(data stored in ACNUC7421 zone)

SWISSPROT: HIS6_SYNFM

ID   HIS6_SYNFM              Reviewed;         259 AA.
AC   A0LFI1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 68.
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};
GN   OrderedLocusNames=Sfum_0483;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) 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:0000255|HAMAP-
CC       Rule:MF_01013}.
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:0000255|HAMAP-Rule:MF_01013};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine 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}.
DR   EMBL; CP000478; ABK16183.1; -; Genomic_DNA.
DR   RefSeq; WP_011697356.1; NC_008554.1.
DR   SMR; A0LFI1; -.
DR   STRING; 335543.Sfum_0483; -.
DR   EnsemblBacteria; ABK16183; ABK16183; Sfum_0483.
DR   KEGG; sfu:Sfum_0483; -.
DR   eggNOG; ENOG4105C0S; Bacteria.
DR   eggNOG; COG0107; LUCA.
DR   HOGENOM; HOG000224612; -.
DR   KO; K02500; -.
DR   OMA; KRIVPCL; -.
DR   OrthoDB; 1522718at2; -.
DR   BioCyc; SFUM335543:G1G7I-494-MONOMER; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000001784; 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;
DR   PRODOM; A0LFI1.
DR   SWISS-2DPAGE; A0LFI1.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Lyase; Reference proteome.
FT   CHAIN         1    259       Imidazole glycerol phosphate synthase
FT                                subunit HisF.
FT                                /FTId=PRO_1000063163.
FT   ACT_SITE     11     11       {ECO:0000255|HAMAP-Rule:MF_01013}.
FT   ACT_SITE    130    130       {ECO:0000255|HAMAP-Rule:MF_01013}.
SQ   SEQUENCE   259 AA;  28237 MW;  A7C7BE1F4D6A3227 CRC64;
     MLSKRIIPCL DVRDGRTTKG IKFRNNVDIG DPVDMGRFYY EEGADEIVFY DITASSDRRG
     IMLDVVKRVA ETIFIPFSVG GGIRTLEDMR DVLLAGAEKV SVNSAAVLNP DIISQGAEAF
     GSQCIVLGMD VKHVAPSTRI PSGYEIVING GRTTTGFDAL WWALEAERLG AGEICLNSID
     ADGTRDGYEL RLTRLISTSV RIPVIASGGA GTPNHLADVL KQGRADAALI ASMVHYGTYS
     IRRIKQFLDD NGIRVRKTW
//

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