DEOB_ECOLI
ID DEOB_ECOLI Reviewed; 407 AA.
AC P0A6K6; P07651; Q2M5T4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Phosphopentomutase;
DE EC=5.4.2.7;
DE AltName: Full=Phosphodeoxyribomutase;
GN Name=deoB; Synonyms=drm, thyR; OrderedLocusNames=b4383, JW4346;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RC STRAIN=K12;
RX PubMed=6087276; DOI=10.1093/nar/12.13.5211;
RA Valentin-Hansen P., Hammer K., Larsen J.E.L., Svendsen I.;
RT "The internal regulated promoter of the deo operon of Escherichia coli K-
RT 12.";
RL Nucleic Acids Res. 12:5211-5224(1984).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(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.
CC -!- SIMILARITY: Belongs to the phosphopentomutase family. {ECO:0000305}.
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DR EMBL; U14003; AAA97279.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77336.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78372.1; -; Genomic_DNA.
DR EMBL; X00742; CAA25325.1; -; Genomic_DNA.
DR PIR; S56607; S56607.
DR RefSeq; NP_418800.1; NC_000913.3.
DR RefSeq; WP_000816471.1; NZ_STEB01000033.1.
DR AlphaFoldDB; P0A6K6; -.
DR SMR; P0A6K6; -.
DR BioGRID; 4263160; 14.
DR BioGRID; 853187; 1.
DR DIP; DIP-48057N; -.
DR IntAct; P0A6K6; 6.
DR STRING; 511145.b4383; -.
DR iPTMnet; P0A6K6; -.
DR jPOST; P0A6K6; -.
DR PaxDb; P0A6K6; -.
DR PRIDE; P0A6K6; -.
DR EnsemblBacteria; AAC77336; AAC77336; b4383.
DR EnsemblBacteria; BAE78372; BAE78372; BAE78372.
DR GeneID; 67416060; -.
DR GeneID; 948910; -.
DR KEGG; ecj:JW4346; -.
DR KEGG; eco:b4383; -.
DR PATRIC; fig|1411691.4.peg.2302; -.
DR EchoBASE; EB0216; -.
DR eggNOG; COG1015; Bacteria.
DR HOGENOM; CLU_053861_0_0_6; -.
DR InParanoid; P0A6K6; -.
DR OMA; YLGNCHA; -.
DR PhylomeDB; P0A6K6; -.
DR BioCyc; EcoCyc:PPENTOMUT-MON; -.
DR BioCyc; MetaCyc:PPENTOMUT-MON; -.
DR BRENDA; 5.4.2.7; 2026.
DR UniPathway; UPA00087; UER00173.
DR PRO; PR:P0A6K6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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; IDA:EcoCyc.
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:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isomerase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..407
FT /note="Phosphopentomutase"
FT /id="PRO_0000199819"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT MOD_RES 287
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
SQ SEQUENCE 407 AA; 44370 MW; 516F3018DC77A077 CRC64;
MKRAFIMVLD SFGIGATEDA ERFGDVGADT LGHIAEACAK GEADNGRKGP LNLPNLTRLG
LAKAHEGSTG FIPAGMDGNA EVIGAYAWAH EMSSGKDTPS GHWEIAGVPV LFEWGYFSDH
ENSFPQELLD KLVERANLPG YLGNCHSSGT VILDQLGEEH MKTGKPIFYT SADSVFQIAC
HEETFGLDKL YELCEIAREE LTNGGYNIGR VIARPFIGDK AGNFQRTGNR HDLAVEPPAP
TVLQKLVDEK HGQVVSVGKI ADIYANCGIT KKVKATGLDA LFDATIKEMK EAGDNTIVFT
NFVDFDSSWG HRRDVAGYAA GLELFDRRLP ELMSLLRDDD ILILTADHGC DPTWTGTDHT
REHIPVLVYG PKVKPGSLGH RETFADIGQT LAKYFGTSDM EYGKAMF
