(data stored in ACNUC7421 zone)
SWISSPROT: HIS3_PSEU2
ID HIS3_PSEU2 Reviewed; 130 AA.
AC Q4ZZG6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 08-MAY-2019, entry version 75.
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=Psyr_0386;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae
RT pv. syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY35456.1; -; Genomic_DNA.
DR RefSeq; WP_003403068.1; NC_007005.1.
DR RefSeq; YP_233494.1; NC_007005.1.
DR SMR; Q4ZZG6; -.
DR STRING; 205918.Psyr_0386; -.
DR EnsemblBacteria; AAY35456; AAY35456; Psyr_0386.
DR GeneID; 3365862; -.
DR KEGG; psb:Psyr_0386; -.
DR PATRIC; fig|205918.7.peg.399; -.
DR eggNOG; ENOG4105K8F; Bacteria.
DR eggNOG; COG0139; LUCA.
DR HOGENOM; HOG000277504; -.
DR KO; K01496; -.
DR OMA; TGYRSCF; -.
DR BioCyc; PSYR205918:G1G4J-387-MONOMER; -.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000000426; 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;
DR PRODOM; Q4ZZG6.
DR SWISS-2DPAGE; Q4ZZG6.
KW Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW Histidine biosynthesis; Hydrolase; Magnesium; Metal-binding; Zinc.
FT CHAIN 1 130 Phosphoribosyl-AMP cyclohydrolase.
FT /FTId=PRO_0000229838.
FT METAL 77 77 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_01021}.
FT METAL 78 78 Zinc; shared with dimeric partner.
FT {ECO:0000255|HAMAP-Rule:MF_01021}.
FT METAL 79 79 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_01021}.
FT METAL 81 81 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_01021}.
FT METAL 95 95 Zinc; shared with dimeric partner.
FT {ECO:0000255|HAMAP-Rule:MF_01021}.
FT METAL 102 102 Zinc; shared with dimeric partner.
FT {ECO:0000255|HAMAP-Rule:MF_01021}.
SQ SEQUENCE 130 AA; 14892 MW; 15BE6CF461B371D8 CRC64;
MKDWLDEIHW NSDGLVPAIA QDHKTGRVLM MAWMNREALS LTAAENRAIY WSRSRGKLWR
KGEESGHVQK LHELRLDCDA DVIILMVEQI GGIACHTGRE SCFYRVYEKS GWKTVDPVLK
DPDAIYPAGH
//
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