HIS1_CAMJR
ID HIS1_CAMJR Reviewed; 299 AA.
AC Q5HSJ4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=CJE1769;
OS Campylobacter jejuni (strain RM1221).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=195099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM1221;
RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA Nelson K.E.;
RT "Major structural differences and novel potential virulence mechanisms from
RT the genomes of multiple Campylobacter species.";
RL PLoS Biol. 3:72-85(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000025; AAW36193.1; -; Genomic_DNA.
DR RefSeq; WP_002858407.1; NC_003912.7.
DR PDB; 4YB5; X-ray; 2.24 A; A/B/C/D/E/F=1-299.
DR PDB; 4YB6; X-ray; 1.98 A; A/B/C/D/E/F=1-299.
DR PDB; 4YB7; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-299.
DR PDB; 5UB9; X-ray; 1.90 A; A/B=1-225.
DR PDB; 5UBG; X-ray; 1.90 A; A/B=1-225.
DR PDB; 5UBH; X-ray; 2.00 A; A/B=1-225.
DR PDB; 5UBI; X-ray; 2.14 A; A/B=1-225.
DR PDBsum; 4YB5; -.
DR PDBsum; 4YB6; -.
DR PDBsum; 4YB7; -.
DR PDBsum; 5UB9; -.
DR PDBsum; 5UBG; -.
DR PDBsum; 5UBH; -.
DR PDBsum; 5UBI; -.
DR AlphaFoldDB; Q5HSJ4; -.
DR SMR; Q5HSJ4; -.
DR KEGG; cjr:CJE1769; -.
DR HOGENOM; CLU_038115_1_0_7; -.
DR OMA; YVMMDYD; -.
DR BRENDA; 2.4.2.17; 1087.
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: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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW Glycosyltransferase; Histidine biosynthesis; Magnesium; Metal-binding;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..299
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000151840"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:5UB9"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:5UB9"
FT STRAND 36..53
FT /evidence="ECO:0007829|PDB:5UB9"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5UB9"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:5UB9"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:5UB9"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:5UB9"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5UB9"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:5UB9"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:5UB9"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:5UB9"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:5UB9"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:5UB9"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:5UB9"
FT TURN 158..162
FT /evidence="ECO:0007829|PDB:5UB9"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:5UB9"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5UB9"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:5UB9"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5UB9"
FT HELIX 204..223
FT /evidence="ECO:0007829|PDB:5UB9"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:4YB6"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:4YB6"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:4YB6"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:4YB6"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:4YB6"
FT STRAND 259..270
FT /evidence="ECO:0007829|PDB:4YB6"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:4YB6"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:4YB6"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:4YB6"
SQ SEQUENCE 299 AA; 33639 MW; 9362C62019697F4E CRC64;
MQENTRLRIA IQKSGRLSKE SIELLSECGV KMHIHEQSLI AFSTNLPIDI LRVRDDDIPG
LIFDGVVDLG IIGENVLEEN ELERQSLGEN PSYKLLKKLD FGYCRLSLAL PQENKFQNLK
DFEGLRIATS YPQLLKRFMK ENGINYKNCT LTGSVEVAPR ANLADAICDL VSSGATLQAN
NLKEVKVIYE SRACLIQKEN ALSKEKQALV DKIMLRVAGV MQARESKYIM LHAPKEKLDK
IQALLPGVER PTILPLAHDE KNVALHMVSK ENLFWETMEA LKEEGASSIL VLPIEKMLK
