HIS6_PYRFU
ID HIS6_PYRFU Reviewed; 251 AA.
AC P58800;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF;
DE EC=4.3.2.10;
DE AltName: Full=IGP synthase cyclase subunit;
DE AltName: Full=IGP synthase subunit HisF;
DE AltName: Full=ImGP synthase subunit HisF;
DE Short=IGPS subunit HisF;
GN Name=hisF; OrderedLocusNames=PF1663;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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 (By similarity). {ECO:0000250}.
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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL81787.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE009950; AAL81787.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_014835588.1; NZ_CP023154.1.
DR AlphaFoldDB; P58800; -.
DR SMR; P58800; -.
DR STRING; 186497.PF1663; -.
DR EnsemblBacteria; AAL81787; AAL81787; PF1663.
DR GeneID; 41713491; -.
DR KEGG; pfu:PF1663; -.
DR PATRIC; fig|186497.12.peg.1729; -.
DR eggNOG; arCOG00617; Archaea.
DR HOGENOM; CLU_048577_4_0_2; -.
DR OMA; IFHYKET; -.
DR OrthoDB; 57066at2157; -.
DR PhylomeDB; P58800; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000001013; 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; -; 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; Cytoplasm; Histidine biosynthesis; Lyase;
KW Reference proteome.
FT CHAIN 1..251
FT /note="Imidazole glycerol phosphate synthase subunit HisF"
FT /id="PRO_0000142287"
FT ACT_SITE 11
FT /evidence="ECO:0000255"
FT ACT_SITE 130
FT /evidence="ECO:0000255"
SQ SEQUENCE 251 AA; 27653 MW; 1BD897DCE72B0D94 CRC64;
MLARRIIAAL DIKDGRVVKG IKFKNIRDAG DPIELAKRYE SEGIDEIVFL DITASYEKRK
ILLDLVERVA EEIYVPFTVG GGIRTVEEAR EIIRRGADKI FINTAAVENP SLIKEIADLI
GSANLVVAID AKWNGKFWEV YTHGGRKPRG MDAVEWAKRV EELGAGEILL TSMDTDGTKQ
GFDIPLTKAV VDAVNIPVIA SGGAGKPEHF LEVFRIGSDA ALAASIFHYG EYTVRELKMF
LAKNGIPVRL D