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Database: UniProt/SWISS-PROT
Entry: HIS3_RHILO
LinkDB: HIS3_RHILO
Original site: HIS3_RHILO 
ID   HIS3_RHILO              Reviewed;         153 AA.
AC   Q98LQ5;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   05-DEC-2018, entry version 84.
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=mlr0923;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of
CC       phosphoribosyl-AMP. {ECO:0000255|HAMAP-Rule:MF_01021}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-
CC         beta-D-ribosyl)-5-[(5-phospho-beta-D-
CC         ribosylamino)methylideneamino]imidazole-4-carboxamide;
CC         Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435,
CC         ChEBI:CHEBI:59457; EC=3.5.4.19; Evidence={ECO:0000255|HAMAP-
CC         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; BA000012; BAB48408.1; -; Genomic_DNA.
DR   RefSeq; WP_010909762.1; NC_002678.2.
DR   ProteinModelPortal; Q98LQ5; -.
DR   SMR; Q98LQ5; -.
DR   STRING; 266835.mlr0923; -.
DR   EnsemblBacteria; BAB48408; BAB48408; BAB48408.
DR   KEGG; mlo:mlr0923; -.
DR   eggNOG; ENOG4105K8F; Bacteria.
DR   eggNOG; COG0139; LUCA.
DR   HOGENOM; HOG000277504; -.
DR   KO; K01496; -.
DR   OMA; MLLMVAH; -.
DR   OrthoDB; POG091H050E; -.
DR   BioCyc; MLOT266835:G1G20-752-MONOMER; -.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000000552; 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; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN         1    153       Phosphoribosyl-AMP cyclohydrolase.
FT                                /FTId=PRO_0000136495.
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   153 AA;  16821 MW;  4A44E3188B90F239 CRC64;
     MSALGFPKTP SDKKALEEGA VFSPRFDPAG LVTVVVTDAE DGMLLMVAHM NAQALALTLE
     TGIAHYWSRS RNALWKKGET SGNFQHVVEM RTDCDQDALW LRVKVLGHDA TCHTGRRSCF
     YRTVGLVDGK GTLVDDGSKP LFDAEFTYRK PSS
//
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