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Database: UniProt/SWISS-PROT
Entry: HIS3_RHIEC
LinkDB: HIS3_RHIEC
Original site: HIS3_RHIEC 
ID   HIS3_RHIEC              Reviewed;         150 AA.
AC   Q2K853;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   20-JUN-2018, entry version 73.
DE   RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01021};
DE            Short=PRA-CH {ECO:0000255|HAMAP-Rule:MF_01021};
DE            EC=3.5.4.19 {ECO:0000255|HAMAP-Rule:MF_01021};
GN   Name=hisI {ECO:0000255|HAMAP-Rule:MF_01021};
GN   OrderedLocusNames=RHE_CH02202;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic
RT   redundancy in seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of
CC       phosphoribosyl-AMP. {ECO:0000255|HAMAP-Rule:MF_01021}.
CC   -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-AMP + H(2)O = 1-
CC       (5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-
CC       ribosylamino)methylideneamino)imidazole-4-carboxamide.
CC       {ECO:0000255|HAMAP-Rule:MF_01021}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01021};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01021};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01021};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01021};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01021}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01021}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01021}.
CC   -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000255|HAMAP-
CC       Rule:MF_01021}.
DR   EMBL; CP000133; ABC90983.1; -; Genomic_DNA.
DR   RefSeq; WP_011425464.1; NC_007761.1.
DR   SMR; Q2K853; -.
DR   STRING; 347834.RHE_CH02202; -.
DR   PRIDE; Q2K853; -.
DR   EnsemblBacteria; ABC90983; ABC90983; RHE_CH02202.
DR   GeneID; 24300754; -.
DR   KEGG; ret:RHE_CH02202; -.
DR   eggNOG; ENOG4105K8F; Bacteria.
DR   eggNOG; COG0139; LUCA.
DR   HOGENOM; HOG000277504; -.
DR   KO; K01496; -.
DR   OMA; TGYRSCF; -.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000001936; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.10.20.400; -; 1.
DR   HAMAP; MF_01021; HisI; 1.
DR   InterPro; IPR026660; PRA-CH.
DR   InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR   InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR   Pfam; PF01502; PRA-CH; 1.
DR   ProDom; PD002610; PRA_CycHdrlase; 1.
DR   SUPFAM; SSF141734; SSF141734; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Hydrolase; Magnesium; Metal-binding; Zinc.
FT   CHAIN         1    150       Phosphoribosyl-AMP cyclohydrolase.
FT                                /FTId=PRO_0000319707.
FT   METAL        93     93       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01021}.
FT   METAL        94     94       Zinc; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01021}.
FT   METAL        95     95       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01021}.
FT   METAL        97     97       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01021}.
FT   METAL       112    112       Zinc; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01021}.
FT   METAL       119    119       Zinc; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01021}.
SQ   SEQUENCE   150 AA;  16703 MW;  C3815FF8E562160B CRC64;
     MGQLIFNQPS EDKSALEDAG DFTPRFDDRG LITAVVADAG DGELLMVAHM NAQALALTIQ
     TGTAHYFSRS RGKIWKKGET SGNLQTVKEI RTDCDQDAIW LKVEVAGHDA TCHTGRRSCF
     YRTVTLREGK PMLDIVDDER HFDPQDVYGK
//
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