(data stored in SCRATCH zone)

SWISSPROT: DEOB_BACSU

ID   DEOB_BACSU              Reviewed;         394 AA.
AC   P46353;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   11-DEC-2019, entry version 138.
DE   RecName: Full=Phosphopentomutase;
DE            EC=5.4.2.7;
DE   AltName: Full=Phosphodeoxyribomutase;
GN   Name=drm; Synonyms=yqkN; OrderedLocusNames=BSU23500;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / BR151;
RX   PubMed=10537218; DOI=10.1099/00221287-145-10-2957;
RA   Schuch R., Garibian A., Saxild H.H., Piggot P.J., Nygaard P.;
RT   "Nucleosides as a carbon source in Bacillus subtilis: characterization of
RT   the drm-pupG operon.";
RL   Microbiology 145:2957-2966(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO 78 AND 316.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of
CC       pentose.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-ribose 1-phosphate = D-ribose 5-phosphate;
CC         Xref=Rhea:RHEA:18793, ChEBI:CHEBI:57720, ChEBI:CHEBI:78346;
CC         EC=5.4.2.7;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-D-ribose 5-
CC         phosphate; Xref=Rhea:RHEA:27658, ChEBI:CHEBI:57259,
CC         ChEBI:CHEBI:62877; EC=5.4.2.7;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC       Note=Binds 1 or 2 manganese ions. {ECO:0000305};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC       1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC       D-ribose 5-phosphate (route II): step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphopentomutase family. {ECO:0000305}.
DR   EMBL; U32685; AAA74433.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12650.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14282.2; -; Genomic_DNA.
DR   PIR; B69619; B69619.
DR   RefSeq; NP_390231.2; NC_000964.3.
DR   RefSeq; WP_003230444.1; NZ_JNCM01000036.1.
DR   SMR; P46353; -.
DR   STRING; 224308.BSU23500; -.
DR   jPOST; P46353; -.
DR   PaxDb; P46353; -.
DR   PRIDE; P46353; -.
DR   EnsemblBacteria; CAB14282; CAB14282; BSU23500.
DR   GeneID; 938728; -.
DR   KEGG; bsu:BSU23500; -.
DR   PATRIC; fig|224308.179.peg.2560; -.
DR   eggNOG; ENOG4105CZG; Bacteria.
DR   eggNOG; COG1015; LUCA.
DR   HOGENOM; HOG000008159; -.
DR   InParanoid; P46353; -.
DR   KO; K01839; -.
DR   OMA; YLGNCHA; -.
DR   PhylomeDB; P46353; -.
DR   BioCyc; BSUB:BSU23500-MONOMER; -.
DR   UniPathway; UPA00087; UER00173.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008973; F:phosphopentomutase activity; IBA:GO_Central.
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-UniRule.
DR   CDD; cd16009; PPM; 1.
DR   Gene3D; 3.30.70.1250; -; 1.
DR   Gene3D; 3.40.720.10; -; 1.
DR   HAMAP; MF_00740; Phosphopentomut; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR010045; DeoB.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR024052; Phosphopentomutase_DeoB_cap_sf.
DR   PANTHER; PTHR21110; PTHR21110; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   PIRSF; PIRSF001491; Ppentomutase; 1.
DR   SUPFAM; SSF143856; SSF143856; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   TIGRFAMs; TIGR01696; deoB; 1.
PE   3: Inferred from homology;
DR   PRODOM; P46353.
DR   SWISS-2DPAGE; P46353.
KW   Cytoplasm; Isomerase; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..394
FT                   /note="Phosphopentomutase"
FT                   /id="PRO_0000199810"
FT   METAL           15
FT                   /note="Manganese"
FT                   /evidence="ECO:0000250"
FT   METAL           293
FT                   /note="Manganese"
FT                   /evidence="ECO:0000250"
FT   METAL           329
FT                   /note="Manganese"
FT                   /evidence="ECO:0000250"
FT   METAL           330
FT                   /note="Manganese"
FT                   /evidence="ECO:0000250"
FT   METAL           341
FT                   /note="Manganese"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        78
FT                   /note="M -> L (in Ref. 2; BAA12650)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        207
FT                   /note="Q -> QFK (in Ref. 1; AAA74433)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        316
FT                   /note="E -> G (in Ref. 2; BAA12650)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   394 AA;  44019 MW;  84034CCC0BFB15C5 CRC64;
     MPAYKYNRVF LIVMDSVGIG EAPDAADFND EGAHTLGHIA EHMNGLHMPN MAKLGLGLIE
     DIKGVEKTEH PLAYYGKMQE ASNGKDTMTG HWEIMGLYID KPFKVFPEGF PDELLQELEK
     RSGRKIIGNK PASGTAILDE LGQEHMETGA LIVYTSADSV LQIAAHEEVV PLEELYRICE
     TARELTLDPK YMVGRIIARP FVGEPGQFKR TPNRHDYALK PFDRTVMNEL KDCGLDVISI
     GKISDIYDGE GITSSRRTVS NMDGMDKVID TLGEDFTGLS FANLVDFDAL FGHRRDPEGY
     GRALEEFDAR LPEVFEKMRE DDLLIITADH GNDPIHHGTD HTREYVPILA YSKKHKKAQM
     LPLADTFADI GATIADNFQT NKPKYGKSFL SLLQ
//

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