(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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