ID   HIS1_STAA9              Reviewed;         204 AA.
AC   A5IWA6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01018};
DE            Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_01018};
DE            Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_01018};
DE            EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_01018};
GN   Name=hisG {ECO:0000255|HAMAP-Rule:MF_01018};
GN   OrderedLocusNames=SaurJH9_2703;
OS   Staphylococcus aureus (strain JH9).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=359786;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JH9;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tomasz A., Richardson P.;
RT   "Complete sequence of chromosome of Staphylococcus aureus subsp. aureus
RT   JH9.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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 HisG enzymatic activity.
CC       {ECO:0000255|HAMAP-Rule:MF_01018}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01018};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01018}.
CC   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_01018}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01018}.
CC   -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by
CC       HisZ.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01018}.
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DR   EMBL; CP000703; ABQ50479.1; -; Genomic_DNA.
DR   RefSeq; WP_000944149.1; NC_009487.1.
DR   AlphaFoldDB; A5IWA6; -.
DR   SMR; A5IWA6; -.
DR   KEGG; saj:SaurJH9_2703; -.
DR   HOGENOM; CLU_038115_2_0_9; -.
DR   OMA; YVMMDYD; -.
DR   UniPathway; UPA00031; UER00006.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd13595; PBP2_HisGs; 1.
DR   HAMAP; MF_01018; HisG_Short; 1.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR   InterPro; IPR024893; ATP_PRibTrfase_HisG_short.
DR   PANTHER; PTHR21403; PTHR21403; 1.
DR   Pfam; PF01634; HisG; 1.
DR   TIGRFAMs; TIGR00070; hisG; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Glycosyltransferase;
KW   Histidine biosynthesis; Nucleotide-binding; Transferase.
FT   CHAIN           1..204
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_1000084162"
SQ   SEQUENCE   204 AA;  22643 MW;  EE81C7225FDB18C2 CRC64;
     MLRIAIAKGR LMDSLINYLD VIEYTTLSET LKNRERQLLL SVDNIECILV KGSDVPIYVE
     QGMADIGIVG SDILDERQYN VNNLLNMPFG ACHFAVAAKP ETTNYRKIAT SYVHTAETYF
     KSKGIDVELI KLNGSVELAC VVDMVDGIVD IVQTGTTLKA NGLVEKQHIS DINARLITNK
     AAYFKKSQLI EQFIRSLEVS IANA