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Database: UniProt
Entry: A0A172TMH6_9BACL
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ID   A0A172TMH6_9BACL        Unreviewed;       391 AA.
AC   A0A172TMH6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   ORFNames=SY83_18950 {ECO:0000313|EMBL:ANE48027.1};
OS   Paenibacillus swuensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE48027.1, ECO:0000313|Proteomes:UP000076927};
RN   [1] {ECO:0000313|EMBL:ANE48027.1, ECO:0000313|Proteomes:UP000076927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY6 {ECO:0000313|EMBL:ANE48027.1,
RC   ECO:0000313|Proteomes:UP000076927};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Paenibacillus swuensis/DY6/whole genome sequencing.";
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; CP011388; ANE48027.1; -; Genomic_DNA.
DR   RefSeq; WP_068609347.1; NZ_CP011388.1.
DR   AlphaFoldDB; A0A172TMH6; -.
DR   STRING; 1178515.SY83_18950; -.
DR   KEGG; pswu:SY83_18950; -.
DR   PATRIC; fig|1178515.4.peg.3829; -.
DR   OrthoDB; 9769930at2; -.
DR   UniPathway; UPA00087; UER00173.
DR   Proteomes; UP000076927; 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; 3.40.720.10; 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:ANE48027.1};
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:UP000076927}.
FT   DOMAIN          5..377
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   BINDING         12
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         290
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         326
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         327
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         338
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
SQ   SEQUENCE   391 AA;  42547 MW;  A2B9BCCF069BA729 CRC64;
     MRFNRIGVIV LDSVGIGELP DAESFGDLGS HTLGHIAEQV PSMALPNLKA LGLGNIEAFG
     TVQKVDKPLA YFGKMAEASV GKDTMTGHWE LMGLKITTPF NTYPDGFPPA LLEAFERETG
     RKVLCNRPAS GTEVLDEYGE EQMKTGAWIV YTSADSVFQI AAHEDIIPLE ELYKACEIAR
     RLTLQEEFSV GRVIARPYIG SPGAFKRTPN RHDYAVVPPS KTVMNGVQEA GYDSISVGKI
     NDIFSGEGVT ASYPTKSNLD GIEKTIELLG TDFKGLLFTN LVDFDSLYGH RRDPVGYAKA
     LEEFDAYVPQ LLEKLGPEDL LMITADHGND PVHPGTDHTR EYVPLLVYSP QLTQPASLAI
     RTTFSDVGAT IADNFGAALP SNGTSFLNEL K
//
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