Q8DTU0 (DEOB_STRMU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphopentomutase
EC=5.4.2.7

Alternative name(s):
Phosphodeoxyribomutase

Gene names

Name:	deoB
Ordered Locus Names:	SMU_1233

Organism

Streptococcus mutans [Complete proteome] [HAMAP]

Taxonomic identifier

1309 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Phosphotransfer between the C1 and C5 carbon atoms of pentose By similarity. HAMAP MF_00740
Catalytic activity	Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate. HAMAP MF_00740 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-alpha-D-ribose 5-phosphate. HAMAP MF_00740
Cofactor	Binds 1 or 2 manganese ions Potential.
Pathway	Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II): step 1/3. HAMAP MF_00740
Subcellular location	Cytoplasm By similarity HAMAP MF_00740.
Sequence similarities	Belongs to the phosphopentomutase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding
Molecular function	Isomerase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cellular metabolic compound salvage Inferred from electronic annotation. Source: InterPro nucleotide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphopentomutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 403

403

Phosphopentomutase HAMAP MF_00740

PRO_0000199851

Sites

Metal binding

13

1

Manganese By similarity

Metal binding

303

1

Manganese By similarity

Metal binding

339

1

Manganese By similarity

Metal binding

340

1

Manganese By similarity

Metal binding

351

1

Manganese By similarity

Secondary structure

1

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403

Helix Strand Turn

Details...

Beta strand

5 – 12

8

Helix

23 – 25

3

Beta strand

26 – 28

3

Helix

33 – 35

3

Helix

38 – 45

8

Helix

51 – 56

6

Helix

58 – 60

3

Beta strand

77 – 84

8

Helix

92 – 99

8

Helix

117 – 127

11

Helix

133 – 135

3

Beta strand

158 – 162

5

Beta strand

164 – 171

8

Turn

174 – 176

3

Helix

179 – 192

14

Beta strand

201 – 206

6

Beta strand

222 – 225

4

Helix

233 – 239

7

Beta strand

243 – 247

5

Helix

250 – 253

4

Turn

254 – 258

5

Beta strand

260 – 262

3

Helix

269 – 281

13

Beta strand

287 – 294

8

Helix

296 – 300

5

Turn

301 – 305

5

Helix

307 – 326

20

Beta strand

332 – 337

6

Beta strand

339 – 341

3

Beta strand

346 – 350

5

Beta strand

356 – 361

6

Helix

378 – 386

9

Helix

399 – 402

4

Sequences

	Sequence		Length	Mass (Da)
	Q8DTU0 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: B5484DA8AA5B8E0B	FASTA	403	43,956
	10 20 30 40 50 60 MSTFNRIHLV VLDSVGIGAA PDANNFSNAG VPDGASDTLG HISKTVGLNV PNMAKIGLGN 70 80 90 100 110 120 IPRDTPLKTV PAENHPTGYV TKLEEVSLGK DTMTGHWEIM GLNITEPFDT FWNGFPEEII 130 140 150 160 170 180 SKIEKFSGRK VIREANKPYS GTAVIDDFGP RQMETGELII YTSADPVLQI AAHEDVIPLD 190 200 210 220 230 240 ELYRICEYAR SITLERPALL GRIIARPYVG KPRNFTRTAN RHDYALSPFA PTVLNKLADA 250 260 270 280 290 300 GVSTYAVGKI NDIFNGSGIT NDMGHNKSNS HGVDTLIKTM GLSAFTKGFS FTNLVDFDAL 310 320 330 340 350 360 YGHRRNAHGY RDCLHEFDER LPEIIAAMKV DDLLLITADH GNDPTYAGTD HTREYVPLLA 370 380 390 400 YSPSFTGNGV LPVGHYADIS ATIADNFGVD TAMIGESFLD KLI

References

[1]

"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen." Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J. Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed: 12397186] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700610 / UA159 / Serotype c.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE014133 Genomic DNA. Translation: AAN58918.1.

RefSeq

NP_721612.1. NC_004350.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3M7V	X-ray	2.00	A/B	2-403	[»]

ProteinModelPortal

Q8DTU0.

SMR

Q8DTU0. Positions 2-403.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBSTRT00000014099; EBSTRP00000013581; EBSTRG00000014099.

GeneID

1028530.

GenomeReviews

Gene locus SMU_1233 in contig AE014133_GR.

KEGG

smu:SMU_1233.

NMPDR

fig|210007.1.peg.1125.

PATRIC

19664553. VBIStrMut61772_1106.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000027299.

HOGENOM

HBG644230.

OMA

KPICYTS.

ProtClustDB

PRK05362.

Enzyme and pathway databases

BioCyc

SMUT210007:SMU_1233-MONOMER.

Family and domain databases

HAMAP

MF_00740. Phosphopentomut.
[Tree]

InterPro

IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR010045. DeoB.
IPR006124. Metalloenzyme.
IPR024052. Phosphopentomutase_DeoB_cap.
[Graphical view]

Gene3D

G3DSA:3.40.720.10. Alk_phosphtse. 2 hits.
G3DSA:3.30.70.1250. G3DSA:3.30.70.1250. 1 hit.

KO

K01839.

Pfam

PF01676. Metalloenzyme. 1 hit.
[Graphical view]

PIRSF

PIRSF001491. Ppentomutase. 1 hit.

SUPFAM

SSF53649. Alkaline_phosphatase_core. 1 hit.
SSF143856. SSF143856. 1 hit.

TIGRFAMs

TIGR01696. DeoB. 1 hit.

ProtoNet

Search...

Entry information

Entry name

DEOB_STRMU

Accession

Primary (citable) accession number: Q8DTU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program