(data stored in ACNUC7421 zone)

SWISSPROT: DEOD_EXIS2

ID   DEOD_EXIS2              Reviewed;         235 AA.
AC   B1YJP1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   11-DEC-2019, entry version 80.
DE   RecName: Full=Purine nucleoside phosphorylase DeoD-type {ECO:0000255|HAMAP-Rule:MF_01627};
DE            Short=PNP {ECO:0000255|HAMAP-Rule:MF_01627};
DE            EC=2.4.2.1 {ECO:0000255|HAMAP-Rule:MF_01627};
GN   Name=deoD {ECO:0000255|HAMAP-Rule:MF_01627}; OrderedLocusNames=Exig_0590;
OS   Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_01627};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy-
CC         alpha-D-ribose 1-phosphate + a purine nucleobase;
CC         Xref=Rhea:RHEA:36431, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57259, ChEBI:CHEBI:142361; EC=2.4.2.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01627};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01627}.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01627}.
DR   EMBL; CP001022; ACB60071.1; -; Genomic_DNA.
DR   RefSeq; WP_012369495.1; NC_010556.1.
DR   SMR; B1YJP1; -.
DR   STRING; 262543.Exig_0590; -.
DR   EnsemblBacteria; ACB60071; ACB60071; Exig_0590.
DR   KEGG; esi:Exig_0590; -.
DR   eggNOG; ENOG4105D3A; Bacteria.
DR   eggNOG; COG0813; LUCA.
DR   HOGENOM; HOG000274896; -.
DR   KO; K03784; -.
DR   OMA; PQCLLCG; -.
DR   OrthoDB; 1028277at2; -.
DR   Proteomes; UP000001681; Chromosome.
DR   GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042278; P:purine nucleoside metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1580; -; 1.
DR   HAMAP; MF_01627; Pur_nucleosid_phosp; 1.
DR   InterPro; IPR004402; DeoD-type.
DR   InterPro; IPR018016; Nucleoside_phosphorylase_CS.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   PANTHER; PTHR43691:SF2; PTHR43691:SF2; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; SSF53167; 1.
DR   TIGRFAMs; TIGR00107; deoD; 1.
DR   PROSITE; PS01232; PNP_UDP_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1YJP1.
DR   SWISS-2DPAGE; B1YJP1.
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..235
FT                   /note="Purine nucleoside phosphorylase DeoD-type"
FT                   /id="PRO_1000186197"
FT   REGION          87..90
FT                   /note="Phosphate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P50389"
FT   REGION          179..181
FT                   /note="Purine nucleoside binding"
FT                   /evidence="ECO:0000250|UniProtKB:P50389"
FT   REGION          203..204
FT                   /note="Purine nucleoside binding"
FT                   /evidence="ECO:0000250|UniProtKB:P50389"
FT   BINDING         4
FT                   /note="Purine nucleoside; shared with dimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:P50389"
FT   BINDING         20
FT                   /note="Phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P50389"
FT   BINDING         24
FT                   /note="Phosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P50389"
FT   BINDING         43
FT                   /note="Phosphate; shared with dimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:P50389"
SQ   SEQUENCE   235 AA;  25807 MW;  333A794EC9084BB8 CRC64;
     MSVHINAAEG QIAETVLLPG DPLRAKYIAD TFLEDVVLYN EVRGMYGFTG TYKGKKVSVQ
     GTGMGVPSMS IYANELVQSY GAKNLIRVGT AGGITPDVKV RDVVIAMSAS HDMAQNRVRF
     NGLDYAPTAS FDLLHKAYMT AKEHGIDAKV GQIFTTDQFY QDDFHHFKKW ADFGCLAIEM
     EAAGLYTLAA KHKVNALTIL TISDHLLTGE ETTAEERQTT FNDMMKVALE TAIQL
//

If you have problems or comments...

PBIL Back to PBIL home page