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HIS3_BURM1
ID   HIS3_BURM1              Reviewed;         138 AA.
AC   Q845U6; A9AE08;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 106.
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=Bmul_0335, BMULJ_02919;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12754231; DOI=10.1128/jb.185.11.3333-3343.2003;
RA   Komatsu H., Imura Y., Ohori A., Nagata Y., Tsuda M.;
RT   "Distribution and organization of auxotrophic genes on the multichromosomal
RT   genome of Burkholderia multivorans ATCC 17616.";
RL   J. Bacteriol. 185:3333-3343(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) 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-beta-
CC         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-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-Rule:MF_01021};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       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}.
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DR   EMBL; AB091436; BAC65277.1; -; Genomic_DNA.
DR   EMBL; CP000868; ABX14030.1; -; Genomic_DNA.
DR   EMBL; AP009385; BAG44804.1; -; Genomic_DNA.
DR   RefSeq; WP_012212591.1; NC_010804.1.
DR   AlphaFoldDB; Q845U6; -.
DR   SMR; Q845U6; -.
DR   STRING; 395019.Bmul_0335; -.
DR   EnsemblBacteria; BAG44804; BAG44804; BMULJ_02919.
DR   KEGG; bmj:BMULJ_02919; -.
DR   KEGG; bmu:Bmul_0335; -.
DR   eggNOG; COG0139; Bacteria.
DR   HOGENOM; CLU_048577_5_0_4; -.
DR   OMA; TGYRSCF; -.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000008815; Chromosome 1.
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; 3.10.20.810; -; 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   SUPFAM; SSF141734; SSF141734; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Hydrolase;
KW   Magnesium; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..138
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT                   /id="PRO_0000136468"
FT   BINDING         84
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT   CONFLICT        51
FT                   /note="E -> D (in Ref. 1; BAC65277)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   138 AA;  15883 MW;  354657D0CB8D0861 CRC64;
     MNTETKPLPA WLDKVRWDDN GLVPVIAQEA STNDVLMFAW MNREALAKTI ETQRAVYYSR
     SRKRLWFKGE ESGHVQHVHE VRLDCDEDVV LLKVEQVSGI ACHTGRHSCF FQKFEGTVDA
     GDWVAVDPVL KDPEHIYK
 
 
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