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Database: UniProt
Entry: B7RUB3_9GAMM
LinkDB: B7RUB3_9GAMM
Original site: B7RUB3_9GAMM 
ID   B7RUB3_9GAMM            Unreviewed;       246 AA.
AC   B7RUB3;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Probable 6-oxopurine nucleoside phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE            EC=2.4.2.1 {ECO:0000256|HAMAP-Rule:MF_01963};
DE   AltName: Full=Purine nucleoside phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE            Short=PNP {ECO:0000256|HAMAP-Rule:MF_01963};
GN   Name=mtaP {ECO:0000313|EMBL:EEB79619.1};
GN   ORFNames=GPB2148_3462 {ECO:0000313|EMBL:EEB79619.1};
OS   marine gamma proteobacterium HTCC2148.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX   NCBI_TaxID=247634 {ECO:0000313|EMBL:EEB79619.1, ECO:0000313|Proteomes:UP000002793};
RN   [1] {ECO:0000313|Proteomes:UP000002793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2148 {ECO:0000313|Proteomes:UP000002793};
RX   PubMed=20472793; DOI=10.1128/jb.00511-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT   OM60/NOR5 clade of the Gammaproteobacteria.";
RL   J. Bacteriol. 192:3842-3843(2010).
CC   -!- FUNCTION: Purine nucleoside phosphorylase which is highly specific for
CC       6-oxopurine nucleosides. Cleaves guanosine or inosine to respective
CC       bases and sugar-1-phosphate molecules. Involved in purine salvage.
CC       {ECO:0000256|HAMAP-Rule:MF_01963}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase +
CC         alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01963};
CC   -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC       {ECO:0000256|HAMAP-Rule:MF_01963}.
CC   -!- SUBUNIT: Homohexamer. Dimer of a homotrimer. {ECO:0000256|HAMAP-
CC       Rule:MF_01963}.
CC   -!- MISCELLANEOUS: Although this enzyme belongs to the family of MTA
CC       phosphorylases based on sequence homology, it has been shown that
CC       conserved amino acid substitutions in the substrate binding pocket
CC       convert the substrate specificity of this enzyme from 6-aminopurines to
CC       6-oxopurines. {ECO:0000256|HAMAP-Rule:MF_01963}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01963}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01963}.
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DR   EMBL; DS999223; EEB79619.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7RUB3; -.
DR   STRING; 247634.GPB2148_3462; -.
DR   eggNOG; COG0005; Bacteria.
DR   HOGENOM; CLU_054456_0_2_6; -.
DR   OrthoDB; 1523230at2; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000002793; Unassembled WGS sequence.
DR   GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:InterPro.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-UniRule.
DR   CDD; cd09010; MTAP_SsMTAPII_like_MTIP; 1.
DR   Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR   HAMAP; MF_01963; MTAP; 1.
DR   InterPro; IPR010044; MTAP.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   PANTHER; PTHR42679; S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR42679:SF2; S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01963};
KW   Purine salvage {ECO:0000256|HAMAP-Rule:MF_01963};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002793};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01963}.
FT   DOMAIN          4..243
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
FT   BINDING         10
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT   BINDING         52..53
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT   BINDING         186
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT   BINDING         209..211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT   SITE            167
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT   SITE            221
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
SQ   SEQUENCE   246 AA;  26139 MW;  36296CDACB8775B4 CRC64;
     MKTLGIIGGT GIDQLEGLEI VDSHAVETPY GDPSRAVEEG MLGGVRVFFL QRHGSPKTIP
     PHLINYRANV WALKSLQVTD LVAINAVGGI SAAMRPGRLV IPDQIVDYTW GRAHTVDTGE
     VGTLLHVDFS DPYDHELREA LLQCAVAQNI AHEGAGVHGV MQGPRLESAA EIRRMAGDGC
     DLVGMTGMPE ASLARELGLA YASICMVVNA AAGLDDKPLT LAVMRANLLR EAAAVRQLIA
     ALVADY
//
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