ID   HIS62_CAMJJ             Reviewed;         248 AA.
AC   A1W0U8; Q939J5; Q9PMY5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Putative imidazole glycerol phosphate synthase subunit hisF2;
DE            EC=4.3.2.10;
DE   AltName: Full=IGP synthase cyclase subunit;
DE   AltName: Full=IGP synthase subunit hisF2;
DE   AltName: Full=ImGP synthase subunit hisF2;
DE            Short=IGPS subunit hisF2;
GN   Name=hisF2; OrderedLocusNames=CJJ81176_1331;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11461915; DOI=10.1074/jbc.m104529200;
RA   Thibault P., Logan S.M., Kelly J.F., Brisson J.-R., Ewing C.P., Trust T.J.,
RA   Guerry P.;
RT   "Identification of the carbohydrate moieties and glycosylation motifs in
RT   Campylobacter jejuni flagellin.";
RL   J. Biol. Chem. 276:34862-34870(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The potential active site Asp residue in position 11 is
CC       replaced by a Leu. {ECO:0000305}.
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DR   EMBL; AY102622; AAK58488.1; -; Genomic_DNA.
DR   EMBL; CP000538; EAQ72788.1; -; Genomic_DNA.
DR   RefSeq; WP_002786691.1; NC_008787.1.
DR   AlphaFoldDB; A1W0U8; -.
DR   SMR; A1W0U8; -.
DR   STRING; 354242.CJJ81176_1331; -.
DR   EnsemblBacteria; EAQ72788; EAQ72788; CJJ81176_1331.
DR   KEGG; cjj:CJJ81176_1331; -.
DR   eggNOG; COG0107; Bacteria.
DR   HOGENOM; CLU_048577_4_0_7; -.
DR   OMA; IMPCLDM; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000000646; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:InterPro.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04731; HisF; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR020021; Glycosyl_amidation-assoc_WbuZ.
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; TIGR03572; WbuZ; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Lyase.
FT   CHAIN           1..248
FT                   /note="Putative imidazole glycerol phosphate synthase
FT                   subunit hisF2"
FT                   /id="PRO_0000281904"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   248 AA;  27438 MW;  0E792CC7D7357708 CRC64;
     MLKTRIIPCV LLKNGQLVKS IEFKDFRTIG HLTSTMRIYN ARNVDELIIL DIDASKSGEI
     DFESIEDLAK ECFMPLTIGG GIKTLEDIQK ILNLGADKIS INSKALEDMD FISKAANRFG
     SQCIVCSIDV KRKGGQFCVY DRGNLLEKSP LELALEYEKK GAGELLLTSV DFEGRAKGYD
     LELLKIFQNK LKIPLIINGG LSNPSDGVEA LNLGADALAG AYIFHFSKYT PKDVKEELAR
     QGFAVRLL