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PUR3_YEAST
ID   PUR3_YEAST              Reviewed;         214 AA.
AC   P04161; D6VT40;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   03-AUG-2022, entry version 178.
DE   RecName: Full=Phosphoribosylglycinamide formyltransferase;
DE            EC=2.1.2.2;
DE   AltName: Full=5'-phosphoribosylglycinamide transformylase;
DE   AltName: Full=GAR transformylase;
DE            Short=GART;
GN   Name=ADE8 {ECO:0000312|SGD:S000002816}; OrderedLocusNames=YDR408C;
GN   ORFNames=D9509.26;
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=3889658; DOI=10.1038/315350a0;
RA   White J.H., Lusnak K., Fogel S.;
RT   "Mismatch-specific post-meiotic segregation frequency in yeast suggests a
RT   heteroduplex recombination intermediate.";
RL   Nature 315:350-352(1985).
RN   [2]
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   [3]
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   [4]
RP   INDUCTION.
RX   PubMed=8336737; DOI=10.1128/mcb.13.8.5099-5111.1993;
RA   Rolfes R.J., Hinnebusch A.G.;
RT   "Translation of the yeast transcriptional activator GCN4 is stimulated by
RT   purine limitation: implications for activation of the protein kinase
RT   GCN2.";
RL   Mol. Cell. Biol. 13:5099-5111(1993).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-
CC         ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-
CC         formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide;
CC         Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:57454, ChEBI:CHEBI:143788, ChEBI:CHEBI:147286;
CC         EC=2.1.2.2;
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-
CC       formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-
CC       ribosyl)glycinamide (10-formyl THF route): step 1/1.
CC   -!- INDUCTION: Induced by amino acid and purine starvation in a GCN4
CC       dependent manner. {ECO:0000269|PubMed:8336737}.
CC   -!- MISCELLANEOUS: Present with 3910 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the GART family. {ECO:0000305}.
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DR   EMBL; M36585; AAA34406.1; -; Genomic_DNA.
DR   EMBL; U32274; AAB64848.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12250.1; -; Genomic_DNA.
DR   PIR; A22316; A8BYD.
DR   RefSeq; NP_010696.3; NM_001180716.3.
DR   AlphaFoldDB; P04161; -.
DR   SMR; P04161; -.
DR   BioGRID; 32468; 56.
DR   DIP; DIP-1177N; -.
DR   IntAct; P04161; 5.
DR   MINT; P04161; -.
DR   STRING; 4932.YDR408C; -.
DR   MaxQB; P04161; -.
DR   PaxDb; P04161; -.
DR   PRIDE; P04161; -.
DR   EnsemblFungi; YDR408C_mRNA; YDR408C; YDR408C.
DR   GeneID; 852017; -.
DR   KEGG; sce:YDR408C; -.
DR   SGD; S000002816; ADE8.
DR   VEuPathDB; FungiDB:YDR408C; -.
DR   eggNOG; KOG3076; Eukaryota.
DR   GeneTree; ENSGT00390000000292; -.
DR   HOGENOM; CLU_038395_0_1_1; -.
DR   InParanoid; P04161; -.
DR   OMA; TGITIHY; -.
DR   BioCyc; MetaCyc:YDR408C-MON; -.
DR   BioCyc; YEAST:YDR408C-MON; -.
DR   UniPathway; UPA00074; UER00126.
DR   PRO; PR:P04161; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P04161; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IMP:SGD.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IMP:SGD.
DR   GO; GO:0046084; P:adenine biosynthetic process; IMP:SGD.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:SGD.
DR   CDD; cd08645; FMT_core_GART; 1.
DR   HAMAP; MF_01930; PurN; 1.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR004607; GART.
DR   InterPro; IPR001555; GART_AS.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
DR   TIGRFAMs; TIGR00639; PurN; 1.
DR   PROSITE; PS00373; GART; 1.
PE   1: Evidence at protein level;
KW   Purine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..214
FT                   /note="Phosphoribosylglycinamide formyltransferase"
FT                   /id="PRO_0000074954"
FT   ACT_SITE        125
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P08179"
FT   BINDING         12..14
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000250|UniProtKB:P08179"
FT   BINDING         105..108
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000250|UniProtKB:P08179"
FT   BINDING         123
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000250|UniProtKB:P08179"
FT   BINDING         167
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000250"
FT   SITE            167
FT                   /note="Raises pKa of active site His"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   214 AA;  23540 MW;  4FC8105E35A0A2A6 CRC64;
     MARIVVLISG SGSNLQALID AQKQGQLGED AHIVSVISSS KKAYGLTRAA DNNIPTKVCS
     LYPYTKGIAK EDKAARAKAR SQFENDLAKL VLEEKPDVII CAGWLLILGS TFLSQLQSVP
     ILNLHPALPG CFDGTTHAIE MAWRKCQDEN KPLTAGCMVH YVIEEVDKGE PLVVKKLEII
     PGEETLEQYE QRVHDAEHIA IVEATYKVLQ QLHK
 
 
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