DEOB_STRMU
ID DEOB_STRMU Reviewed; 403 AA.
AC Q8DTU0;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
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}; OrderedLocusNames=SMU_1233;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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}.
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DR EMBL; AE014133; AAN58918.1; -; Genomic_DNA.
DR RefSeq; NP_721612.1; NC_004350.2.
DR RefSeq; WP_002263210.1; NC_004350.2.
DR PDB; 3M7V; X-ray; 2.00 A; A/B=2-403.
DR PDB; 4N7T; X-ray; 2.00 A; A/B=2-403.
DR PDBsum; 3M7V; -.
DR PDBsum; 4N7T; -.
DR AlphaFoldDB; Q8DTU0; -.
DR SMR; Q8DTU0; -.
DR STRING; 210007.SMU_1233; -.
DR PRIDE; Q8DTU0; -.
DR EnsemblBacteria; AAN58918; AAN58918; SMU_1233.
DR GeneID; 66817381; -.
DR KEGG; smu:SMU_1233; -.
DR PATRIC; fig|210007.7.peg.1106; -.
DR eggNOG; COG1015; Bacteria.
DR HOGENOM; CLU_053861_0_0_9; -.
DR OMA; YLGNCHA; -.
DR PhylomeDB; Q8DTU0; -.
DR UniPathway; UPA00087; UER00173.
DR EvolutionaryTrace; Q8DTU0; -.
DR Proteomes; UP000002512; 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; 3.30.70.1250; -; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..403
FT /note="Phosphopentomutase"
FT /id="PRO_0000199851"
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 STRAND 4..12
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:4N7T"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 201..211
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:4N7T"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 269..281
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:4N7T"
FT TURN 300..305
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 307..326
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:4N7T"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:4N7T"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:4N7T"
SQ SEQUENCE 403 AA; 43956 MW; B5484DA8AA5B8E0B CRC64;
MSTFNRIHLV VLDSVGIGAA PDANNFSNAG VPDGASDTLG HISKTVGLNV PNMAKIGLGN
IPRDTPLKTV PAENHPTGYV TKLEEVSLGK DTMTGHWEIM GLNITEPFDT FWNGFPEEII
SKIEKFSGRK VIREANKPYS GTAVIDDFGP RQMETGELII YTSADPVLQI AAHEDVIPLD
ELYRICEYAR SITLERPALL GRIIARPYVG KPRNFTRTAN RHDYALSPFA PTVLNKLADA
GVSTYAVGKI NDIFNGSGIT NDMGHNKSNS HGVDTLIKTM GLSAFTKGFS FTNLVDFDAL
YGHRRNAHGY RDCLHEFDER LPEIIAAMKV DDLLLITADH GNDPTYAGTD HTREYVPLLA
YSPSFTGNGV LPVGHYADIS ATIADNFGVD TAMIGESFLD KLI
