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Entry: A0A1M5QB11_9BACT
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Original site: A0A1M5QB11_9BACT 
ID   A0A1M5QB11_9BACT        Unreviewed;       263 AA.
AC   A0A1M5QB11;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Imidazole glycerol phosphate synthase subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
DE            EC=4.3.2.10 {ECO:0000256|HAMAP-Rule:MF_01013};
DE   AltName: Full=IGP synthase cyclase subunit {ECO:0000256|HAMAP-Rule:MF_01013};
DE   AltName: Full=IGP synthase subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
DE   AltName: Full=ImGP synthase subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
DE            Short=IGPS subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
GN   Name=hisF {ECO:0000256|HAMAP-Rule:MF_01013};
GN   ORFNames=SAMN05720761_1098 {ECO:0000313|EMBL:SHH11337.1};
OS   Fibrobacter sp. UWCM.
OC   Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=1896208 {ECO:0000313|EMBL:SHH11337.1, ECO:0000313|Proteomes:UP000184289};
RN   [1] {ECO:0000313|EMBL:SHH11337.1, ECO:0000313|Proteomes:UP000184289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWCM {ECO:0000313|EMBL:SHH11337.1,
RC   ECO:0000313|Proteomes:UP000184289};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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       ECO:0000256|HAMAP-Rule:MF_01013}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_01013};
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, ECO:0000256|HAMAP-Rule:MF_01013}.
CC   -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|ARBA:ARBA00011152,
CC       ECO:0000256|HAMAP-Rule:MF_01013}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01013}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family.
CC       {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|HAMAP-Rule:MF_01013,
CC       ECO:0000256|RuleBase:RU003657}.
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DR   EMBL; FQWR01000009; SHH11337.1; -; Genomic_DNA.
DR   RefSeq; WP_073114596.1; NZ_FQWR01000009.1.
DR   AlphaFoldDB; A0A1M5QB11; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000184289; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04731; HisF; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01013; HisF; 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, ECO:0000256|HAMAP-
KW   Rule:MF_01013}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01013};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_01013};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01013}.
FT   ACT_SITE        11
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
SQ   SEQUENCE   263 AA;  28212 MW;  C8638D73C3856E1C CRC64;
     MLTKRLIVCL DVRNRKVTKG VKFKGNIDIG DPVEMGAQYS ADGVDELVFY DITASAENRP
     CDMEMIRQIA KRVFIPFAVG GGIRNLDDMH EALLAGAEKV SVNSLAVLHP EIIADGAKAF
     GRQCVVLGMD AKFLGVSDKF KSGYEVYIRG GRQAMGIDAV EWAKKAEDLG VGEICLNAID
     TDGVRNGYEL NITDQVARAV QVPVIASGGA GTPAHIVDLF RKTAADAALV ASMVHFGDYT
     VPGIKKEMLA AGIPVRKKMN GEV
//
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