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Database: UniProt/TrEMBL
Entry: A0A120KH11_RHIRD
LinkDB: A0A120KH11_RHIRD
Original site: A0A120KH11_RHIRD 
ID   A0A120KH11_RHIRD        Unreviewed;       150 AA.
AC   A0A120KH11;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
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   ORFNames=AWN88_13690 {ECO:0000313|EMBL:AMD59325.1};
OS   Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS   radiobacter).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=358 {ECO:0000313|EMBL:AMD59325.1, ECO:0000313|Proteomes:UP000068966};
RN   [1] {ECO:0000313|EMBL:AMD59325.1, ECO:0000313|Proteomes:UP000068966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S33 {ECO:0000313|EMBL:AMD59325.1,
RC   ECO:0000313|Proteomes:UP000068966};
RA   Wang S., Yu W., Li H., Huang H.;
RT   "Complete genome sequence of Agrobacterium tumefaciens strain S33.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; CP014260; AMD59325.1; -; Genomic_DNA.
DR   RefSeq; WP_006698834.1; NZ_CP014260.1.
DR   EnsemblBacteria; AMD59325; AMD59325; AWN88_13690.
DR   KEGG; ata:AWN88_13690; -.
DR   PATRIC; fig|358.63.peg.4676; -.
DR   KO; K01496; -.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000068966; Chromosome linear.
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:UP000068966};
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:AMD59325.1};
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;  16423 MW;  E5864AEF9321598C CRC64;
     MSIPFPSAPA DKEALENAGL FSPKFDAHGL VTAVVTDARD GELLMVAHMN AQALSLTLET
     GIAHYYSRSR DKIWKKGETS GNLQTVKEFR TDCDQDAVWL KVSVAGHDAT CHTGRRSCFY
     RTVELADGQA VTKITDDTRH FDPATTYSGT
//
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