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Database: UniProt
Entry: G0EH83_PYRF1
LinkDB: G0EH83_PYRF1
Original site: G0EH83_PYRF1 
ID   G0EH83_PYRF1            Unreviewed;       252 AA.
AC   G0EH83;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
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   OrderedLocusNames=Pyrfu_1449 {ECO:0000313|EMBL:AEM39307.1};
OS   Pyrolobus fumarii (strain DSM 11204 / 1A).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Pyrolobus.
OX   NCBI_TaxID=694429 {ECO:0000313|EMBL:AEM39307.1, ECO:0000313|Proteomes:UP000001037};
RN   [1] {ECO:0000313|EMBL:AEM39307.1, ECO:0000313|Proteomes:UP000001037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11204 / 1A {ECO:0000313|Proteomes:UP000001037};
RX   PubMed=21886865;
RA   Anderson I., Goker M., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA   Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Huntemann M.,
RA   Liolios K., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Huber H.,
RA   Yasawong M., Rohde M., Spring S., Abt B., Sikorski J., Wirth R.,
RA   Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of the hyperthermophilic chemolithoautotroph
RT   Pyrolobus fumarii type strain (1A).";
RL   Stand. Genomic Sci. 4:381-392(2011).
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|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|HAMAP-
CC       Rule:MF_01013}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01013}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000256|HAMAP-
CC       Rule:MF_01013, ECO:0000256|RuleBase:RU003657}.
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DR   EMBL; CP002838; AEM39307.1; -; Genomic_DNA.
DR   RefSeq; WP_014026984.1; NC_015931.1.
DR   AlphaFoldDB; G0EH83; -.
DR   STRING; 694429.Pyrfu_1449; -.
DR   GeneID; 11138636; -.
DR   KEGG; pfm:Pyrfu_1449; -.
DR   eggNOG; arCOG00617; Archaea.
DR   HOGENOM; CLU_048577_4_0_2; -.
DR   InParanoid; G0EH83; -.
DR   OMA; IFHYKET; -.
DR   OrthoDB; 6261at2157; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000001037; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001037}.
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;  27141 MW;  8D7D326DB9126F49 CRC64;
     MEAIRIIPCL DVKDGRVVKG VRFENLRDAG DPVELAARYE EEGADEIVFL DISATPEGRE
     TLINVVRDTA SVLSIPLTVG GGVRSLKDFE KLMDSGADKV SINTAAVRNP DLITQAAREY
     GSQAVVVAID AKRVGPQKWE VYVSAGKVPT GLDAVEWAIE AVRRGAGEIL LTSIDMDGTK
     QGYDIQLTRA IAEKVPVPVI ASGGAGKLEH FWEAVVYGKA SAVLAASVFH FRILTIRQVK
     DYLASKGIPV RL
//
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