HIS1_SALTY
ID HIS1_SALTY Reviewed; 299 AA.
AC P00499;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ATP phosphoribosyltransferase;
DE Short=ATP-PRT;
DE Short=ATP-PRTase;
DE EC=2.4.2.17;
GN Name=hisG; OrderedLocusNames=STM2071;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=377278; DOI=10.1073/pnas.76.4.1589;
RA Piszkiewicz D., Tilley B.E., Rand-Meir T., Parsons S.M.;
RT "Amino acid sequence of ATP phosphoribosyltransferase of Salmonella
RT typhimurium.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:1589-1592(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=3062174; DOI=10.1016/0022-2836(88)90194-5;
RA Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.;
RT "Structure and function of the Salmonella typhimurium and Escherichia coli
RT K-12 histidine operons.";
RL J. Mol. Biol. 203:585-606(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Barnes W.M., Husson R.N., Whittier R.;
RL Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2666402; DOI=10.1128/jb.171.8.4472-4478.1989;
RA Ciampi M.S., Alifano P., Nappo A.G., Bruni C.B., Carlomagno M.S.;
RT "Features of the rho-dependent transcription termination polar element
RT within the hisG cistron of Salmonella typhimurium.";
RL J. Bacteriol. 171:4472-4478(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RC STRAIN=LT2;
RX PubMed=360216; DOI=10.1073/pnas.75.9.4281;
RA Barnes W.M.;
RT "DNA sequence from the histidine operon control region: seven histidine
RT codons in a row.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:4281-4285(1978).
RN [7]
RP CATALYTIC ACTIVITY, COFACTOR, AND INHIBITION BY HISTIDINE.
RX PubMed=13682989;
RA Ames B.N., Martin R.G., Garry B.J.;
RT "The first step of histidine biosynthesis.";
RL J. Biol. Chem. 236:2019-2026(1961).
RN [8]
RP INHIBITION BY HISTIDINE, AND SUBUNIT.
RC STRAIN=LT2;
RX PubMed=5337591; DOI=10.1016/s0021-9258(18)96066-7;
RA Voll M.J., Appella E., Martin R.G.;
RT "Purification and composition studies of phosphoribosyladenosine
RT triphosphate:pyrophosphate phosphoribosyltransferase, the first enzyme of
RT histidine biosynthesis.";
RL J. Biol. Chem. 242:1760-1767(1967).
RN [9]
RP INHIBITION BY AMP AND ADP.
RX PubMed=332083; DOI=10.1016/0003-9861(77)90270-3;
RA Morton D.P., Parsons S.M.;
RT "Inhibition of ATP phosphoribosyltransferase by AMP and ADP in the absence
RT and presence of histidine.";
RL Arch. Biochem. Biophys. 181:643-648(1977).
RN [10]
RP REGULATION BY PPGPP.
RX PubMed=319792; DOI=10.1016/0006-291x(77)91390-0;
RA Morton D.P., Parsons S.M.;
RT "Synergistic inhibition of ATP phosphoribosyltransferase by guanosine
RT tetraphosphate and histidine.";
RL Biochem. Biophys. Res. Commun. 74:172-177(1977).
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 Evidence={ECO:0000269|PubMed:13682989};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:13682989};
CC -!- ACTIVITY REGULATION: Feedback inhibited by histidine. Also inhibited by
CC AMP and ADP.
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 (Probable).
CC {ECO:0000305|PubMed:5337591}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Repressed by ppGpp in the presence of histidine.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC subfamily. {ECO:0000305}.
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DR EMBL; X13464; CAA31822.1; -; Genomic_DNA.
DR EMBL; J01804; AAA88614.1; -; Genomic_DNA.
DR EMBL; M28367; AAA27142.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20975.1; -; Genomic_DNA.
DR EMBL; V01371; CAA24657.1; -; Genomic_DNA.
DR PIR; JS0156; XREBT.
DR RefSeq; NP_461016.1; NC_003197.2.
DR RefSeq; WP_000886603.1; NC_003197.2.
DR AlphaFoldDB; P00499; -.
DR SMR; P00499; -.
DR STRING; 99287.STM2071; -.
DR PaxDb; P00499; -.
DR EnsemblBacteria; AAL20975; AAL20975; STM2071.
DR GeneID; 1253592; -.
DR KEGG; stm:STM2071; -.
DR PATRIC; fig|99287.12.peg.2193; -.
DR HOGENOM; CLU_038115_1_0_6; -.
DR PhylomeDB; P00499; -.
DR BioCyc; SENT99287:STM2071-MON; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001014; 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; 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 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Glycosyltransferase; Histidine biosynthesis; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..299
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000151864"
SQ SEQUENCE 299 AA; 33212 MW; EE165D90C49B36F8 CRC64;
MLDNTRLRIA IQKSGRLSDD SRELLARCGI KINLHTQRLI AMAENMPIDI LRVRDDDIPG
LVMDGVVDLG IIGENVLEEE LLNRRAQGED PRYLTLRRLD FGGCRLSLAT PVDEAWDGPA
ALDGKRIATS YPHLLKRYLD QKGVSFKSCL LNGSVEVAPR AGLADAICDL VSTGATLEAN
GLREVEVIYR SKACLIQRDG EMAQSKQELI DKLLTRIQGV IQARESKYIM MHAPSERLEE
VIALLPGAER PTILPLAGEQ QRVAMHMVSS ETLFWETMEK LKALGASSIL VLPIEKMME
