GENTAUR Molecular Products.

 DEOB_STRA5              Reviewed;         403 AA.
 Q8CMH6;
 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
 01-MAR-2003, sequence version 1.
 28-FEB-2018, entry version 95.
 RecName: Full=Phosphopentomutase {ECO:0000255|HAMAP-Rule:MF_00740};
          EC=5.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00740};
 AltName: Full=Phosphodeoxyribomutase {ECO:0000255|HAMAP-Rule:MF_00740};
 Name=deoB1 {ECO:0000255|HAMAP-Rule:MF_00740}; Synonyms=deoB-1;
 OrderedLocusNames=SAG1182;
 and
 Name=deoB2 {ECO:0000255|HAMAP-Rule:MF_00740}; Synonyms=deoB-2;
 OrderedLocusNames=SAG2069;
 Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
 Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
 Streptococcus.
 NCBI_TaxID=208435;
 [1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=ATCC BAA-611 / 2603 V/R;
 PubMed=12200547; DOI=10.1073/pnas.182380799;
 Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
 Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
 Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
 DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R.,
 Radune D., Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S.,
 Carty H.A., Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M.,
 Iacobini E.T., Brettoni C., Galli G., Mariani M., Vegni F., Maione D.,
 Rinaudo D., Rappuoli R., Telford J.L., Kasper D.L., Grandi G.,
 Fraser C.M.;
 "Complete genome sequence and comparative genomic analysis of an
 emerging human pathogen, serotype V Streptococcus agalactiae.";
 Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
 -!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of
     pentose. {ECO:0000255|HAMAP-Rule:MF_00740}.
 -!- CATALYTIC ACTIVITY: Alpha-D-ribose 1-phosphate = D-ribose 5-
     phosphate. {ECO:0000255|HAMAP-Rule:MF_00740}.
 -!- CATALYTIC ACTIVITY: 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-
     alpha-D-ribose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00740}.
 -!- COFACTOR:
     Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
       Evidence={ECO:0000255|HAMAP-Rule:MF_00740};
     Note=Binds 1 or 2 manganese ions. {ECO:0000255|HAMAP-
     Rule:MF_00740};
 -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-
     ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
     diphosphate from D-ribose 5-phosphate (route II): step 1/3.
     {ECO:0000255|HAMAP-Rule:MF_00740}.
 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00740}.
 -!- SIMILARITY: Belongs to the phosphopentomutase family.
     {ECO:0000255|HAMAP-Rule:MF_00740}.
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 EMBL; AE009948; AAN00064.1; -; Genomic_DNA.
 EMBL; AE009948; AAN00928.1; -; Genomic_DNA.
 RefSeq; NP_688191.1; NC_004116.1.
 RefSeq; NP_689055.1; NC_004116.1.
 RefSeq; WP_000077187.1; NC_004116.1.
 ProteinModelPortal; Q8CMH6; -.
 SMR; Q8CMH6; -.
 EnsemblBacteria; AAN00064; AAN00064; SAG1182.
 EnsemblBacteria; AAN00928; AAN00928; SAG2069.
 GeneID; 1013989; -.
 GeneID; 1014880; -.
 KEGG; sag:SAG1182; -.
 KEGG; sag:SAG2069; -.
 PATRIC; fig|208435.3.peg.1189; -.
 HOGENOM; HOG000008159; -.
 KO; K01839; -.
 OMA; CHASGTE; -.
 UniPathway; UPA00087; UER00173.
 Proteomes; UP000000821; Chromosome.
 GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO; GO:0008973; F:phosphopentomutase activity; IEA:UniProtKB-EC.
 GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
 GO; GO:0043094; P:cellular metabolic compound salvage; IEA:InterPro.
 GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro.
 CDD; cd16009; PPM; 1.
 Gene3D; 3.30.70.1250; -; 1.
 Gene3D; 3.40.720.10; -; 2.
 HAMAP; MF_00740; Phosphopentomut; 1.
 InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
 InterPro; IPR017850; Alkaline_phosphatase_core_sf.
 InterPro; IPR010045; DeoB.
 InterPro; IPR006124; Metalloenzyme.
 InterPro; IPR024052; Phosphopentomutase_DeoB_cap_sf.
 PANTHER; PTHR21110; PTHR21110; 1.
 Pfam; PF01676; Metalloenzyme; 1.
 PIRSF; PIRSF001491; Ppentomutase; 1.
 SUPFAM; SSF143856; SSF143856; 1.
 SUPFAM; SSF53649; SSF53649; 2.
 TIGRFAMs; TIGR01696; deoB; 1.
 3: Inferred from homology;
 Complete proteome; Cytoplasm; Isomerase; Manganese; Metal-binding;
 Reference proteome.
 CHAIN         1    403       Phosphopentomutase.
                              /FTId=PRO_0000199850.
 METAL        13     13       Manganese. {ECO:0000255|HAMAP-
                              Rule:MF_00740}.
 METAL       303    303       Manganese. {ECO:0000255|HAMAP-
                              Rule:MF_00740}.
 METAL       339    339       Manganese. {ECO:0000255|HAMAP-
                              Rule:MF_00740}.
 METAL       340    340       Manganese. {ECO:0000255|HAMAP-
                              Rule:MF_00740}.
 METAL       351    351       Manganese. {ECO:0000255|HAMAP-
                              Rule:MF_00740}.
 SEQUENCE   403 AA;  44202 MW;  1B2D6A62D2C3ED60 CRC64;
 MSQFDRIHLV VLDSVGIGAA PDANDFVNAG VPDGASDTLG HISKTVGLAV PNMAKIGLGN
 IPRPQALKTV PAEENPSGYA TKLQEVSLGK DTMTGHWEIM GLNITEPFDT FWNGFPEDII
 TKIEDFSGRK VIREANKPYS GTAVIDDFGP RQMETGELII YTSADPVLQI AAHEDIIPLE
 ELYRICEYAR SITMERPALL GRIIARPYVG EPGNFTRTAN RHDYAVSPFE DTVLNKLDQA
 GIDTYAVGKI NDIFNGSGIN HDMGHNKSNS HGIDTLIKTM GLSEFEKGFS FTNLVDFDAL
 YGHRRDPHGY RDCLHEFDER LPEIISAMRD KDLLLITADH GNDPTYAGTD HTREYIPLLA
 YSPSFTGNGL IPVGHFADIS ATVADNFGVD TAMIGESFLQ DLV

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