HIS62_CAMJE
ID HIS62_CAMJE Reviewed; 248 AA.
AC Q0P8U3; Q939J5; Q9PMY5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=Cj1314c;
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}.
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; AL111168; CAL35428.1; -; Genomic_DNA.
DR PIR; G81274; G81274.
DR RefSeq; WP_002858306.1; NC_002163.1.
DR RefSeq; YP_002344704.1; NC_002163.1.
DR AlphaFoldDB; Q0P8U3; -.
DR SMR; Q0P8U3; -.
DR STRING; 192222.Cj1314c; -.
DR PaxDb; Q0P8U3; -.
DR PRIDE; Q0P8U3; -.
DR EnsemblBacteria; CAL35428; CAL35428; Cj1314c.
DR GeneID; 905606; -.
DR KEGG; cje:Cj1314c; -.
DR PATRIC; fig|192222.6.peg.1296; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_7; -.
DR OMA; IMPCLDM; -.
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:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR006062; His_biosynth.
DR InterPro; IPR004651; HisF.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Lyase;
KW Reference proteome.
FT CHAIN 1..248
FT /note="Putative imidazole glycerol phosphate synthase
FT subunit hisF2"
FT /id="PRO_0000142139"
FT ACT_SITE 129
FT /evidence="ECO:0000255"
SQ SEQUENCE 248 AA; 27498 MW; D5086CF0DA677359 CRC64;
MLKTRIIPCV LLKNSQLVKS IEFKDFRTIG HLTSTMRIYN ARNVDELIIL DIDASKSGEI
DFESIEDLAK ECFMPLTIGG GIKTLEDIQK ILNLGADKIS INSKALEDMD FISKAGNRFG
SQCIVCSIDV KRKGDQFCVY DRGNLLEKSP LELALEYEKK GAGELLLTSV DFEGKAKGYD
LELLKIFQNK LKIPLIINGG LSKPSDGVEA LNLGADALAG AYIFHFSKYT PKDVKEELAR
QGFAVRLL
