DEOB_CHRVO
ID DEOB_CHRVO Reviewed; 405 AA.
AC Q7NRT1;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Phosphopentomutase {ECO:0000255|HAMAP-Rule:MF_00740};
DE EC=5.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00740};
DE AltName: Full=Phosphodeoxyribomutase {ECO:0000255|HAMAP-Rule:MF_00740};
GN Name=deoB {ECO:0000255|HAMAP-Rule:MF_00740}; OrderedLocusNames=CV_3699;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
CC -!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of
CC pentose. {ECO:0000255|HAMAP-Rule:MF_00740}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00740};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00740};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00740};
CC Note=Binds 1 or 2 manganese ions. {ECO:0000255|HAMAP-Rule:MF_00740};
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. {ECO:0000255|HAMAP-
CC Rule:MF_00740}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00740}.
CC -!- SIMILARITY: Belongs to the phosphopentomutase family.
CC {ECO:0000255|HAMAP-Rule:MF_00740}.
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DR EMBL; AE016825; AAQ61361.1; -; Genomic_DNA.
DR RefSeq; WP_011137246.1; NC_005085.1.
DR AlphaFoldDB; Q7NRT1; -.
DR SMR; Q7NRT1; -.
DR STRING; 243365.CV_3699; -.
DR EnsemblBacteria; AAQ61361; AAQ61361; CV_3699.
DR KEGG; cvi:CV_3699; -.
DR eggNOG; COG1015; Bacteria.
DR HOGENOM; CLU_053861_0_0_4; -.
DR OMA; YLGNCHA; -.
DR OrthoDB; 1772797at2; -.
DR UniPathway; UPA00087; UER00173.
DR Proteomes; UP000001424; Chromosome.
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:UniProtKB-UniRule.
DR GO; GO:0008973; F:phosphopentomutase activity; IEA:UniProtKB-UniRule.
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..405
FT /note="Phosphopentomutase"
FT /id="PRO_0000199814"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT BINDING 308
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT BINDING 344
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT BINDING 345
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT BINDING 356
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
SQ SEQUENCE 405 AA; 43450 MW; 35D0818CF3A60A06 CRC64;
MKRAIILILD SLGIGAAADA PKFGDAGSNT LGHIAMEAAA GRADIGRSGP LKLPNLSRMG
LGHACQLSSG YFPEGMDPAA PAAAYGYARE ISSGKDTPSG HWEIAGVPVL FDWGYFSDHD
NSFPQQLLDA IVDKAGLPGY LGNCHASGTE ILDRLGEEHM KTGKPIFYTS ADSVFQIACH
EETYGLERLY ELCKITRELL EPYNIGRVIA RPFVGEGKGK FARTGNRKDL AVEPPAATVL
KKLADAGGDV VSIGKIADIY AHVGITHKHK ATGFDQLWDA TLTAMDQHRD KPAIIMANFV
DFDSSYGHRR NTAGYAAALE EFDARLPEVM AALGDDDILI LSADHGCDPT WPGTDHTREH
IPVLCYGKQV KAGPIGERAT FADIGQSVAA HLGLPRMDYG TSFLD
