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PURNU_HAEIN
ID   PURNU_HAEIN             Reviewed;         244 AA.
AC   P44552;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Purine nucleoside phosphorylase HI_0175;
DE            EC=2.4.2.1 {ECO:0000250|UniProtKB:P84138};
DE   AltName: Full=Adenosine deaminase HI_0175;
DE            EC=3.5.4.4 {ECO:0000250|UniProtKB:P84138};
DE   AltName: Full=S-methyl-5'-thioadenosine phosphorylase HI_0175;
DE            EC=2.4.2.28 {ECO:0000250|UniProtKB:P84138};
GN   OrderedLocusNames=HI_0175;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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}.
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DR   EMBL; L42023; AAC21844.1; -; Genomic_DNA.
DR   PIR; E64144; E64144.
DR   RefSeq; NP_438343.1; NC_000907.1.
DR   RefSeq; WP_005694112.1; NC_000907.1.
DR   AlphaFoldDB; P44552; -.
DR   SMR; P44552; -.
DR   STRING; 71421.HI_0175; -.
DR   EnsemblBacteria; AAC21844; AAC21844; HI_0175.
DR   KEGG; hin:HI_0175; -.
DR   PATRIC; fig|71421.8.peg.179; -.
DR   eggNOG; COG1496; Bacteria.
DR   HOGENOM; CLU_065784_1_1_6; -.
DR   OMA; CFADCVP; -.
DR   PhylomeDB; P44552; -.
DR   BioCyc; HINF71421:G1GJ1-185-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
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; Reference proteome;
KW   Transferase; Zinc.
FT   CHAIN           1..244
FT                   /note="Purine nucleoside phosphorylase HI_0175"
FT                   /id="PRO_0000163164"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P84138"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P84138"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P84138"
SQ   SEQUENCE   244 AA;  27138 MW;  B840AA696571F8E2 CRC64;
     MQAINPNWNV PKNIHAFTTT REGGVSLAPY LSFNLGDHVG DNKSAVKTNR TLLVEKFGLP
     QTPIFLTQTH STRVIQLPYS GQNLEADAVY TNVPNQVCVV MTADCLPVLF TTTSGNEVAA
     THAGWRGLCD GVLEETVKYF QAKPEDIIAW FGPAIGPKAF QVGIDVVEKF VVVDEKAKLA
     FQPDAIEEGK YLSNLYQIAT QRLNNLGITQ IYGGNHCTFN EKEKFFSYRR DNQTGRMASV
     IWFE
 
 
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