ID   A0A3R7U953_9FLAO        Unreviewed;       252 AA.
AC   A0A3R7U953;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   08-MAY-2019, entry version 2.
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; Bacteroidetes; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=1986726 {ECO:0000313|EMBL:RPG55716.1};
RN   [1] {ECO:0000313|EMBL:RPG55716.1}
RP   NUCLEOTIDE SEQUENCE.
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
RT   resource for marine microbiology.";
RL   PeerJ 5:e3558-e3558(2017).
RN   [2] {ECO:0000313|EMBL:RPG55716.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TMED235 {ECO:0000313|EMBL:RPG55716.1};
RA   Graham E.D., Tully B.J.;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to
CC       IGP, AICAR and glutamate. The HisF subunit catalyzes the
CC       cyclization activity that produces IGP and AICAR from PRFAR using
CC       the ammonia provided by the HisH subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01013, ECO:0000256|SAAS:SAAS01090838}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-
CC         (5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
CC         = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide +
CC         D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-
CC         glutamate; Xref=Rhea:RHEA:24793, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58278, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:58475, ChEBI:CHEBI:58525; EC=4.3.2.10;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01013,
CC         ECO:0000256|SAAS:SAAS01124585};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01013, ECO:0000256|SAAS:SAAS01090813}.
CC   -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|HAMAP-
CC       Rule:MF_01013, ECO:0000256|SAAS:SAAS01090811}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01013,
CC       ECO:0000256|SAAS:SAAS01090833}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000256|HAMAP-
CC       Rule:MF_01013, ECO:0000256|RuleBase:RU003657,
CC       ECO:0000256|SAAS:SAAS01090835}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:RPG55716.1}.
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DR   EMBL; NHKG02000084; RPG55716.1; -; Genomic_DNA.
DR   UniPathway; UPA00031; UER00010.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   CDD; cd04731; HisF; 1.
DR   Gene3D; 3.20.20.70; -; 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   Pfam; PF00977; His_biosynth; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR00735; hisF; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01013,
KW   ECO:0000256|RuleBase:RU003657, ECO:0000256|SAAS:SAAS01090809};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01013,
KW   ECO:0000256|SAAS:SAAS01090827};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01013,
KW   ECO:0000256|RuleBase:RU003657, ECO:0000256|SAAS:SAAS01090822};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01013, ECO:0000256|SAAS:SAAS01090814,
KW   ECO:0000313|EMBL:RPG55716.1}.
FT   ACT_SITE     11     11       {ECO:0000256|HAMAP-Rule:MF_01013}.
FT   ACT_SITE    130    130       {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
//