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Database: UniProt/TrEMBL
Entry: G9A4Z5_RHIFH
LinkDB: G9A4Z5_RHIFH
Original site: G9A4Z5_RHIFH 
ID   G9A4Z5_RHIFH            Unreviewed;       150 AA.
AC   G9A4Z5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   28-FEB-2018, entry version 40.
DE   RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00976554};
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:SAAS00976537};
GN   Name=hisI {ECO:0000256|HAMAP-Rule:MF_01021,
GN   ECO:0000313|EMBL:CCE95639.1};
GN   OrderedLocusNames=SFHH103_01141 {ECO:0000313|EMBL:CCE95639.1};
OS   Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE95639.1, ECO:0000313|Proteomes:UP000007735};
RN   [1] {ECO:0000313|EMBL:CCE95639.1, ECO:0000313|Proteomes:UP000007735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH103 {ECO:0000313|EMBL:CCE95639.1,
RC   ECO:0000313|Proteomes:UP000007735};
RX   PubMed=22374952; DOI=10.1128/JB.06729-11;
RA   Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J.,
RA   Margaret I., Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S.,
RA   Szczepanowski R., Vinardell J.M., Zehner S., Gottfert M.;
RT   "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL   J. Bacteriol. 194:1617-1618(2012).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of
CC       phosphoribosyl-AMP. {ECO:0000256|HAMAP-Rule:MF_01021,
CC       ECO:0000256|SAAS:SAAS00976573}.
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:SAAS00976579}.
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:SAAS00976563}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01021,
CC       ECO:0000256|SAAS:SAAS00976534}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021,
CC       ECO:0000256|SAAS:SAAS00976539}.
CC   -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000256|HAMAP-
CC       Rule:MF_01021, ECO:0000256|SAAS:SAAS00976567}.
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DR   EMBL; HE616890; CCE95639.1; -; Genomic_DNA.
DR   RefSeq; WP_014328118.1; NC_016812.1.
DR   STRING; 1117943.SFHH103_01141; -.
DR   GeneID; 34334625; -.
DR   KEGG; sfh:SFHH103_01141; -.
DR   PATRIC; fig|380.5.peg.1215; -.
DR   eggNOG; ENOG4105K8F; Bacteria.
DR   eggNOG; COG0139; LUCA.
DR   KO; K01496; -.
DR   OMA; TGYRSCF; -.
DR   OrthoDB; POG091H050E; -.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000007735; 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   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 {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00976560};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007735};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00976532};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00976556};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00976548, ECO:0000313|EMBL:CCE95639.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00976550};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00976576};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00976542}.
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;  B349BAB01C0BD2EA CRC64;
     MALTFVAPSK DKAELETGSA FTPRFDEKGL VTAVVTDARD GELLMVAHMN AEALALTIET
     GIAHYYSRSR DSLWKKGESS GNVQTVQEIR TDCDQDAVWL KVTVAGHDAT CHTGRRSCFY
     RAVGVENGKA RVTITDEHRH FDPAQIYAEK
//
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