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Database: UniProt/TrEMBL
Entry: D2NVD7_LISM1
LinkDB: D2NVD7_LISM1
Original site: D2NVD7_LISM1 
ID   D2NVD7_LISM1            Unreviewed;       394 AA.
AC   D2NVD7;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   11-JUN-2014, entry version 28.
DE   RecName: Full=Phosphopentomutase;
DE            EC=5.4.2.7;
DE   AltName: Full=Phosphodeoxyribomutase;
GN   Name=drm; Synonyms=deoB; OrderedLocusNames=LM5578_2155;
OS   Listeria monocytogenes serotype 1/2a (strain 08-5578).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=653938;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=08-5578;
RX   PubMed=20167121; DOI=10.1186/1471-2164-11-120;
RA   Gilmour M.W., Graham M., Van Domselaar G., Tyler S., Kent H.,
RA   Trout-Yakel K.M., Larios O., Allen V., Lee B., Nadon C.;
RT   "High-throughput genome sequencing of two Listeria monocytogenes
RT   clinical isolates during a large foodborne outbreak.";
RL   BMC Genomics 11:120-120(2010).
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; CP001602; ADB68902.1; -; Genomic_DNA.
DR   RefSeq; YP_003414264.1; NC_013766.1.
DR   ProteinModelPortal; D2NVD7; -.
DR   SMR; D2NVD7; 3-393.
DR   EnsemblBacteria; ADB68902; ADB68902; LM5578_2155.
DR   GeneID; 8749138; -.
DR   KEGG; lmn:LM5578_2155; -.
DR   PATRIC; 35278828; VBILisMon159512_2170.
DR   HOGENOM; HOG000008159; -.
DR   KO; K01839; -.
DR   BioCyc; LMON653938:GJ8G-2185-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        14     14       Manganese (By similarity){EA3}.
FT   METAL       292    292       Manganese (By similarity){EA3}.
FT   METAL       328    328       Manganese (By similarity){EA3}.
FT   METAL       329    329       Manganese (By similarity){EA3}.
FT   METAL       340    340       Manganese (By similarity){EA3}.
SQ   SEQUENCE   394 AA;  43746 MW;  1D2D6202D2C95D23 CRC64;
     MPDKFKRVHV VVMDSVGIGE APDAAKFGDF DVDTFGHIAK HVGGLKMPEM GKLGLSNIRE
     IEGIKKAEKP LAYYTKMQEA SNGKDTMTGH WEIMGLYIDT PFRVFPDGFP DDLINQIEEK
     TGRKVIGNKP ASGTEIMAEL GEEHVKTGAL IVYTSADSVL QIAAHEDVVP LEELYEICEF
     CRKITLDDPY MLGRIIARPF VGEPGAFVRT PNRHDYALKP FKPTVMDALK DGGKDVIAIG
     KISDIFDGEG VTESIRTKSN MDGMDQFIAV LDKDFNGMSF LNLVDFDALF GHRRDPQGYA
     DALVDFDGRL VEVMEKLTDD DLLIITADHG NDPTYTGTDH TREFVPLLVY SPRFKNGGSE
     LELRKTFADL GATVADNFDV KMPEYGTSFL RDLK
//
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