HIS6_CORGL
ID HIS6_CORGL Reviewed; 258 AA.
AC O31139;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF;
DE EC=4.3.2.10;
DE AltName: Full=IGP synthase cyclase subunit;
DE AltName: Full=IGP synthase subunit HisF;
DE AltName: Full=ImGP synthase subunit HisF;
DE Short=IGPS subunit HisF;
GN Name=hisF; OrderedLocusNames=Cgl2094, cg2297;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=9647764; DOI=10.1006/bbrc.1998.8850;
RA Jung S.-I., Han M.-S., Kwon J.-H., Cheon C.-I., Min K.-H., Lee M.-S.;
RT "Cloning of the histidine biosynthetic genes of Corynebacterium glutamicum:
RT organization and sequencing analysis of the hisA, impA, and hisF gene
RT cluster.";
RL Biochem. Biophys. Res. Commun. 247:741-745(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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; AF030405; AAB84280.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99487.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20430.1; -; Genomic_DNA.
DR PIR; JE0214; JE0214.
DR RefSeq; NP_601293.1; NC_003450.3.
DR RefSeq; WP_003856413.1; NC_006958.1.
DR AlphaFoldDB; O31139; -.
DR SMR; O31139; -.
DR STRING; 196627.cg2297; -.
DR World-2DPAGE; 0001:O31139; -.
DR GeneID; 58308775; -.
DR KEGG; cgb:cg2297; -.
DR KEGG; cgl:Cgl2094; -.
DR PATRIC; fig|196627.13.peg.2030; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_11; -.
DR OMA; IFHYKET; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000000582; 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..258
FT /note="Imidazole glycerol phosphate synthase subunit HisF"
FT /id="PRO_0000142148"
FT ACT_SITE 12
FT /evidence="ECO:0000255"
FT ACT_SITE 131
FT /evidence="ECO:0000255"
FT CONFLICT 28..31
FT /note="RDAG -> AMLA (in Ref. 1; AAB84280)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="S -> W (in Ref. 1; AAB84280)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="Missing (in Ref. 1; AAB84280)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="A -> R (in Ref. 1; AAB84280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 258 AA; 27245 MW; 7A28B377697B52DF CRC64;
MGVAIRVIPC LDVDNGRVVK GVNFENLRDA GDPVELAKRY DEEGADELTF LDVTASKHGR
GTMLDVVRRT ADQVFIPLTV GGGVRSEEDV DQLLRAGADK VSVNTSAIAR PELLSELSKR
FGAQCIVLSV DARRVPEGGT PQPSGFEVTT HGGSKSAELD AIEWAKRGEE LGVGEILLNS
MDGDGTKNGF DLELLEKVRA AVSIPVIASG GAGKAEHFPP AVAAGANAVL AATIFHFREV
TIAEVKGAIK DAGFEVRK
