(data stored in ACNUC7421 zone)

SWISSPROT: DEOD_HISS2

ID   DEOD_HISS2              Reviewed;         238 AA.
AC   B0UVM2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 64.
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=HSM_0161;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-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; CP000947; ACA31374.1; -; Genomic_DNA.
DR   RefSeq; WP_012340740.1; NC_010519.1.
DR   SMR; B0UVM2; -.
DR   EnsemblBacteria; ACA31374; ACA31374; HSM_0161.
DR   GeneID; 31486439; -.
DR   KEGG; hsm:HSM_0161; -.
DR   HOGENOM; HOG000274896; -.
DR   KO; K03784; -.
DR   OMA; PQCLLCG; -.
DR   OrthoDB; 1028277at2; -.
DR   BioCyc; HSOM228400:G1GB8-166-MONOMER; -.
DR   Proteomes; UP000008543; 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; B0UVM2.
DR   SWISS-2DPAGE; B0UVM2.
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..238
FT                   /note="Purine nucleoside phosphorylase DeoD-type"
FT                   /id="PRO_1000088104"
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   238 AA;  25929 MW;  43CE307B272A3BCE CRC64;
     MTPHINAPAG AFADVVLMPG DPLRAKYIAE TFLENAQEVT NVRNMLGYTG TYKGRKISVM
     GHGMGIPSCS IYAKELITEY GVKKIIRVGS CGAVNMDVKI RDVIIGLGAC TDSKVNRIRF
     KDNDFAAIAD FGMARAAVQA AKNKGIDVKV GNLFSADLFY TPDLEMFDVM EKYGILGVEM
     EAAGIYGVAA EFKAKALTIC TVSDHIRTHE QTSAEERQLT FNEMIEIALE SVLLEDSL
//

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