HIS61_CAMJE
ID HIS61_CAMJE Reviewed; 255 AA.
AC Q9PM72; Q0P825;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit hisF1;
DE EC=4.3.2.10;
DE AltName: Full=IGP synthase cyclase subunit;
DE AltName: Full=IGP synthase subunit hisF1;
DE AltName: Full=ImGP synthase subunit hisF1;
DE Short=IGPS subunit hisF1;
GN Name=hisF1; Synonyms=hisF; OrderedLocusNames=Cj1603;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC AICAR and glutamate. The HisF subunit catalyzes the cyclization
CC activity that produces IGP and AICAR from PRFAR using the ammonia
CC provided by the HisH subunit (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-
CC phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-
CC amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-
CC erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate;
CC Xref=Rhea:RHEA:24793, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58278, ChEBI:CHEBI:58359, ChEBI:CHEBI:58475,
CC ChEBI:CHEBI:58525; EC=4.3.2.10;
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
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DR EMBL; AL111168; CAL35700.1; -; Genomic_DNA.
DR PIR; A81256; A81256.
DR RefSeq; WP_002851492.1; NC_002163.1.
DR RefSeq; YP_002344972.1; NC_002163.1.
DR AlphaFoldDB; Q9PM72; -.
DR SMR; Q9PM72; -.
DR IntAct; Q9PM72; 8.
DR STRING; 192222.Cj1603; -.
DR PaxDb; Q9PM72; -.
DR PRIDE; Q9PM72; -.
DR EnsemblBacteria; CAL35700; CAL35700; Cj1603.
DR GeneID; 905871; -.
DR KEGG; cje:Cj1603; -.
DR PATRIC; fig|192222.6.peg.1579; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_7; -.
DR OMA; IFHYKET; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04731; HisF; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01013; HisF; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR004651; HisF.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00735; hisF; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Lyase;
KW Reference proteome.
FT CHAIN 1..255
FT /note="Imidazole glycerol phosphate synthase subunit hisF1"
FT /id="PRO_0000142138"
FT ACT_SITE 11
FT /evidence="ECO:0000255"
FT ACT_SITE 130
FT /evidence="ECO:0000255"
SQ SEQUENCE 255 AA; 28059 MW; 5760DD5178730D1A CRC64;
MLTKRIIACL DVKDGRVVKG TQFKNHKDMG DIIELARYYS QNGIDELVFY DIAASARKER
ISREWVSEVA KNINISFCVA GGIKSEEDAA ELLANGADKI SINSPALNDP SLITRLAKSF
GVQCVVVGID SFKDENGNLK VFQYTGDEKT SKHSGKSTLE WVKKVQDLGA GEIVLNMMNQ
DGVKNGYDLE QLEAVYKICK VPLIASGGAG KMEHFLEAFK LGIDGALAAS VFHQKLIDIK
ELKIYLKNQG LSIRI
