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Database: UniProt/TrEMBL
Entry: A0A0E0UBD3_SINMB
LinkDB: A0A0E0UBD3_SINMB
Original site: A0A0E0UBD3_SINMB 
ID   A0A0E0UBD3_SINMB        Unreviewed;       150 AA.
AC   A0A0E0UBD3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-SEP-2017, entry version 17.
DE   RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00103129};
DE            Short=PRA-CH {ECO:0000256|HAMAP-Rule:MF_01021};
DE            EC=3.5.4.19 {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00391815};
GN   Name=hisI {ECO:0000256|HAMAP-Rule:MF_01021};
GN   OrderedLocusNames=SinmeB_1049 {ECO:0000313|EMBL:AEG03977.1};
OS   Sinorhizobium meliloti (strain BL225C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=698936 {ECO:0000313|EMBL:AEG03977.1, ECO:0000313|Proteomes:UP000008709};
RN   [1] {ECO:0000313|Proteomes:UP000008709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL225C {ECO:0000313|Proteomes:UP000008709};
RX   PubMed=21569405; DOI=10.1186/1471-2164-12-235;
RG   US DOE Joint Genome Institute;
RA   Galardini M., Mengoni A., Brilli M., Pini F., Fioravanti A., Lucas S.,
RA   Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Land M., Hauser L.,
RA   Woyke T., Mikhailova N., Ivanova N., Daligault H., Bruce D.,
RA   Detter C., Tapia R., Han C., Teshima H., Mocali S., Bazzicalupo M.,
RA   Biondi E.G.;
RT   "Exploring the symbiotic pangenome of the nitrogen-fixing bacterium
RT   Sinorhizobium meliloti.";
RL   BMC Genomics 12:235-235(2011).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of
CC       phosphoribosyl-AMP. {ECO:0000256|HAMAP-Rule:MF_01021,
CC       ECO:0000256|SAAS:SAAS00391850}.
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:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00391825}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00391810}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01021,
CC       ECO:0000256|SAAS:SAAS00391880}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021,
CC       ECO:0000256|SAAS:SAAS00006977}.
CC   -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000256|HAMAP-
CC       Rule:MF_01021, ECO:0000256|SAAS:SAAS00578260}.
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DR   EMBL; CP002740; AEG03977.1; -; Genomic_DNA.
DR   RefSeq; WP_003534698.1; NC_017322.1.
DR   ProteinModelPortal; A0A0E0UBD3; -.
DR   SMR; A0A0E0UBD3; -.
DR   EnsemblBacteria; AEG03977; AEG03977; SinmeB_1049.
DR   KEGG; smq:SinmeB_1049; -.
DR   KO; K01496; -.
DR   OMA; TGYRSCF; -.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000008709; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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 {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00103205};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008709};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00006957};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00103201};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00469262, ECO:0000313|EMBL:AEG03977.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00006960};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00006980};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00006961}.
FT   DOMAIN       45    120       PRA-CH. {ECO:0000259|Pfam:PF01502}.
FT   METAL        92     92       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01021}.
FT   METAL        93     93       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01021}.
FT   METAL        94     94       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01021}.
FT   METAL        96     96       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01021}.
FT   METAL       111    111       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01021}.
FT   METAL       118    118       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01021}.
SQ   SEQUENCE   150 AA;  16560 MW;  301D4FE9B60D6E83 CRC64;
     MTLTFASPPQ DKAELESGPA FTPRFDEKGL ITAVVTDARD GELLMVAHMN AEALSLTLET
     GFAHYYSRSR DRLWKKGESS GNLQTVREIR TDCDQDAVWL KVSVAGHDAT CHTGRRSCFY
     RTVGVADGEA KVAITDDHRH FDPAQIYAGN
//
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