HIS1_YEAST
ID HIS1_YEAST Reviewed; 297 AA.
AC P00498; D3DLV8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=ATP phosphoribosyltransferase;
DE Short=ATP-PRT;
DE Short=ATP-PRTase;
DE EC=2.4.2.17;
GN Name=HIS1; OrderedLocusNames=YER055C;
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=6300123; DOI=10.1016/s0021-9258(18)32564-x;
RA Hinnebusch A.G., Fink G.R.;
RT "Repeated DNA sequences upstream from HIS1 also occur at several other co-
RT regulated genes in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 258:5238-5247(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-
CC diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial
CC role in the pathway because the rate of histidine biosynthesis seems to
CC be controlled primarily by regulation of the enzymatic activity (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-
CC alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017,
CC ChEBI:CHEBI:73183; EC=2.4.2.17;
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; V01306; CAA24613.1; -; Genomic_DNA.
DR EMBL; U18813; AAB64591.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07712.1; -; Genomic_DNA.
DR PIR; A00583; XRBY.
DR RefSeq; NP_010975.3; NM_001178946.3.
DR AlphaFoldDB; P00498; -.
DR SMR; P00498; -.
DR BioGRID; 36795; 28.
DR IntAct; P00498; 5.
DR MINT; P00498; -.
DR STRING; 4932.YER055C; -.
DR iPTMnet; P00498; -.
DR MaxQB; P00498; -.
DR PaxDb; P00498; -.
DR PRIDE; P00498; -.
DR EnsemblFungi; YER055C_mRNA; YER055C; YER055C.
DR GeneID; 856782; -.
DR KEGG; sce:YER055C; -.
DR SGD; S000000857; HIS1.
DR VEuPathDB; FungiDB:YER055C; -.
DR eggNOG; KOG2831; Eukaryota.
DR HOGENOM; CLU_038115_1_2_1; -.
DR InParanoid; P00498; -.
DR OMA; YVMMDYD; -.
DR BioCyc; YEAST:YER055C-MON; -.
DR UniPathway; UPA00031; UER00006.
DR PRO; PR:P00498; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P00498; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IMP:SGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IMP:SGD.
DR Gene3D; 3.30.70.120; -; 1.
DR HAMAP; MF_00079; HisG_Long; 1.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR020621; ATP_PRibTrfase_HisG_long.
DR InterPro; IPR013115; HisG_C.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR PANTHER; PTHR21403; PTHR21403; 1.
DR Pfam; PF01634; HisG; 1.
DR Pfam; PF08029; HisG_C; 1.
DR SUPFAM; SSF54913; SSF54913; 1.
DR TIGRFAMs; TIGR00070; hisG; 1.
DR TIGRFAMs; TIGR03455; HisG_C-term; 1.
DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW Glycosyltransferase; Histidine biosynthesis; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..297
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000151958"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 297 AA; 32266 MW; 9251252C0EFF8A80 CRC64;
MDLVNHLTDR LLFAIPKKGR LYSKSVSILN GADITFHRSQ RLDIALSTSL PVALVFLPAA
DIPTFVGEGK CDLGITGVDQ VRESNVDVDL AIDLQFGNCK LQVQVPVNGE YKKPEQLIGK
TIVTSFVKLA EKYFADLEGT TVEKMTTRIK FVSGSVEASC ALGIGDAIVD LVESGETMRA
AGLVDIATVL STSAYLIESK NPKSDKSLIA TIKSRIEGVM TAQRFVSCIY NAPEDKLPEL
LKVTPGRRAP TISKIDDEGW VAVSSMIERK TKGVVLDELK RLGASDIMVF EISNCRV
