HIS1_CAMLR
ID HIS1_CAMLR Reviewed; 299 AA.
AC B9KEH8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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}; OrderedLocusNames=Cla_0097;
OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=306263;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM2100 / D67 / ATCC BAA-1060;
RX PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT "The complete genome sequence and analysis of the human pathogen
RT Campylobacter lari.";
RL Foodborne Pathog. Dis. 5:371-386(2008).
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 -!- 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}.
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DR EMBL; CP000932; ACM63463.1; -; Genomic_DNA.
DR RefSeq; WP_012660848.1; NC_012039.1.
DR AlphaFoldDB; B9KEH8; -.
DR SMR; B9KEH8; -.
DR STRING; 306263.Cla_0097; -.
DR EnsemblBacteria; ACM63463; ACM63463; CLA_0097.
DR GeneID; 7411329; -.
DR KEGG; cla:CLA_0097; -.
DR PATRIC; fig|306263.5.peg.97; -.
DR eggNOG; COG0040; Bacteria.
DR HOGENOM; CLU_038115_1_0_7; -.
DR OMA; YVMMDYD; -.
DR OrthoDB; 1419568at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000007727; 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 Transferase.
FT CHAIN 1..299
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_1000118247"
SQ SEQUENCE 299 AA; 33370 MW; 636D0D36CA451362 CRC64;
MQENSRLRIA IQKSGRLSKD SIALLESIGV KLRIHDQSLI AFSTNLPIDL LRVRDDDIPG
LIFDGVVDLG IVGENVLEEN ELERKSKNEN ADFIMLKKLD FGGCRLSLAL PENSEYKGVE
SFKNLRIATS YPQLLKRFME ENNIPYKTCM LTGSVEVAPS ANLADGICDL VSSGATLKAN
GLKEVMVIYK SKACIIQRKE SLVSHKQELI DKLLIRINGV MQARESKYIM LHAPIEKLEK
ITALLPGVEK PTILPLENDK ARVALHMVSQ ENLFWETMEA LKKEGASAIL VLPIEKMLS
