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Database: UniProt
Entry: B9YCM6_9FIRM
LinkDB: B9YCM6_9FIRM
Original site: B9YCM6_9FIRM 
ID   B9YCM6_9FIRM            Unreviewed;       395 AA.
AC   B9YCM6;
DT   14-APR-2009, integrated into UniProtKB/TrEMBL.
DT   14-APR-2009, sequence version 1.
DT   24-JAN-2024, entry version 76.
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:EEF66256.1};
GN   ORFNames=HOLDEFILI_03587 {ECO:0000313|EMBL:EEF66256.1};
OS   Holdemania filiformis DSM 12042.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Holdemania.
OX   NCBI_TaxID=545696 {ECO:0000313|EMBL:EEF66256.1, ECO:0000313|Proteomes:UP000005950};
RN   [1] {ECO:0000313|EMBL:EEF66256.1, ECO:0000313|Proteomes:UP000005950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF66256.1,
RC   ECO:0000313|Proteomes:UP000005950};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEF66256.1, ECO:0000313|Proteomes:UP000005950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF66256.1,
RC   ECO:0000313|Proteomes:UP000005950};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Holdemania filiformis DSM 12042.";
RL   Submitted (FEB-2009) 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:EEF66256.1}.
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DR   EMBL; ACCF01000226; EEF66256.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9YCM6; -.
DR   STRING; 545696.HOLDEFILI_03587; -.
DR   eggNOG; COG1015; Bacteria.
DR   HOGENOM; CLU_053861_0_0_9; -.
DR   UniPathway; UPA00087; UER00173.
DR   Proteomes; UP000005950; 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:EEF66256.1};
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}.
FT   DOMAIN          6..382
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   BINDING         14
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         294
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         330
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         331
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         342
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
SQ   SEQUENCE   395 AA;  44245 MW;  F8D956F1EB13C2B0 CRC64;
     MTMKYKRIFT IVMDSVGCGE MPDAEHYGDR GADTIGHIAK TVGGLTMPAM EKLGYGNLHS
     ILGVEPQRDP QGYYTKMLEA SVGKDTMTGH WEMMGLYIDK PFQTFTDTGF PQELIDELEK
     RTGYKIVGNK SASGTEILDE LGEHHMKTKD MIVYTSADSV LQIAAHEEVF GLEELYRCCE
     IARELTMKDE WKVGRVIARP FIGEGKGHFT RTSNRHDLAL KPFGRTVLNE LKDKGFDVIS
     VGKIKDIFDG EGITEAYKST SSHHGMEQTI ELTQKDFTGL CFVNLVDFDA KWGHRRNPQG
     YAQELEDYDQ LLTTFLGQLR EEDLVIITAD HGNDPCHTGT DHTREMVPLI LYSPSHQGSG
     LLPLANTFAN LGATVAENFE VSMPEYGESY LSYLK
//
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