ID E3DXA3_BACA1 Unreviewed; 394 AA.
AC E3DXA3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 01-MAY-2013, entry version 19.
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 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:HAMAP.
DR GO; GO:0008973; F:phosphopentomutase activity; IEA: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: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; SSF53649; Alkaline_phosphatase_core; 1.
DR SUPFAM; SSF143856; SSF143856; 1.
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).
FT METAL 293 293 Manganese (By similarity).
FT METAL 329 329 Manganese (By similarity).
FT METAL 330 330 Manganese (By similarity).
FT METAL 341 341 Manganese (By similarity).
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
//
