ID A0A1X7MWI4_9LACT Unreviewed; 251 AA.
AC A0A1X7MWI4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF {ECO:0000256|ARBA:ARBA00016318};
DE EC=4.3.2.10 {ECO:0000256|ARBA:ARBA00012809};
DE AltName: Full=IGP synthase cyclase subunit {ECO:0000256|ARBA:ARBA00030264};
DE AltName: Full=IGP synthase subunit HisF {ECO:0000256|ARBA:ARBA00031409};
DE AltName: Full=ImGP synthase subunit HisF {ECO:0000256|ARBA:ARBA00032401};
GN ORFNames=SAMN04488700_1036 {ECO:0000313|EMBL:SMH29189.1};
OS Carnobacterium iners.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1073423 {ECO:0000313|EMBL:SMH29189.1, ECO:0000313|Proteomes:UP000193435};
RN [1] {ECO:0000313|EMBL:SMH29189.1, ECO:0000313|Proteomes:UP000193435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG26642 {ECO:0000313|EMBL:SMH29189.1,
RC ECO:0000313|Proteomes:UP000193435};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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. {ECO:0000256|ARBA:ARBA00025475}.
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 Evidence={ECO:0000256|ARBA:ARBA00000619};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC {ECO:0000256|ARBA:ARBA00005091}.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|ARBA:ARBA00011152}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family.
CC {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|RuleBase:RU003657}.
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DR EMBL; FXBJ01000002; SMH29189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7MWI4; -.
DR STRING; 1073423.SAMN04488700_1036; -.
DR OrthoDB; 9781903at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000193435; Unassembled WGS sequence.
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; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR004651; HisF.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR00735; hisF; 1.
DR PANTHER; PTHR21235:SF2; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE HISHF; 1.
DR PANTHER; PTHR21235; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H IGP SYNTHASE SUBUNIT HISF/H; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU003657};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102,
KW ECO:0000256|RuleBase:RU003657};
KW Reference proteome {ECO:0000313|Proteomes:UP000193435}.
SQ SEQUENCE 251 AA; 27060 MW; B188CF24C960ED8C CRC64;
MLIRVIPCLD VRDGRVVKGK QFDQIVDVDD PEVLAEYYSK AGADELVFYD ITATNEKRNV
SLDFIEKVVE KITIPLCVGG GVSNLADFTN IMDKGANKVS INSGAVKTPE LIKEASEKFS
SKAVVLGMDI KKIGEDKWRI FTNGARIDTG LDAVEWAIEA VKLGAGELVV NSIDADGMKE
GYDIELLNKL ASAVSVPVIA SGGAGKLEDF VEAATKGKAR GVLAASVFHY KEIEIGDLKQ
YMKSKGLEVS L
//
