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Database: UniProt
Entry: A0A1E8F252_9CLOT
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ID   A0A1E8F252_9CLOT        Unreviewed;       390 AA.
AC   A0A1E8F252;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Phosphopentomutase {ECO:0000256|HAMAP-Rule:MF_00740};
DE            EC=5.4.2.7 {ECO:0000256|HAMAP-Rule:MF_00740};
DE   AltName: Full=Phosphodeoxyribomutase {ECO:0000256|HAMAP-Rule:MF_00740};
GN   Name=deoB {ECO:0000256|HAMAP-Rule:MF_00740,
GN   ECO:0000313|EMBL:OFI07612.1};
GN   ORFNames=CLOACE_02160 {ECO:0000313|EMBL:OFI07612.1};
OS   Clostridium acetireducens DSM 10703.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121290 {ECO:0000313|EMBL:OFI07612.1, ECO:0000313|Proteomes:UP000175744};
RN   [1] {ECO:0000313|EMBL:OFI07612.1, ECO:0000313|Proteomes:UP000175744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10703 {ECO:0000313|EMBL:OFI07612.1,
RC   ECO:0000313|Proteomes:UP000175744};
RA   Poehlein A., Fluechter S., Duerre P., Daniel R.;
RT   "Genome sequence of Clostridium acetireducens DSM 10703.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of
CC       pentose. {ECO:0000256|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; Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00740};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00740};
CC       Note=Binds 1 or 2 manganese ions. {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_00740}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00740}.
CC   -!- SIMILARITY: Belongs to the phosphopentomutase family.
CC       {ECO:0000256|ARBA:ARBA00010373, ECO:0000256|HAMAP-Rule:MF_00740}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OFI07612.1}.
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DR   EMBL; LZFO01000002; OFI07612.1; -; Genomic_DNA.
DR   RefSeq; WP_070109189.1; NZ_LZFO01000002.1.
DR   AlphaFoldDB; A0A1E8F252; -.
DR   STRING; 1121290.CLAOCE_02160; -.
DR   PATRIC; fig|1121290.3.peg.219; -.
DR   OrthoDB; 9769930at2; -.
DR   UniPathway; UPA00087; UER00173.
DR   Proteomes; UP000175744; Unassembled WGS sequence.
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; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   Gene3D; 3.30.70.1250; Phosphopentomutase; 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   NCBIfam; TIGR01696; deoB; 1.
DR   PANTHER; PTHR21110; PHOSPHOPENTOMUTASE; 1.
DR   PANTHER; PTHR21110:SF0; PHOSPHOPENTOMUTASE; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   PIRSF; PIRSF001491; Ppentomutase; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   SUPFAM; SSF143856; DeoB insert domain-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00740};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00740, ECO:0000313|EMBL:OFI07612.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00740};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00740}; Reference proteome {ECO:0000313|Proteomes:UP000175744}.
FT   DOMAIN          4..376
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   BINDING         11
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         288
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         324
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         325
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         336
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
SQ   SEQUENCE   390 AA;  43153 MW;  DE21A72CD63D74CF CRC64;
     MINRVILIIL DSVGIGELPD ATEYGDEGSN TLENISRKLG GLSLPNMESI GLGHINGVKE
     IKKQNNVTGA FGKCAEMSKG KDTVTGHWEI AGLVLKKSLK TYPKGFPKDI IDEFKNKIGR
     NILGNKVASG TEIIKELGNE HIKTGYPIVY TSADSVFQIA AHEEVIKLEE LYNMCKIARK
     MLTGDRTVGR IIARPFIGEK GDYTRTSNRK DFALDPFGKT MLDYIKESGS NVMAVGKIND
     IYNGKGITDA VHIDNNMDGV DKTLEYMKTN KKGLIFTNLV DFDMLYGHRN NVEGYANALI
     EFDNRLPEII NEMEKEDVII LTADHGCDPT TPSTDHSREY VPVLVYGENI KSGVNIGTRK
     CYCDIGKTVL DLLSVKNNLF GESFAKDIVK
//
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