ID A0A1I4XVS2_9NEIS Unreviewed; 253 AA.
AC A0A1I4XVS2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ORFNames=SAMN05660284_01144 {ECO:0000313|EMBL:SFN29998.1};
OS Formivibrio citricus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Formivibrio.
OX NCBI_TaxID=83765 {ECO:0000313|EMBL:SFN29998.1, ECO:0000313|Proteomes:UP000242869};
RN [1] {ECO:0000313|Proteomes:UP000242869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6150 {ECO:0000313|Proteomes:UP000242869};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOVE01000006; SFN29998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4XVS2; -.
DR STRING; 83765.SAMN05660284_01144; -.
DR OrthoDB; 9781903at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000242869; 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 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:UP000242869}.
SQ SEQUENCE 253 AA; 27050 MW; 228BBC544167398B CRC64;
MLKKRVIPVL LLRDGRMAKG VQFGNYRDTG NPKTAVRIYS AQDADELVFL DIQASLQSRT
ALLEIIREAA TECFMPLAAG GGIESIDDVR ELLLAGADKV VVTTAAVTNP GLITAISERF
GNQCVVAGID YRCDADGAKV WIRCGTEATQ LDPVEHARNL AALGAGEIFL NSIDHDGLMD
GYDLDMAEKI ASAVSVPVIV CGGAGNFMHL AELLKDTSAS AAACASLFHF GDNNPIRARS
YLRNLGIPMR VLK
//
