RL   Gene 186:13-20(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8896275;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b<1085::aid-yea9>3.3.co;2-s;
RA   Eide L.G., Sander C., Prydz H.;
RT   "Sequencing and analysis of a 35.4 kb region on the right arm of chromosome
RT   IV from Saccharomyces cerevisiae reveal 23 open reading frames.";
RL   Yeast 12:1085-1090(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: The glycine cleavage system (glycine decarboxylase complex)
CC       catalyzes the degradation of glycine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-
CC         aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-
CC         5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] +
CC         NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC   -!- SUBUNIT: Component of the glycine decarboxylase complex (GDC), which is
CC       composed of four proteins: P, T, L and H.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- MISCELLANEOUS: Present with 4090 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
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DR   EMBL; L41522; AAB05000.1; -; Genomic_DNA.
DR   EMBL; X95966; CAA65211.1; -; Genomic_DNA.
DR   EMBL; Z49770; CAA89844.1; -; Genomic_DNA.
DR   EMBL; Z74315; CAA98840.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11865.1; -; Genomic_DNA.
DR   PIR; S54642; S54642.
DR   RefSeq; NP_010302.1; NM_001180327.1.
DR   AlphaFoldDB; P48015; -.
DR   SMR; P48015; -.
DR   BioGRID; 32069; 196.
DR   ComplexPortal; CPX-1268; Glycine decarboxylase multienzyme complex.
DR   IntAct; P48015; 3.
DR   STRING; 4932.YDR019C; -.
DR   iPTMnet; P48015; -.
DR   MaxQB; P48015; -.
DR   PaxDb; P48015; -.
DR   PRIDE; P48015; -.
DR   EnsemblFungi; YDR019C_mRNA; YDR019C; YDR019C.
DR   GeneID; 851582; -.
DR   KEGG; sce:YDR019C; -.
DR   SGD; S000002426; GCV1.
DR   VEuPathDB; FungiDB:YDR019C; -.
DR   eggNOG; KOG2770; Eukaryota.
DR   GeneTree; ENSGT00940000157524; -.
DR   HOGENOM; CLU_007884_10_0_1; -.
DR   InParanoid; P48015; -.
DR   OMA; MPVQYPA; -.
DR   BioCyc; YEAST:YDR019C-MON; -.
DR   Reactome; R-SCE-6783984; Glycine degradation.
DR   PRO; PR:P48015; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P48015; protein.
DR   GO; GO:0005960; C:glycine cleavage complex; IC:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006546; P:glycine catabolic process; IC:ComplexPortal.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR   GO; GO:0006544; P:glycine metabolic process; IMP:SGD.
DR   GO; GO:0006730; P:one-carbon metabolic process; IMP:SGD.
DR   Gene3D; 3.30.1360.120; -; 1.
DR   InterPro; IPR006223; GCS_T.
DR   InterPro; IPR028896; GCST/YgfZ/DmdA.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR43757; PTHR43757; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   SUPFAM; SSF101790; SSF101790; 1.
DR   TIGRFAMs; TIGR00528; gcvT; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Mitochondrion; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..400
FT                   /note="Aminomethyltransferase, mitochondrial"
FT                   /id="PRO_0000010766"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         397
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        122
FT                   /note="D -> E (in Ref. 1; AAB05000)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   400 AA;  44469 MW;  FFA349B0E0176D65 CRC64;
     MSIIKKIVFK RFNSTLKKTA LHDLHVSLGG TMVPYAGYSM PVLYKGQTHI ESHNWTRTNA
     GLFDVSHMLQ SKLSGPHSVK FLQRVTPTDF NALPVGSGTL SVLLNPQGGV VDDTIITKEN
     DDNEFYIVTN AGCAERDTEF FHDELQNGST LDCQWKIIEG RSLLALQGPK AKDVLEPLLS
     KTAPGKDLKE LFFGQRHEFA LKDGSLVQIA RGGYTGEDGF EISIANEKAV EFAEQLLANP
     VMKPIGLAAR DSLRLEAGMC LYGHELDESI TPVEAALNWV ISKSRRDLVD QKYWFNGYAK
     IMDQLNNKTY SKVRVGFKYL KKGPAARNGV KIFLPDAETE VGLVTSGSAS PTLNNINIGQ
     AYVQKGYHKK GTKLLVQVRN KFYPIELAKM PLVPTHYYKQ
 
 
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