ID A0A3N7IRW7_9BURK Unreviewed; 254 AA.
AC A0A3N7IRW7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=imidazole glycerol-phosphate synthase {ECO:0000256|ARBA:ARBA00012809};
DE EC=4.3.2.10 {ECO:0000256|ARBA:ARBA00012809};
DE AltName: Full=IGP synthase cyclase subunit {ECO:0000256|ARBA:ARBA00030264};
GN Name=hisF {ECO:0000313|EMBL:RQP21612.1};
GN ORFNames=DZC73_27280 {ECO:0000313|EMBL:RQP21612.1};
OS Albitalea terrae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Albitalea.
OX NCBI_TaxID=2496871 {ECO:0000313|EMBL:RQP21612.1, ECO:0000313|Proteomes:UP000267464};
RN [1] {ECO:0000313|EMBL:RQP21612.1, ECO:0000313|Proteomes:UP000267464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-16 {ECO:0000313|EMBL:RQP21612.1,
RC ECO:0000313|Proteomes:UP000267464};
RA Khan S.A., Jeon C.O., Chun B.H., Jeong S.E.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RQP21612.1, ECO:0000313|Proteomes:UP000267464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-16 {ECO:0000313|EMBL:RQP21612.1,
RC ECO:0000313|Proteomes:UP000267464};
RA Shunsuke S.S.;
RT "Rhizobacter gummiphilus sp. nov., a rubber-degrading bacterium isolated
RT from the soil of a botanical garden in Japan.";
RL Submitted (DEC-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RQP21612.1}.
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DR EMBL; QUSW01000010; RQP21612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N7IRW7; -.
DR OrthoDB; 9781903at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000267464; 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; NF038364; AglZ_HisF2_fam; 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:UP000267464}.
SQ SEQUENCE 254 AA; 27393 MW; 0722E00DB3344700 CRC64;
MLRPRIIPCL LVHKGGLVKT VGFDKPKYVG DPLNAVRIFN EKEVDELMVV DIDATREGRD
PDYALIRSMA AECRMPLAYG GGVRTVEQFQ RIVGLGVEKV AVSAAAVNDP ALITAAAERV
GRQSIVVVMD VRRKRSKWEV FTHNGTRATG LDAAEFARRA EQLGAGEIVV NSIDQDGQMK
GYDLDLVRSV RGATSRPLTV LGGAGKLTDI AGLVREFGII GAAAGSLFVF KGIYRAVLIN
YPQRADKDAL IASA
//
