ID   DEOB_CLOK1              Reviewed;         389 AA.
AC   B9E115;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=CKR_1139;
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016;
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA   Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT   of Clostridia species.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; AP009049; BAH06190.1; -; Genomic_DNA.
DR   RefSeq; WP_012101628.1; NC_011837.1.
DR   AlphaFoldDB; B9E115; -.
DR   SMR; B9E115; -.
DR   EnsemblBacteria; BAH06190; BAH06190; CKR_1139.
DR   KEGG; ckr:CKR_1139; -.
DR   HOGENOM; CLU_053861_0_0_9; -.
DR   UniPathway; UPA00087; UER00173.
DR   Proteomes; UP000007969; 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.
FT   CHAIN           1..389
FT                   /note="Phosphopentomutase"
FT                   /id="PRO_1000148239"
FT   BINDING         10
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT   BINDING         287
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT   BINDING         323
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT   BINDING         324
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT   BINDING         335
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
SQ   SEQUENCE   389 AA;  43019 MW;  C76CDB855E9C8BBB CRC64;
     MERVILIVFD SVGIGELPDA KEYGDVGSNT LGNISKAAGG LEIPTLYKLG IGNIQGVENL
     RRCEKPIGSF GKCAELSKGK DTVTGHWEMA GIVLKTPLNT YPQGFPEDII EEFQVKIGRK
     VLGNKVASGT EIINELGKEH VDTGYPIVYT SADSVFQVAA HEKIIPVEEL YKMCKIAREM
     LLGDRTVGRV IARPFIYDKG KYVRTSNRKD FALDPPGKTM LDYIKEVGLD VMAVGKIEDI
     YNKRGITEAV HIKNNMDGID KTLGYMKKNK SGLIFANLVD FDMLYGHRND TEGYAKALVE
     ADKRIPEIIS NMNEEDVLII TADHGCDPTT KSTDHSREYI PVLVYGKNLK AGVDIGIRKS
     YSDIGKTILE LLDIKNNLQG IGFKDLINK