DEOB_STRTR
ID DEOB_STRTR Reviewed; 403 AA.
AC Q9EUQ2; Q8KUL6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
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};
OS Streptococcus thermophilus.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-250 / LMG 18311;
RA Almiron-Roig E., Griffin A.M., Gasson M.J.;
RT "Cloning and sequence analysis of a region involved in nucleotide
RT metabolism in Streptococcus thermophilus.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MR-1C;
RX PubMed=12647947; DOI=10.3168/jds.s0022-0302(03)73619-4;
RA Broadbent J.R., McMahon D.J., Welker D.L., Oberg C.J., Moineau S.;
RT "Biochemistry, genetics, and applications of exopolysaccharide production
RT in Streptococcus thermophilus: a review.";
RL J. Dairy Sci. 86:407-423(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ251799; CAC21180.1; -; Genomic_DNA.
DR EMBL; AF448249; AAM93387.1; -; Genomic_DNA.
DR RefSeq; WP_002948787.1; NZ_LT604076.1.
DR RefSeq; WP_014608357.1; NZ_WMLD01000003.1.
DR AlphaFoldDB; Q9EUQ2; -.
DR SMR; Q9EUQ2; -.
DR STRING; 322159.STER_1077; -.
DR GeneID; 66898918; -.
DR PATRIC; fig|1308.47.peg.1084; -.
DR eggNOG; COG1015; Bacteria.
DR UniPathway; UPA00087; UER00173.
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..403
FT /note="Phosphopentomutase"
FT /id="PRO_0000199858"
FT BINDING 13
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT BINDING 303
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT BINDING 339
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT BINDING 340
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT BINDING 351
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT CONFLICT 135..137
FT /note="SNR -> ANK (in Ref. 2; AAM93387)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="S -> C (in Ref. 2; AAM93387)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 44419 MW; 256BC5AC302CE1DC CRC64;
MSKFNRMHLI VLDSVGIGAA PDANNFVNAG VPDGASDTLG HISKTVGLNV PNMAKLGLGN
IPREQPLKTV PAESNPTGYA TKLEEVSLGK DTMTGHWEIM GLNITEPFDT FWNGFPEEIL
TQIEEFSGRK VIRESNRPYS GTAVIDDFGP RQMETGELII YTSADPVLQI AAHEDIIPVE
ELYRICEFAR SITLERPALL GRIIARPYVG EPGNFTRTSN RRDLAISPFA PTVLDKLNEA
GIDTYSVGKI SDIFNGEGIN HDMGHNKSNN HGVDNLIKAM TSEDFKHGFS FTNLVDFDAL
YGHRRNPQGY RDCLHEFDER LPEIIAAMKE DDLLMITADH GNDPTYAGTD HTREYIPFLA
YSPSFKSSGL IPVGHFADIS ATIADNFGVE KAMIGESFLD KLV
