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Database: UniProt/TrEMBL
Entry: E3DXA3_BACA1
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ID   E3DXA3_BACA1            Unreviewed;       394 AA.
AC   E3DXA3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   11-JUN-2014, entry version 23.
DE   RecName: Full=Phosphopentomutase;
DE            EC=5.4.2.7;
DE   AltName: Full=Phosphodeoxyribomutase;
GN   Name=deoB; OrderedLocusNames=BATR1942_10030;
OS   Bacillus atrophaeus (strain 1942).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=720555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1942;
RA   Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C.,
RA   Bruce D., Karavis M., McGregor P., Hong C., Park K.H., Akmal A.,
RA   Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA   Lindquist J., Liem A., Fochler E., Tapia R., Bishop-Lilly K.,
RA   Detter C., Han C., Sozhamannan S., Rosenzweig C.N., Skowronski E.;
RT   "Genomic signatures of strain selection and enhancement in Bacillus
RT   atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of
CC       pentose (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-
CC       alpha-D-ribose 5-phosphate.
CC   -!- CATALYTIC ACTIVITY: Alpha-D-ribose 1-phosphate = D-ribose 5-
CC       phosphate.
CC   -!- COFACTOR: Binds 1 or 2 manganese ions (By similarity).
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-
CC       ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
CC       diphosphate from D-ribose 5-phosphate (route II): step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphopentomutase family.
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DR   EMBL; CP002207; ADP32939.1; -; Genomic_DNA.
DR   RefSeq; YP_003973870.1; NC_014639.1.
DR   EnsemblBacteria; ADP32939; ADP32939; BATR1942_10030.
DR   GeneID; 9891977; -.
DR   KEGG; bae:BATR1942_10030; -.
DR   PATRIC; 42570797; VBIBacAtr152324_2012.
DR   HOGENOM; HOG000008159; -.
DR   KO; K01839; -.
DR   OMA; IRTKDNM; -.
DR   BioCyc; BATR720555:GHTA-2009-MONOMER; -.
DR   UniPathway; UPA00087; UER00173.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008973; F:phosphopentomutase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0043094; P:cellular metabolic compound salvage; IEA:InterPro.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.70.1250; -; 1.
DR   Gene3D; 3.40.720.10; -; 2.
DR   HAMAP; MF_00740; Phosphopentomut; 1.
DR   InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
DR   InterPro; IPR017850; Alkaline_phosphatase_core.
DR   InterPro; IPR010045; DeoB.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR024052; Phosphopentomutase_DeoB_cap.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   PIRSF; PIRSF001491; Ppentomutase; 1.
DR   SUPFAM; SSF143856; SSF143856; 1.
DR   SUPFAM; SSF53649; SSF53649; 2.
DR   TIGRFAMs; TIGR01696; deoB; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Isomerase; Manganese; Metal-binding.
FT   METAL        15     15       Manganese (By similarity){EA3}.
FT   METAL       293    293       Manganese (By similarity){EA3}.
FT   METAL       329    329       Manganese (By similarity){EA3}.
FT   METAL       330    330       Manganese (By similarity){EA3}.
FT   METAL       341    341       Manganese (By similarity){EA3}.
SQ   SEQUENCE   394 AA;  43948 MW;  1CD1BBACC310747F CRC64;
     MPAYNYNRVF LIVMDSVGIG EAPDAADFDD KGANTLGHIA EHMNGLHMPH MANLGLGLIG
     DIQGVEKTES PLAYYGKMKE ASNGKDTMTG HWEIMGLYID KPFKVFPEGF PDELIQELEK
     RSGRKIIGNK PASGTEILDE LGKEHVETGA LIVYTSADSV LQIAAHEEVV PLDELYSICE
     TARELTLDPK YMVGRIIARP FVDEPGNFKR TPNRHDYALK PFERTVMNEL KDSGLDVISI
     GKISDIYDGE GITSSRRTVS NMDGMDKVIE TLDEEFTGIS FANLVDFDAL YGHRRDPEGY
     GRALEEFDAR LPEVFEKMKE DDVLIITADH GNDPVHHGTD HTREYVPLLV YSKKHQKAQK
     LPLADTFADI GATIADNFHT KKPKYGKSFL SLLQ
//
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