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Database: UniProt
Entry: A0A154BR69_ANASB
LinkDB: A0A154BR69_ANASB
Original site: A0A154BR69_ANASB 
ID   A0A154BR69_ANASB        Unreviewed;       256 AA.
AC   A0A154BR69;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=AXX12_08280 {ECO:0000313|EMBL:KYZ76421.1};
OS   Anaerosporomusa subterranea.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Anaerosporomusa.
OX   NCBI_TaxID=1794912 {ECO:0000313|EMBL:KYZ76421.1, ECO:0000313|Proteomes:UP000076268};
RN   [1] {ECO:0000313|EMBL:KYZ76421.1, ECO:0000313|Proteomes:UP000076268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU4 {ECO:0000313|EMBL:KYZ76421.1,
RC   ECO:0000313|Proteomes:UP000076268};
RA   Choi J.K., Shah M., Yee N.;
RT   "Anaerosporomusa subterraneum gen. nov., sp. nov., a spore-forming obligate
RT   anaerobe isolated from saprolite.";
RL   Submitted (FEB-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}.
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:KYZ76421.1}.
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DR   EMBL; LSGP01000017; KYZ76421.1; -; Genomic_DNA.
DR   RefSeq; WP_066241864.1; NZ_LSGP01000017.1.
DR   AlphaFoldDB; A0A154BR69; -.
DR   STRING; 1794912.AXX12_08280; -.
DR   OrthoDB; 9781903at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000076268; Unassembled WGS sequence.
DR   GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:InterPro.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
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; IPR020021; Glycosyl_amidation-assoc_WbuZ.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR004651; HisF.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; NF038364; AglZ_HisF2_fam; 1.
DR   NCBIfam; TIGR03572; WbuZ; 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:UP000076268}.
SQ   SEQUENCE   256 AA;  27951 MW;  10D2DE7D581609D9 CRC64;
     MYLRPRVIPC LLLKNNGLVK TVKFKDPRYL GDPINAVRIF NEKYVDELAI LDIVATKEKR
     SPNLELLSRI AAEAFMPMCY GGGISTLDEV KIILGMGFEK VVINTSAVKN PMLIQEASGH
     FGSQSIVVSI DVKKNFFGKY RAYINCGEVA TDYDPAELAR KVEQLGAGEI FLNSIDKDGT
     MSGYDLGLIK KVSESVGIPV IACGGARNVD DLSMALHNGK ADAMAAGSMF VYYGKHKAVL
     ITFPNEEELI KAGVFT
//
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