ID HIS6_STRMU Reviewed; 251 AA.
AC Q8DTR3;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
DE EC=4.3.2.10 {ECO:0000255|HAMAP-Rule:MF_01013};
DE AltName: Full=IGP synthase cyclase subunit {ECO:0000255|HAMAP-Rule:MF_01013};
DE AltName: Full=IGP synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
DE AltName: Full=ImGP synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
DE Short=IGPS subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
GN Name=hisF {ECO:0000255|HAMAP-Rule:MF_01013}; OrderedLocusNames=SMU_1264;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01013}.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000255|HAMAP-
CC Rule:MF_01013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01013}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000255|HAMAP-
CC Rule:MF_01013}.
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DR EMBL; AE014133; AAN58946.1; -; Genomic_DNA.
DR RefSeq; NP_721640.1; NC_004350.2.
DR RefSeq; WP_002263180.1; NC_004350.2.
DR AlphaFoldDB; Q8DTR3; -.
DR SMR; Q8DTR3; -.
DR STRING; 210007.SMU_1264; -.
DR KEGG; smu:SMU_1264; -.
DR PATRIC; fig|210007.7.peg.1133; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_9; -.
DR OrthoDB; 9781903at2; -.
DR PhylomeDB; Q8DTR3; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000002512; 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; Cytoplasm; Histidine biosynthesis; Lyase;
KW Reference proteome.
FT CHAIN 1..251
FT /note="Imidazole glycerol phosphate synthase subunit HisF"
FT /id="PRO_0000142241"
FT ACT_SITE 11
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01013"
FT ACT_SITE 130
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01013"
SQ SEQUENCE 251 AA; 26874 MW; 1C27D132D16BFBEA CRC64;
MLKKRIIPCL DVKDGRVVKG VNFVNLTDVG DPVDAARAYY EAGCDELVFL DITATSDNRE
TTVDMVRHVA DQVFIPFTVG GGIRSVDDMN KMLKAGADKV AVNSSAIANP QLIKDCAEKF
GSQCVVVAID ARKEADDSWH VYVAGGRKDT GIDLLAWVKE AVQLGAGEIL LTSMDKDGTK
SGFDLDMLNA VAQLADIPII ASGGAGNMEH MVEIFEKTPA TGALAASIFH YGEVSIADTK
KAMKEHGIEV R
//
