PURNU_BACTN
ID PURNU_BACTN Reviewed; 270 AA.
AC Q89ZI8;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Purine nucleoside phosphorylase BT_4389;
DE EC=2.4.2.1 {ECO:0000250|UniProtKB:P84138};
DE AltName: Full=Adenosine deaminase BT_4389;
DE EC=3.5.4.4 {ECO:0000250|UniProtKB:P84138};
DE AltName: Full=S-methyl-5'-thioadenosine phosphorylase BT_4389;
DE EC=2.4.2.28 {ECO:0000250|UniProtKB:P84138};
GN OrderedLocusNames=BT_4389 {ECO:0000312|EMBL:AAO79494.1};
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=16740638; DOI=10.1074/jbc.m600577200;
RA Beloqui A., Pita M., Polaina J., Martinez-Arias A., Golyshina O.V.,
RA Zumarraga M., Yakimov M.M., Garcia-Arellano H., Alcalde M., Fernandez V.M.,
RA Elborough K., Andreu J.M., Ballesteros A., Plou F.J., Timmis K.N.,
RA Ferrer M., Golyshin P.N.;
RT "Novel polyphenol oxidase mined from a metagenome expression library of
RT bovine rumen: biochemical properties, structural analysis, and phylogenetic
RT relationships.";
RL J. Biol. Chem. 281:22933-22942(2006).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.0 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid
CC (at pH 4.5 and 40 degrees Celsius) {ECO:0000269|PubMed:16740638};
CC KM=0.83 uM for syringaldazine (at pH 4.5 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:16740638};
CC Note=kcat is 13000 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-
CC 6-sulfonic acid as substrate. kcat is 33300 min(-1) with
CC syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius).
CC {ECO:0000269|PubMed:16740638};
CC pH dependence:
CC Optimum pH is 4.5-6.0. Maintains 80% activity at pH 4.0-7.5.
CC {ECO:0000269|PubMed:16740638};
CC Temperature dependence:
CC Optimum temperature is 52 degrees Celsius. Maintains more than 80%
CC activity at 55 degrees Celsius. {ECO:0000269|PubMed:16740638};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16740638}.
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; AE015928; AAO79494.1; -; Genomic_DNA.
DR RefSeq; NP_813300.1; NC_004663.1.
DR RefSeq; WP_011109232.1; NC_004663.1.
DR AlphaFoldDB; Q89ZI8; -.
DR SMR; Q89ZI8; -.
DR STRING; 226186.BT_4389; -.
DR PaxDb; Q89ZI8; -.
DR PRIDE; Q89ZI8; -.
DR EnsemblBacteria; AAO79494; AAO79494; BT_4389.
DR GeneID; 60925565; -.
DR KEGG; bth:BT_4389; -.
DR PATRIC; fig|226186.12.peg.4467; -.
DR eggNOG; COG1496; Bacteria.
DR HOGENOM; CLU_065784_0_0_10; -.
DR InParanoid; Q89ZI8; -.
DR OMA; CFADCVP; -.
DR SABIO-RK; Q89ZI8; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Copper; Hydrolase; Metal-binding; Oxidoreductase; Reference proteome;
KW Transferase; Zinc.
FT CHAIN 1..270
FT /note="Purine nucleoside phosphorylase BT_4389"
FT /id="PRO_0000440779"
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 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P84138"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P84138"
SQ SEQUENCE 270 AA; 30118 MW; 0989A7E370C4DC81 CRC64;
MISITKDKRM LGYESLSSYS NISHFVTTRQ GGCSEGNYAS FNCTPYSGDE AEKVRRNQTL
LMEGMSQIPE ELVIPVQTHE TNYLLIGDAY LSASSQQRQE MLHGVDALIT REPGYCLCIS
TADCVPVLVY DKKHGAIAAI HAGWRGTVAY IVRDTLLRME KEFGTSGEDV VACIGPSISL
ASFEVGEEVY EAFQKNGFDM PRISIRKEET GKHHIDLWEA NRMQILAFGV PSGQVELARI
CTYIHHDEFF SARRLGIKSG RILSGIMIHK
