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   04-NOV-2026, entry version 185.
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; DOI=10.1038/387s078;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 46.
DR   FunCoup; P00498; 286.
DR   IntAct; P00498; 18.
DR   STRING; 4932.YER055C; -.
DR   iPTMnet; P00498; -.
DR   PaxDb; 4932-YER055C; -.
DR   PeptideAtlas; P00498; -.
DR   EnsemblFungi; YER055C_mRNA; YER055C; YER055C.
DR   GeneID; 856782; -.
DR   KEGG; sce:YER055C; -.
DR   AGR; SGD:S000000857; -.
DR   SGD; S000000857; HIS1.
DR   VEuPathDB; FungiDB:YER055C; -.
DR   eggNOG; KOG2831; Eukaryota.
DR   HOGENOM; CLU_038115_1_2_1; -.
DR   InParanoid; P00498; -.
DR   OMA; AAKQYKY; -.
DR   OrthoDB; 2574at2759; -.
DR   BioCyc; YEAST:YER055C-MONOMER; -.
DR   UniPathway; UPA00031; UER00006.
DR   BioGRID-ORCS; 856782; 6 hits in 10 CRISPR screens.
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:0003879; F:ATP phosphoribosyltransferase activity; IMP:SGD.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0000105; P:L-histidine biosynthetic process; IMP:SGD.
DR   CDD; cd13592; PBP2_HisGL2; 1.
DR   FunFam; 3.30.70.120:FF:000003; ATP phosphoribosyltransferase; 1.
DR   FunFam; 3.40.190.10:FF:000123; HIS1p ATP phosphoribosyltransferase; 1.
DR   Gene3D; 3.30.70.120; -; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   HAMAP; MF_00079; HisG_Long; 1.
DR   InterPro; IPR020621; ATP-PRT_HisG_long.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR018198; ATP_PRibTrfase_CS.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR   InterPro; IPR013115; HisG_C.
DR   InterPro; IPR011322; N-reg_PII-like_a/b.
DR   InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR   NCBIfam; TIGR00070; hisG; 1.
DR   NCBIfam; TIGR03455; HisG_C-term; 1.
DR   PANTHER; PTHR21403:SF8; ATP PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1.
DR   Pfam; PF01634; HisG; 1.
DR   Pfam; PF08029; HisG_C; 1.
DR   SUPFAM; SSF54913; GlnB-like; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 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
//