ID W9V0U4_9GAMM Unreviewed; 263 AA.
AC W9V0U4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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_1 {ECO:0000313|EMBL:EXJ09762.1};
GN ORFNames=D791_03257 {ECO:0000313|EMBL:EXJ09762.1};
OS Nitrincola nitratireducens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=1229521 {ECO:0000313|EMBL:EXJ09762.1, ECO:0000313|Proteomes:UP000019464};
RN [1] {ECO:0000313|Proteomes:UP000019464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK23 {ECO:0000313|Proteomes:UP000019464};
RA Singh A., Pinnaka A.K., Vaidya B.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXJ09762.1, ECO:0000313|Proteomes:UP000019464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK23 {ECO:0000313|EMBL:EXJ09762.1,
RC ECO:0000313|Proteomes:UP000019464};
RX PubMed=26481633; DOI=10.1016/j.syapm.2015.09.002;
RA Singh A., Vaidya B., Tanuku N.R., Pinnaka A.K.;
RT "Nitrincola nitratireducens sp. nov. isolated from a haloalkaline crater
RT lake.";
RL Syst. Appl. Microbiol. 38:555-562(2015).
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:EXJ09762.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AONB01000020; EXJ09762.1; -; Genomic_DNA.
DR RefSeq; WP_036513267.1; NZ_AONB01000020.1.
DR AlphaFoldDB; W9V0U4; -.
DR STRING; 1229521.D791_03257; -.
DR PATRIC; fig|1229521.3.peg.3291; -.
DR OrthoDB; 9807749at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000019464; 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}; Lyase {ECO:0000313|EMBL:EXJ09762.1}.
SQ SEQUENCE 263 AA; 28348 MW; 8412BA8C17C1BC7B CRC64;
MLRPRIIPCL LVHQGGLVKT QRFKDPKYVG DPINAVKIFN EKEADELMVL DIDAAVKGAA
PDFTMIAKLA AECRMPLCYG GGVTSAEQAS RIIDMGVEKV AVSSAAIRNP TLLTEIAAAV
GRQSVVAVLD VRQKKGFFAK GYELCIHNAT QAVKSDPLDM AKQLQEAGAG EIVINFVDQD
GLMQGYDLEY AAEFKRVLKV PVTFLGGAGS LDHLQQLISK LGIVGAAAGS LFVFKGKYRA
VLINYPSPEQ KIQLCRDALN IKG
//