ID   HIS1_VIBCH              Reviewed;         298 AA.
AC   Q9KSX4;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 2.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=ATP phosphoribosyltransferase;
DE            Short=ATP-PRT;
DE            Short=ATP-PRTase;
DE            EC=2.4.2.17;
GN   Name=hisG; OrderedLocusNames=VC_1132;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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 (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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Feedback inhibited by histidine. {ECO:0000250}.
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. Long
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF94291.1; Type=Erroneous initiation; Evidence={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; AE003852; AAF94291.1; ALT_INIT; Genomic_DNA.
DR   PIR; G82237; G82237.
DR   RefSeq; NP_230777.1; NC_002505.1.
DR   RefSeq; WP_001194704.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KSX4; -.
DR   SMR; Q9KSX4; -.
DR   STRING; 243277.VC_1132; -.
DR   DNASU; 2614402; -.
DR   EnsemblBacteria; AAF94291; AAF94291; VC_1132.
DR   GeneID; 57739808; -.
DR   GeneID; 66939042; -.
DR   KEGG; vch:VC_1132; -.
DR   PATRIC; fig|243277.26.peg.1081; -.
DR   eggNOG; COG0040; Bacteria.
DR   HOGENOM; CLU_038115_1_0_6; -.
DR   OMA; YVMMDYD; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000584; Chromosome 1.
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; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Glycosyltransferase;
KW   Histidine biosynthesis; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..298
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_0000151869"
SQ   SEQUENCE   298 AA;  32934 MW;  5DFE68C92EC962C6 CRC64;
     MQTQRLRIAI QKKGRLSQEC QELLKKCGVK FNIMGERLVV HSLNMPIDLL LVRDDDIPGL
     IMDGVVDLGF VGENVLEETR LDRLALNQRN EFTTLRRMDF GGCRLSIAIE KDAEYRGPQD
     LNGKRIATTY PQLLKAYMDR QGVDFSTCML TGSVEVAPRA GLADAIADLV STGATLEANG
     LKEVEVIFES KATLIQRPGA FAADKAALID KLLTRMHGVQ QAKESKYIML HAPVEKLAQI
     KTLLPGAEDP TVLPLSADKS KVAVHMVSSE NLFWETMEQL KALGASSILV LPIEKMME