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Database: UniProt/SWISS-PROT
Entry: HIS3_SINFN
LinkDB: HIS3_SINFN
Original site: HIS3_SINFN 
ID   HIS3_SINFN              Reviewed;         152 AA.
AC   C3MB44;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 47.
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=NGR_c12560;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP25037.1; -; Genomic_DNA.
DR   RefSeq; WP_012707814.1; NC_012587.1.
DR   RefSeq; YP_002825790.1; NC_012587.1.
DR   SMR; C3MB44; -.
DR   STRING; 394.NGR_c12560; -.
DR   EnsemblBacteria; ACP25037; ACP25037; NGR_c12560.
DR   GeneID; 7793129; -.
DR   KEGG; rhi:NGR_c12560; -.
DR   PATRIC; fig|394.7.peg.4074; -.
DR   eggNOG; ENOG4105K8F; Bacteria.
DR   eggNOG; COG0139; LUCA.
DR   HOGENOM; HOG000277504; -.
DR   KO; K01496; -.
DR   OMA; NCEQNSL; -.
DR   OrthoDB; POG091H050E; -.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000001054; 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   HAMAP; MF_01021; HisI; 1.
DR   InterPro; IPR026660; PRA-CH.
DR   InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR   Pfam; PF01502; PRA-CH; 1.
DR   ProDom; PD002610; PRA_CycHdrlase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN         1    152       Phosphoribosyl-AMP cyclohydrolase.
FT                                /FTId=PRO_1000149076.
FT   METAL        92     92       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01021}.
FT   METAL        93     93       Zinc; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01021}.
FT   METAL        94     94       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01021}.
FT   METAL        96     96       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01021}.
FT   METAL       111    111       Zinc; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01021}.
FT   METAL       118    118       Zinc; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01021}.
SQ   SEQUENCE   152 AA;  16798 MW;  9F34D7E02228186F CRC64;
     MTLTFPAPSK DKAELETGPA FTPRFDEKGL VTAVVTDARD GELLMVAHMN AEALALTIET
     GIAHYYSRSR NSLWKKGESS GNTQAVQEIR TDCDQDAIWL KVTVAGHDAT CHTGRRSCFY
     RTVGVENGKA RVTITDEHRH FDPAQIYAEK KG
//
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