ID   HIS1_SYNE7              Reviewed;         218 AA.
AC   Q31Q54;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Synpcc7942_0783;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
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; CP000100; ABB56815.1; -; Genomic_DNA.
DR   RefSeq; WP_011243066.1; NC_007604.1.
DR   AlphaFoldDB; Q31Q54; -.
DR   SMR; Q31Q54; -.
DR   STRING; 1140.Synpcc7942_0783; -.
DR   PRIDE; Q31Q54; -.
DR   EnsemblBacteria; ABB56815; ABB56815; Synpcc7942_0783.
DR   KEGG; syf:Synpcc7942_0783; -.
DR   eggNOG; COG0040; Bacteria.
DR   HOGENOM; CLU_038115_2_0_3; -.
DR   OMA; VASKFVH; -.
DR   OrthoDB; 1419568at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_0783-MON; -.
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; 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; Transferase.
FT   CHAIN           1..218
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_1000063313"
SQ   SEQUENCE   218 AA;  23791 MW;  15F4968CC4B37EF6 CRC64;
     MLTIALPKGA LLKDSIRLLQ SAGLDFSAFL EPGNRQLQIL DRQERAKALL VRNSDVPVYV
     EYGQAQLGVV GYDVLREKTA RVAQLIDLRF GGCRMSIAVK ASSPYRSVLD LPAHCRIASK
     FVHCARDYFH NLDLPVEIVP LSGSVELGPI TGMSEAIVDL VATGQTLREN GLVEIETLFD
     STARLIANPL AYRINADGIS ELIEELRQSV TQAIAATC