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Database: UniProt/SWISS-PROT
Entry: HIS3_BRUMB
LinkDB: HIS3_BRUMB
Original site: HIS3_BRUMB 
ID   HIS3_BRUMB              Reviewed;         139 AA.
AC   C0RJ48;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   05-DEC-2018, entry version 54.
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=BMEA_A1117;
OS   Brucella melitensis biotype 2 (strain ATCC 23457).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=546272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23457;
RA   Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W.,
RA   Lu J., Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M.,
RA   Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA   Munk C., Tapia R., Han C., Detter J.C., Bruce D., Brettin T.S.;
RT   "Brucella melitensis ATCC 23457 whole genome shotgun sequencing
RT   project.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001488; ACO00856.1; -; Genomic_DNA.
DR   RefSeq; WP_002966830.1; NC_012441.1.
DR   ProteinModelPortal; C0RJ48; -.
DR   SMR; C0RJ48; -.
DR   EnsemblBacteria; ACO00856; ACO00856; BMEA_A1117.
DR   GeneID; 29593718; -.
DR   KEGG; bmi:BMEA_A1117; -.
DR   HOGENOM; HOG000277504; -.
DR   KO; K01496; -.
DR   OMA; TGYRSCF; -.
DR   BioCyc; BMEL546272:G1GV6-1113-MONOMER; -.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000001748; Chromosome I.
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; Zinc.
FT   CHAIN         1    139       Phosphoribosyl-AMP cyclohydrolase.
FT                                /FTId=PRO_1000149066.
FT   METAL        91     91       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01021}.
FT   METAL        92     92       Zinc; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01021}.
FT   METAL        93     93       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01021}.
FT   METAL        95     95       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01021}.
FT   METAL       110    110       Zinc; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01021}.
FT   METAL       117    117       Zinc; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01021}.
SQ   SEQUENCE   139 AA;  15280 MW;  A150156774790556 CRC64;
     MSIFPAQPSD KKAVEEGAAF MPRFDASGLI TAIVTDARDG ELLMVAHMNE EALRLTLETG
     IAHYWSRSRK TLWKKGETSG NLQSVVELRT DCDQDALWLK VHVAGDGPTC HTGRRSCFYR
     QVVSSGGKVA LTMASDHDQ
//
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