ID   HIS1_KLEPN              Reviewed;         100 AA.
AC   P05148;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=ATP phosphoribosyltransferase;
DE            Short=ATP-PRT;
DE            Short=ATP-PRTase;
DE            EC=2.4.2.17;
DE   Flags: Fragment;
GN   Name=hisG;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6321433; DOI=10.1128/jb.157.3.764-771.1984;
RA   Rodriguez R.L., West R.W. Jr.;
RT   "Histidine operon control region of Klebsiella pneumoniae: analysis with an
RT   Escherichia coli promoter-probe plasmid vector.";
RL   J. Bacteriol. 157:764-771(1984).
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   -!- SUBUNIT: Equilibrium between an active dimeric form, an inactive
CC       hexameric form and higher aggregates. Interconversion between the
CC       various forms is largely reversible and is influenced by the natural
CC       substrates and inhibitors of the enzyme (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC       subfamily. {ECO:0000305}.
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DR   EMBL; K01997; AAA25073.1; -; Genomic_DNA.
DR   AlphaFoldDB; P05148; -.
DR   SMR; P05148; -.
DR   PRIDE; P05148; -.
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-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR   PANTHER; PTHR21403; PTHR21403; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Glycosyltransferase;
KW   Histidine biosynthesis; Magnesium; Metal-binding; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..>100
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_0000151853"
FT   NON_TER         100
SQ   SEQUENCE   100 AA;  11408 MW;  BDA8FEB042E012DE CRC64;
     MLDNSRLRIA IQKSGRLSED SRELLSRCGI KVNLHTQRLI ALAENMPIDI LRVRDDDIPG
     LIMNGVVDLG IIGENVLEEE LLNRRAQGED PRHFNPRRLD