ID D2NVD7_LISM1 Unreviewed; 394 AA.
AC D2NVD7;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 01-MAY-2013, entry version 25.
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: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 14 14 Manganese (By similarity).
FT METAL 292 292 Manganese (By similarity).
FT METAL 328 328 Manganese (By similarity).
FT METAL 329 329 Manganese (By similarity).
FT METAL 340 340 Manganese (By similarity).
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
//
