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Database: UniProt
Entry: A0A285ILG1_9RHOB
LinkDB: A0A285ILG1_9RHOB
Original site: A0A285ILG1_9RHOB 
ID   A0A285ILG1_9RHOB        Unreviewed;       406 AA.
AC   A0A285ILG1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN06297129_1569 {ECO:0000313|EMBL:SNY48774.1};
OS   Pseudooceanicola antarcticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=1247613 {ECO:0000313|EMBL:SNY48774.1, ECO:0000313|Proteomes:UP000231655};
RN   [1] {ECO:0000313|EMBL:SNY48774.1, ECO:0000313|Proteomes:UP000231655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12662 {ECO:0000313|EMBL:SNY48774.1,
RC   ECO:0000313|Proteomes:UP000231655};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OBEA01000002; SNY48774.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285ILG1; -.
DR   OrthoDB; 9769930at2; -.
DR   UniPathway; UPA00087; UER00173.
DR   Proteomes; UP000231655; 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};
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          3..396
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   BINDING         10
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         309
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         345
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         346
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT   BINDING         357
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
SQ   SEQUENCE   406 AA;  42622 MW;  6F68E6037DBBEDF8 CRC64;
     MSRAFLVVMD SVGIGGAPDA DRFFNGSTPD SGANTLAHIA EACAAGRADE GRSGPLHLPN
     LAALGLGEAV TLASGAAAPG LAAPVTGLYA AASEVSPGKD TPSGHWELAG VPVPWDWHYF
     PDTTPSFPDE LVQEVCKLAG VDGILGNCHA SGTRIIADLG EEHMRTGKPI CYTSADSVFQ
     IAAHEESFGN QRLQELCKAL APVLHKMKVG RVISRPFVGE PGNFTRTANR RDYAVALPSP
     GLCDWVQAAG GKVHGVGKIG DIFSMQGIDD VVKGPDSDLM DQLDRLVEEA EEGSLTFANF
     VEFDSLYGHR RDIAGYARAL EWFDARIGQV IAGLRPGDML LITADHGNDP SWTGSDHTRE
     RVPVLIAGLS DRGAGGNLGL CQFTDVAATV AAHLDVPALG PGRSLI
//
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