HIS6_HELMO
ID HIS6_HELMO Reviewed; 261 AA.
AC Q8GDQ6;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 62.
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};
DE Flags: Fragment;
GN Name=hisF {ECO:0000255|HAMAP-Rule:MF_01013};
OS Heliobacterium mobile (Heliobacillus mobilis).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC Heliobacterium.
OX NCBI_TaxID=28064;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12446909; DOI=10.1126/science.1075558;
RA Raymond J., Zhaxybayeva O., Gogarten J.P., Gerdes S.Y., Blankenship R.E.;
RT "Whole-genome analysis of photosynthetic prokaryotes.";
RL Science 298:1616-1620(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; AY142920; AAN87524.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GDQ6; -.
DR SMR; Q8GDQ6; -.
DR UniPathway; UPA00031; UER00010.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
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.
FT CHAIN 1..>261
FT /note="Imidazole glycerol phosphate synthase subunit HisF"
FT /id="PRO_0000142166"
FT ACT_SITE 11
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01013"
FT ACT_SITE 130
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01013"
FT NON_TER 261
SQ SEQUENCE 261 AA; 28553 MW; 69B03C9560582690 CRC64;
MLAKRIIPCL DVHGGRVVKG TNFVNLRDAG DPVELAAVYD KEGADELVFL DITASSDGRA
IMLDVVRRTA EEVFIPFTVG GGLRTVEDIR EMLKAGADKI SLNTSAVQTP QLIGDSAWKF
GSQCIVVAID ARRRRDEEGR LLEGWEVYTH GGRKPTGIDV LEWARKVEEL GCGEILLTSM
DKDGTKDGYD IPLTRAVSEA VKIPVIASGG VGNLEHICEG LTAGKADAAL AASIFHYKEY
TIRETKEYLR GKGVHVRKWR D
