位置:首页 > 蛋白库 > PURNU_XYLFT
PURNU_XYLFT
ID   PURNU_XYLFT             Reviewed;         260 AA.
AC   Q87AR8;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Purine nucleoside phosphorylase PD_1754;
DE            EC=2.4.2.1 {ECO:0000250|UniProtKB:P84138};
DE   AltName: Full=Adenosine deaminase PD_1754;
DE            EC=3.5.4.4 {ECO:0000250|UniProtKB:P84138};
DE   AltName: Full=S-methyl-5'-thioadenosine phosphorylase PD_1754;
DE            EC=2.4.2.28 {ECO:0000250|UniProtKB:P84138};
GN   OrderedLocusNames=PD_1754;
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=183190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Temecula1 / ATCC 700964;
RX   PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA   Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA   Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA   Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA   Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA   Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA   Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA   Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA   Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA   Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA   Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA   Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's disease
RT   and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(2003).
CC   -!- FUNCTION: Purine nucleoside enzyme that catalyzes the phosphorolysis of
CC       adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and
CC       the respective free bases, adenine and hypoxanthine. Also catalyzes the
CC       phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-
CC       5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase
CC       activity. {ECO:0000250|UniProtKB:P84138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate;
CC         Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC         Evidence={ECO:0000250|UniProtKB:P84138};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27643;
CC         Evidence={ECO:0000250|UniProtKB:P84138};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-
CC         thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:11852,
CC         ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58533; EC=2.4.2.28;
CC         Evidence={ECO:0000250|UniProtKB:P84138};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11853;
CC         Evidence={ECO:0000250|UniProtKB:P84138};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate +
CC         hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368,
CC         ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC         Evidence={ECO:0000250|UniProtKB:P84138};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27647;
CC         Evidence={ECO:0000250|UniProtKB:P84138};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine + H(+) + H2O = inosine + NH4(+);
CC         Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4;
CC         Evidence={ECO:0000250|UniProtKB:P84138};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
CC         Evidence={ECO:0000250|UniProtKB:P84138};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:P33644};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P84138};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q1EIR0}.
CC   -!- SIMILARITY: Belongs to the purine nucleoside phosphorylase YfiH/LACC1
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009442; AAO29588.1; -; Genomic_DNA.
DR   RefSeq; WP_004089660.1; NC_004556.1.
DR   AlphaFoldDB; Q87AR8; -.
DR   SMR; Q87AR8; -.
DR   EnsemblBacteria; AAO29588; AAO29588; PD_1754.
DR   GeneID; 58017279; -.
DR   KEGG; xft:PD_1754; -.
DR   HOGENOM; CLU_065784_1_1_6; -.
DR   OMA; CFADCVP; -.
DR   Proteomes; UP000002516; Chromosome.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:UniProtKB-EC.
DR   CDD; cd16833; YfiH; 1.
DR   Gene3D; 3.60.140.10; -; 1.
DR   InterPro; IPR003730; Cu_polyphenol_OxRdtase.
DR   InterPro; IPR038371; Cu_polyphenol_OxRdtase_sf.
DR   InterPro; IPR011324; Cytotoxic_necrot_fac-like_cat.
DR   PANTHER; PTHR30616; PTHR30616; 1.
DR   Pfam; PF02578; Cu-oxidase_4; 1.
DR   SUPFAM; SSF64438; SSF64438; 1.
DR   TIGRFAMs; TIGR00726; TIGR00726; 1.
PE   3: Inferred from homology;
KW   Copper; Hydrolase; Metal-binding; Oxidoreductase; Transferase; Zinc.
FT   CHAIN           1..260
FT                   /note="Purine nucleoside phosphorylase PD_1754"
FT                   /id="PRO_0000163186"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P84138"
FT   BINDING         120
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P84138"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P84138"
SQ   SEQUENCE   260 AA;  27664 MW;  14EE46C5B34E829A CRC64;
     MGKFPSWVLV ADWPPPPGVM ALSTLRDGPG VSVAPFDRLN LGNCSGVAGD APVCVERNRS
     RLVQMLGLPS VPHWLRQVHG VEVLRVDVLP QSIARVVEPT ADAAVTSVAG AVLVILTADC
     LPVVLAAVDG SEIGVVHAGW RGLADDVLER TVAALRTSPE CLQAWLGPAA GPQAYEVGVD
     VYAAFVERDS GAACAFSVTR PGHWYVDLYA LARQRLMRAG LSAVSIYGGG LCTISDPQRF
     FSHRRDRRSG RFATLAWIGC
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024