(data stored in ACNUC7421 zone)

SWISSPROT: DEOD_EDWI9

ID   DEOD_EDWI9              Reviewed;         237 AA.
AC   C5BHJ5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 47.
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};
GN   OrderedLocusNames=NT01EI_0565;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Purine nucleoside + phosphate = purine +
CC       alpha-D-ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01627}.
CC   -!- CATALYTIC ACTIVITY: Purine deoxynucleoside + phosphate = purine +
CC       2'-deoxy-alpha-D-ribose 1-phosphate. {ECO:0000255|HAMAP-
CC       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; CP001600; ACR67794.1; -; Genomic_DNA.
DR   RefSeq; WP_015869994.1; NC_012779.2.
DR   ProteinModelPortal; C5BHJ5; -.
DR   SMR; C5BHJ5; -.
DR   STRING; 634503.NT01EI_0565; -.
DR   PRIDE; C5BHJ5; -.
DR   EnsemblBacteria; ACR67794; ACR67794; NT01EI_0565.
DR   GeneID; 7960333; -.
DR   KEGG; eic:NT01EI_0565; -.
DR   PATRIC; fig|634503.3.peg.510; -.
DR   eggNOG; ENOG4105D3A; Bacteria.
DR   eggNOG; COG0813; LUCA.
DR   HOGENOM; HOG000274896; -.
DR   KO; K03784; -.
DR   OMA; PQCLLCG; -.
DR   OrthoDB; POG091H02M1; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
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   PANTHER; PTHR43691:SF1; PTHR43691:SF1; 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; C5BHJ5.
DR   SWISS-2DPAGE; C5BHJ5.
KW   Complete proteome; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN         1    237       Purine nucleoside phosphorylase DeoD-
FT                                type.
FT                                /FTId=PRO_1000215749.
FT   REGION       88     91       Phosphate binding.
FT                                {ECO:0000250|UniProtKB:P50389}.
FT   REGION      180    182       Purine nucleoside binding.
FT                                {ECO:0000250|UniProtKB:P50389}.
FT   REGION      204    205       Purine nucleoside binding.
FT                                {ECO:0000250|UniProtKB:P50389}.
FT   BINDING       5      5       Purine nucleoside; shared with dimeric
FT                                partner. {ECO:0000250|UniProtKB:P50389}.
FT   BINDING      21     21       Phosphate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:P50389}.
FT   BINDING      25     25       Phosphate.
FT                                {ECO:0000250|UniProtKB:P50389}.
FT   BINDING      44     44       Phosphate; shared with dimeric partner.
FT                                {ECO:0000250|UniProtKB:P50389}.
SQ   SEQUENCE   237 AA;  25654 MW;  ACFED10150AF7ABB CRC64;
     MATPHINAEM GDFADVVLMP GDPLRAKHIA ETFLQDVRQV NNVRGMLGFT GTYKGRKISV
     MGHGMGIPSC SIYAKELITD FGVKKIIRVG SCGAVSMDVK LRDVVIGMGA CTDSKVNRLR
     FKDNDFAAIA DFDMVRNAAD AAKAKGIDAR VGNLFSADLF YSPDPTMFDV MEKYGILGVE
     MEAAGIYGVA AEFGVKALTI CTVSDHIRTH EQTTAAERQT TFNDMIEIAL ESVLLGD
//

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