DEOB_SHIFL
ID DEOB_SHIFL Reviewed; 407 AA.
AC P0A6K9; P07651;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Phosphopentomutase;
DE EC=5.4.2.7;
DE AltName: Full=Phosphodeoxyribomutase;
GN Name=deoB; OrderedLocusNames=SF4415, S4686;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of
CC pentose. {ECO:0000250}.
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; AE005674; AAN45830.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19604.1; -; Genomic_DNA.
DR RefSeq; NP_710123.1; NC_004337.2.
DR RefSeq; WP_000816471.1; NZ_WPGW01000013.1.
DR AlphaFoldDB; P0A6K9; -.
DR SMR; P0A6K9; -.
DR STRING; 198214.SF4415; -.
DR EnsemblBacteria; AAN45830; AAN45830; SF4415.
DR EnsemblBacteria; AAP19604; AAP19604; S4686.
DR GeneID; 1026333; -.
DR GeneID; 67416060; -.
DR KEGG; sfl:SF4415; -.
DR KEGG; sfx:S4686; -.
DR PATRIC; fig|198214.7.peg.5203; -.
DR HOGENOM; CLU_053861_0_0_6; -.
DR OMA; YLGNCHA; -.
DR OrthoDB; 1772797at2; -.
DR UniPathway; UPA00087; UER00173.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 Acetylation; Cytoplasm; Isomerase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..407
FT /note="Phosphopentomutase"
FT /id="PRO_0000199838"
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:0000250"
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
