(data stored in ACNUC29543 zone)

SWISSPROT: A5GRH3_SYNR3

ID   A5GRH3_SYNR3            Unreviewed;       278 AA.
AC   A5GRH3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 80.
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   ECO:0000313|EMBL:CAK27482.1};
GN   OrderedLocusNames=SynRCC307_0579 {ECO:0000313|EMBL:CAK27482.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27482.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27482.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-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:0000256|HAMAP-
CC       Rule:MF_01013, ECO:0000256|SAAS:SAAS01090838}.
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:0000256|HAMAP-Rule:MF_01013,
CC         ECO:0000256|SAAS:SAAS01124585};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01013, ECO:0000256|SAAS:SAAS01090813}.
CC   -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|HAMAP-
CC       Rule:MF_01013, ECO:0000256|SAAS:SAAS01090811}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01013,
CC       ECO:0000256|SAAS:SAAS01090833}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000256|HAMAP-
CC       Rule:MF_01013, ECO:0000256|RuleBase:RU003657,
CC       ECO:0000256|SAAS:SAAS01090835}.
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DR   EMBL; CT978603; CAK27482.1; -; Genomic_DNA.
DR   STRING; 316278.SynRCC307_0579; -.
DR   EnsemblBacteria; CAK27482; CAK27482; SynRCC307_0579.
DR   KEGG; syr:SynRCC307_0579; -.
DR   eggNOG; ENOG4105C0S; Bacteria.
DR   eggNOG; COG0107; LUCA.
DR   HOGENOM; HOG000224612; -.
DR   KO; K02500; -.
DR   OMA; KRIVPCL; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000001115; 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; A5GRH3.
DR   SWISS-2DPAGE; A5GRH3.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01013,
KW   ECO:0000256|RuleBase:RU003657, ECO:0000256|SAAS:SAAS01090809};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01013,
KW   ECO:0000256|SAAS:SAAS01090827};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01013,
KW   ECO:0000256|RuleBase:RU003657, ECO:0000256|SAAS:SAAS01090822};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01013, ECO:0000256|SAAS:SAAS01090814,
KW   ECO:0000313|EMBL:CAK27482.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115}.
FT   ACT_SITE     33     33       {ECO:0000256|HAMAP-Rule:MF_01013}.
FT   ACT_SITE    152    152       {ECO:0000256|HAMAP-Rule:MF_01013}.
SQ   SEQUENCE   278 AA;  28562 MW;  05DD3182DD36E659 CRC64;
     MLTGFRGNLT SAISFLCAAG AAVVAKRIIP CLDMAAGRVV KGVNFVGLRD AGDPVELACR
     YDAAGADELV FLDIAATHQG RETLVELVER TASQLFIPFT VGGGIRSLEG ITALLRAGAD
     KVSLNSSAVK DPELIRAGAR QFGAQCIVVA IDARRGAGGG WDVYVKGGRE NTGLDAIAWA
     QQVVECGAGE LLLTSMDGDG TQKGYDLELT AAIADAVSVP VIASGGAGSL DHIAEVLEST
     GAAAALLASL LHDGVLTVEQ IKADLQRRGV PVRPLVDA
//

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