ID   HIS1_SYNS9              Reviewed;         216 AA.
AC   Q3AYI1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=Syncc9902_0880;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) 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; CP000097; ABB25846.1; -; Genomic_DNA.
DR   RefSeq; WP_011359683.1; NC_007513.1.
DR   AlphaFoldDB; Q3AYI1; -.
DR   SMR; Q3AYI1; -.
DR   STRING; 316279.Syncc9902_0880; -.
DR   EnsemblBacteria; ABB25846; ABB25846; Syncc9902_0880.
DR   KEGG; sye:Syncc9902_0880; -.
DR   eggNOG; COG0040; Bacteria.
DR   HOGENOM; CLU_038115_2_0_3; -.
DR   OMA; VASKFVH; -.
DR   OrthoDB; 1419568at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002712; Chromosome.
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; IPR018198; ATP_PRibTrfase_CS.
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.
DR   PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Glycosyltransferase;
KW   Histidine biosynthesis; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..216
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_1000063316"
SQ   SEQUENCE   216 AA;  23059 MW;  4005433C1F9888D1 CRC64;
     MITVALAKGA LLKDSVARFA AAGLDFSAVL DKDNRQLMVP TPCGRARALL VRNGDVPTYV
     SYGQAQLGVV GYDVLKEHQL PVAQLVDLGF GGCRMSVAVK ASSGYQRALD LPAHCRVASK
     FTHCAREYFD SLDLPVELVH LNGSVELGPI TGMSEAIVDL VATGRTLRDN GLVEIEELFR
     SSARLVGHPL SMRLDDGALT EIVTAIRAVE PSKGEA