HIS1_ECO57
ID HIS1_ECO57 Reviewed; 299 AA.
AC Q8X8T4; Q9WX46;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00079};
DE Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_00079};
DE Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_00079};
DE EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_00079};
GN Name=hisG {ECO:0000255|HAMAP-Rule:MF_00079};
GN OrderedLocusNames=Z3181, ECs2820;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-299.
RC STRAIN=O157:H- / 184 / EHEC;
RX PubMed=10222209; DOI=10.1006/mpat.1998.0253;
RA Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y.;
RT "Analysis of the genes responsible for the O-antigen synthesis in
RT enterohaemorrhagic Escherichia coli O157.";
RL Microb. Pathog. 26:235-247(1999).
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_00079}.
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_00079};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00079};
CC -!- ACTIVITY REGULATION: Feedback inhibited by histidine.
CC {ECO:0000255|HAMAP-Rule:MF_00079}.
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_00079}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_00079}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00079}.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00079}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA77746.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG57078.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36243.1; -; Genomic_DNA.
DR EMBL; AB008676; BAA77746.1; ALT_INIT; Genomic_DNA.
DR PIR; B85827; B85827.
DR PIR; D90981; D90981.
DR RefSeq; NP_310847.1; NC_002695.1.
DR RefSeq; WP_000131775.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X8T4; -.
DR SMR; Q8X8T4; -.
DR STRING; 155864.EDL933_3091; -.
DR EnsemblBacteria; AAG57078; AAG57078; Z3181.
DR EnsemblBacteria; BAB36243; BAB36243; ECs_2820.
DR GeneID; 912832; -.
DR KEGG; ece:Z3181; -.
DR KEGG; ecs:ECs_2820; -.
DR PATRIC; fig|386585.9.peg.2955; -.
DR eggNOG; COG0040; Bacteria.
DR HOGENOM; CLU_038115_1_0_6; -.
DR OMA; YVMMDYD; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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..299
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000151850"
SQ SEQUENCE 299 AA; 33352 MW; 6D1B865234881630 CRC64;
MTDNTRLRIA MQKSGRLSDD SRELLARCGI KINLHTQRLI AMAENMPIDI LRVRDDDIPG
LVMDGVVDLG IIGENVLEEE LLNRRAQGED PRYFTLRRLD FGGCRLSLAT PVDDAWDGPL
SLNGKRIATS YPHLLKRYLD QKGISFKSCL LNGSVEVAPR AGLADAICDL VSTGATLEAN
GLREVEVIYR SKACLIQRDG EMEESKQQLI DKLLTRIQGV IQARESKYIM MHAPTQRLDE
VIALLPGAER PTILPLAGDQ QRVAMHMVSS ETLFWETMEK LKALGASSIL VLPIEKMME
