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 03-AUG-2022, entry version 144.
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}.
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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 AlphaFoldDB; P46353; -.
DR SMR; P46353; -.
DR STRING; 224308.BSU23500; -.
DR jPOST; P46353; -.
DR PaxDb; P46353; -.
DR PRIDE; P46353; -.
DR EnsemblBacteria; CAB14282; CAB14282; BSU_23500.
DR GeneID; 938728; -.
DR KEGG; bsu:BSU23500; -.
DR PATRIC; fig|224308.179.peg.2560; -.
DR eggNOG; COG1015; Bacteria.
DR InParanoid; P46353; -.
DR OMA; YLGNCHA; -.
DR PhylomeDB; P46353; -.
DR BioCyc; BSUB:BSU23500-MON; -.
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;
KW Cytoplasm; Isomerase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..394
FT /note="Phosphopentomutase"
FT /id="PRO_0000199810"
FT BINDING 15
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
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
