PURNU_CORGL
ID PURNU_CORGL Reviewed; 246 AA.
AC P94338; O24747;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Purine nucleoside phosphorylase Cgl2154/cg2365;
DE EC=2.4.2.1 {ECO:0000250|UniProtKB:P84138};
DE AltName: Full=Adenosine deaminase Cgl2154/cg2365;
DE EC=3.5.4.4 {ECO:0000250|UniProtKB:P84138};
DE AltName: Full=S-methyl-5'-thioadenosine phosphorylase Cgl2154/cg2365;
DE EC=2.4.2.28 {ECO:0000250|UniProtKB:P84138};
GN OrderedLocusNames=Cgl2154, cg2365;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9240446; DOI=10.1006/bbrc.1997.6930;
RA Kobayashi M., Asai Y., Hatakeyama K., Kijima N., Wachi M., Nagai K.,
RA Yukawa H.;
RT "Cloning, sequencing, and characterization of the ftsZ gene from coryneform
RT bacteria.";
RL Biochem. Biophys. Res. Commun. 236:383-388(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=9738885; DOI=10.1007/s004380050793;
RA Honrubia M.P., Fernandez F.J., Gil J.A.;
RT "Identification, characterization, and chromosomal organization of the ftsZ
RT gene from Brevibacterium lactofermentum.";
RL Mol. Gen. Genet. 259:97-104(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(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}.
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DR EMBL; AB003132; BAA21688.1; -; Genomic_DNA.
DR EMBL; Y08964; CAA70159.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99547.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20494.1; -; Genomic_DNA.
DR RefSeq; NP_601356.1; NC_003450.3.
DR RefSeq; WP_011014919.1; NC_006958.1.
DR AlphaFoldDB; P94338; -.
DR SMR; P94338; -.
DR STRING; 196627.cg2365; -.
DR PRIDE; P94338; -.
DR KEGG; cgb:cg2365; -.
DR KEGG; cgl:Cgl2154; -.
DR PATRIC; fig|196627.13.peg.2092; -.
DR eggNOG; COG1496; Bacteria.
DR HOGENOM; CLU_065784_3_1_11; -.
DR OMA; CFADCVP; -.
DR Proteomes; UP000000582; 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; Reference proteome;
KW Transferase; Zinc.
FT CHAIN 1..246
FT /note="Purine nucleoside phosphorylase Cgl2154/cg2365"
FT /id="PRO_0000163161"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P84138"
FT BINDING 107
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 CONFLICT 29
FT /note="S -> T (in Ref. 1; BAA21688)"
FT /evidence="ECO:0000305"
FT CONFLICT 38..41
FT /note="DDPQ -> YYPK (in Ref. 1; BAA21688)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="D -> N (in Ref. 2; CAA70159)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="V -> I (in Ref. 2; CAA70159)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="N -> K (in Ref. 1; BAA21688)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="I -> L (in Ref. 1; BAA21688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 26004 MW; 63C1CEB7DF05069E CRC64;
MDSLDPRNRP VRKVFTTRAG GVSQSPYASF NLGDHVGDDP QAVASNRNRL ADIIGLSPDK
VVYMEQIHSN TVTVIDEAPA DGQAVEATDA LVTTQRGLAL AVLVADCVPV LLSDTDAGVI
AAVHAGRMGA RNGIVAKTIA KMEELGAKPS RIHALMGAAA SGANYEVPEA MARDVEAKLP
GSIARTTKGT TGLDIRAGLL RQMLSLGVQM IDSDPRCTIE DEDLFSYRRE GTTGRQAGVV
WLPKEA
