ID DEOB_STAEQ Reviewed; 396 AA.
AC Q5HM86;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 01-MAY-2013, entry version 66.
DE RecName: Full=Phosphopentomutase;
DE EC=5.4.2.7;
DE AltName: Full=Phosphodeoxyribomutase;
GN Name=deoB; Synonyms=drm; OrderedLocusNames=SERP1743;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA Hance I.R., Nelson K.E., Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete
RT genome analysis of an early methicillin-resistant Staphylococcus
RT aureus strain and a biofilm-producing methicillin-resistant
RT Staphylococcus epidermidis strain.";
RL J. Bacteriol. 187:2426-2438(2005).
CC -!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of
CC pentose (By similarity).
CC -!- CATALYTIC ACTIVITY: Alpha-D-ribose 1-phosphate = D-ribose 5-
CC phosphate.
CC -!- CATALYTIC ACTIVITY: 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-
CC alpha-D-ribose 5-phosphate.
CC -!- COFACTOR: Binds 1 or 2 manganese ions (Potential).
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; CP000029; AAW55073.1; -; Genomic_DNA.
DR RefSeq; YP_189307.1; NC_002976.3.
DR ProteinModelPortal; Q5HM86; -.
DR STRING; 176279.SERP1743; -.
DR EnsemblBacteria; AAW55073; AAW55073; SERP1743.
DR GeneID; 3242740; -.
DR KEGG; ser:SERP1743; -.
DR PATRIC; 19614407; VBIStaEpi130894_1702.
DR eggNOG; COG1015; -.
DR HOGENOM; HOG000008159; -.
DR KO; K01839; -.
DR OMA; PNMAKLG; -.
DR ProtClustDB; PRK05362; -.
DR BioCyc; SEPI176279:GJJB-1812-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 CHAIN 1 396 Phosphopentomutase.
FT /FTId=PRO_0000199846.
FT METAL 14 14 Manganese (By similarity).
FT METAL 291 291 Manganese (By similarity).
FT METAL 327 327 Manganese (By similarity).
FT METAL 328 328 Manganese (By similarity).
FT METAL 339 339 Manganese (By similarity).
SQ SEQUENCE 396 AA; 44475 MW; A3EC52119AFD8B17 CRC64;
MTTPFKRIHL IVMDSVGIGE GPDAAAFNDE GSHTLKHTLE GFKQKLPHLE QLGLGNIAPL
PVVSKVTHPG AFYTKLSEAS VGKDTMTGHW EIMGLNIMQP FKVYPNGFPE ELVKEIESMT
GRKVVANRPA SGTQIIDEWG EHQMKTGDLI VYTSADPVLQ IAAHEDVIPL EELYEICEKV
RELTKDPKYL IGRIIARPYV GEPGNFTRTS NRHDYALKPF GRTVMNSLKD NGYDVIAIGK
INDIYDGEGV TEAIRTKNNM DGMDQLIEVV KKDFEGISFL NLVDFDALYG HRRDKEGYAQ
AIKDFDLRLP ELMNHLREDD LVIITADHGN DPIAKGTDHT REYIPLLMFS PKIKDYHELS
QDTTFSSIGV TIADNFNVEL PKYGKSYLKE MGVEHQ
//
