PURNU_UNKP
ID PURNU_UNKP Reviewed; 262 AA.
AC Q1EIR0;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Adenosine deaminase RL5;
DE EC=3.5.4.4 {ECO:0000250|UniProtKB:P84138};
DE AltName: Full=Laccase RL5 {ECO:0000303|PubMed:16740638};
DE AltName: Full=Multicopper oxidase RL5 {ECO:0000303|PubMed:16740638};
DE AltName: Full=Polyphenol oxidase {ECO:0000303|PubMed:16740638};
DE EC=1.10.3.- {ECO:0000269|PubMed:16740638};
DE AltName: Full=Purine nucleoside phosphorylase RL5;
DE EC=2.4.2.1 {ECO:0000250|UniProtKB:P84138};
DE AltName: Full=S-methyl-5'-thioadenosine phosphorylase RL5;
DE EC=2.4.2.28 {ECO:0000250|UniProtKB:P84138};
GN Name=rl5 {ECO:0000303|PubMed:16740638, ECO:0000312|EMBL:CAK32504.1};
OS Unknown prokaryotic organism.
OC Bacteria; environmental samples.
OX NCBI_TaxID=2725;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, 3D-STRUCTURE
RP MODELING, AND MUTAGENESIS OF ASN-36; TYR-40; MET-68; HIS-73; CYS-75;
RP ASN-114; CYS-118; HIS-135; CYS-172; CYS-175; HIS-190; HIS-207; HIS-233;
RP CYS-234; CYS-237 AND HIS-239.
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 (By similarity).
CC Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into
CC adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate (By similarity).
CC Also has adenosine deaminase activity (By similarity). Also acts as a
CC multicopper oxidase able to oxidize a wide variety of polyphenols and
CC related compounds in vitro (PubMed:16740638). Displays substrate
CC preference as follows: syringaldazine > 2,6-dimethoxyphenol > veratryl
CC alcohol > guaiacol > tetramethylbenzidine > 4-methoxybenzyl alcohol >
CC 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) >> phenol
CC red > 1-hydroxybenzotriazole (PubMed:16740638). Cannot use 3,4-
CC dimetoxybenzyl alcohol and violuric acid as substrates
CC (PubMed:16740638). As this enzyme is derived from a rumen microbial
CC community, it may have a role in the digestion of complex plant
CC materials such as ryegrass lignin (PubMed:16740638).
CC {ECO:0000250|UniProtKB:P84138, ECO:0000269|PubMed:16740638}.
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 cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:16740638};
CC Note=Binds 4 Cu cations per subunit. {ECO:0000269|PubMed:16740638};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid (at
CC pH 4.5 and 40 degrees Celsius) {ECO:0000269|PubMed:16740638};
CC KM=0.43 uM for syringaldazine (at pH 4.5 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:16740638};
CC KM=0.45 uM for 2,6-dimethoxyphenol (at pH 4.5 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:16740638};
CC Note=kcat is 18 sec(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-
CC sulfonic acid as substrate. kcat is 660 sec(-1) with syringaldazine
CC as substrate. kcat is 1175 sec(-1) with 2,6-dimethoxyphenol as
CC substrate (at pH 4.5 and 40 degrees Celsius).
CC {ECO:0000269|PubMed:16740638};
CC pH dependence:
CC Optimum pH is 4.0-5.0. Activity is very high over a broad pH range
CC from 4.0 to 9.0. Exhibits more than 70% activity at pH 3.5 and 9.5.
CC {ECO:0000269|PubMed:16740638};
CC Temperature dependence:
CC Optimum temperature is about 60 degrees Celsius. Is fully stable at
CC this temperature. {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}.
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DR EMBL; AM269758; CAK32504.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1EIR0; -.
DR SMR; Q1EIR0; -.
DR PRIDE; Q1EIR0; -.
DR SABIO-RK; Q1EIR0; -.
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; Transferase; Zinc.
FT CHAIN 1..262
FT /note="Adenosine deaminase RL5"
FT /id="PRO_0000440780"
FT BINDING 36
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:16740638"
FT BINDING 40
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:16740638"
FT BINDING 68
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:16740638"
FT BINDING 73
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:16740638"
FT BINDING 75
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:16740638"
FT BINDING 114
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:16740638"
FT BINDING 118
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:16740638"
FT BINDING 135
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:16740638"
FT BINDING 172
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:16740638"
FT BINDING 175
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:16740638"
FT BINDING 234
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:16740638"
FT BINDING 237
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:16740638"
FT MUTAGEN 36
FT /note="N->A: Loss of 1.0 of Cu/mol of protein. Loss of
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 40
FT /note="Y->A: Loss of 1.0 of Cu/mol of protein. Loss of
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 68
FT /note="M->A: No effect on Cu content. No effect on
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 73
FT /note="H->A: Loss of 1.0 of Cu/mol of protein. No effect on
FT secondary structure. Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 75
FT /note="C->Q: Loss of 1.0 of Cu/mol of protein. No effect on
FT secondary structure. Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 114
FT /note="N->A: Loss of 1.0 of Cu/mol of protein. Loss of
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 118
FT /note="C->Q: Loss of 1.0 of Cu/mol of protein. No effect on
FT secondary structure. Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 135
FT /note="H->A: Loss of 1.0 of Cu/mol of protein. No effect on
FT secondary structure. Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 172
FT /note="C->Q: Loss of 1.0 of Cu/mol of protein. Loss of
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 175
FT /note="C->Q: Loss of 1.0 of Cu/mol of protein. Loss of
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 190
FT /note="H->A: Binds only 1.0 of Cu/mol of protein. Causes
FT major change in secondary structure. Displays about 10% of
FT wild-type catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 207
FT /note="H->A: Binds only 1.0 of Cu/mol of protein. Causes
FT major change in secondary structure. Displays about 10% of
FT wild-type catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 233
FT /note="H->A: Loss of 1.0 of Cu/mol of protein. No effect on
FT secondary structure. Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 234
FT /note="C->Q: No effect on Cu content. No effect on
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 237
FT /note="C->Q: Loss of 1.0 of Cu/mol of protein. Loss of
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:16740638"
FT MUTAGEN 239
FT /note="H->A: Binds only 1.0 of Cu/mol of protein. Causes
FT major change in secondary structure. Loss of catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:16740638"
SQ SEQUENCE 262 AA; 28282 MW; 326C915E8A48610F CRC64;
MIELEKLDFA KSVEGVEAFS TTRGQVDGRN AYSGVNLCDY VGDDALRVLD ARLTLAMQLG
VDLDDLVMPR QTHSCRVAVI DERFRALDID EQEAALEGVD ALVTRLQGIV IGVNTADCVP
IVLVDSQAGI VAVSHAGWRG TVGRIAKAVV EEMCRQGATV DRIQAAMGPS ICQDCFEVGD
EVVEAFKKAH FNLNDIVVRN PATGKAHIDL RAANRAVLVA AGVPAANIVE SQHCSRCEHT
SFFSARRLGI NSGRTFTGIY RK
