ID   A0A3R7U953_9FLAO        Unreviewed;       252 AA.
AC   A0A3R7U953;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   28-JUN-2023, entry version 15.
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   ECO:0000313|EMBL:RPG55716.1};
GN   ORFNames=CBD95_005625 {ECO:0000313|EMBL:RPG55716.1};
OS   Flavobacteriales bacterium TMED235.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=1986726 {ECO:0000313|EMBL:RPG55716.1, ECO:0000313|Proteomes:UP000196715};
RN   [1] {ECO:0000313|EMBL:RPG55716.1, ECO:0000313|Proteomes:UP000196715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED235 {ECO:0000313|EMBL:RPG55716.1};
RX   PubMed=28713657; DOI=10.7717/peerj.3558;
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 metagenome-assembled genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   PeerJ 5:e3558-e3558(2017).
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}.
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:RPG55716.1}.
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; NHKG02000084; RPG55716.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R7U953; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000196715; 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   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.
DR   TIGRFAMs; TIGR00735; hisF; 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|HAMAP-Rule:MF_01013, ECO:0000313|EMBL:RPG55716.1}.
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   252 AA;  27279 MW;  827CE67B850A098B CRC64;
     MLKIRIIPCL DVKNGRVVKG INFKNLKDAG DPVLSAQAYD ELGADEICFL DIAATLENRD
     VTVNLVRKTA EKCFIPITVG GGIRTIEDIR HLLLNGADKV SFNSAAIRDP DIISTAANKF
     GSQCIVVAID AKKTKNDKWE IFSHGGTKET GIEAISFAKD MQERGAGEIL LTSMDKDGTK
     DGYDIELTKL ISDSLNIPII ASGGAGKLEH FKSVLEKGKA SAILAASIFH FGEISIKQVK
     SYLRSEGIPV RM
//