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Protein

Phosphopentomutase

Gene

deoB

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Phosphotransfer between the C1 and C5 carbon atoms of pentose.UniRule annotation

Catalytic activityi

Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate.UniRule annotation
2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-alpha-D-ribose 5-phosphate.UniRule annotation

Cofactori

Mn2+UniRule annotationNote: Binds 1 or 2 manganese ions.UniRule annotation

Pathwayi: 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II).UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Phosphopentomutase (deoB)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi13ManganeseUniRule annotation1
Metal bindingi303ManganeseUniRule annotation1
Metal bindingi339ManganeseUniRule annotation1
Metal bindingi340ManganeseUniRule annotation1
Metal bindingi351ManganeseUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00087; UER00173.

Names & Taxonomyi

Protein namesi
Recommended name:
PhosphopentomutaseUniRule annotation (EC:5.4.2.7UniRule annotation)
Alternative name(s):
PhosphodeoxyribomutaseUniRule annotation
Gene namesi
Name:deoBUniRule annotation
Ordered Locus Names:SMU_1233
OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
Taxonomic identifieri210007 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000002512 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001998511 – 403PhosphopentomutaseAdd BLAST403

Interactioni

Protein-protein interaction databases

STRINGi210007.SMU_1233.

Structurei

Secondary structure

1403
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 12Combined sources9
Helixi23 – 25Combined sources3
Beta strandi26 – 28Combined sources3
Helixi33 – 35Combined sources3
Helixi38 – 45Combined sources8
Helixi51 – 56Combined sources6
Helixi58 – 60Combined sources3
Beta strandi77 – 84Combined sources8
Helixi92 – 99Combined sources8
Helixi117 – 127Combined sources11
Helixi133 – 135Combined sources3
Beta strandi136 – 138Combined sources3
Helixi141 – 155Combined sources15
Beta strandi158 – 162Combined sources5
Beta strandi164 – 173Combined sources10
Turni174 – 176Combined sources3
Helixi179 – 191Combined sources13
Beta strandi201 – 211Combined sources11
Beta strandi214 – 217Combined sources4
Beta strandi222 – 225Combined sources4
Helixi233 – 239Combined sources7
Beta strandi243 – 247Combined sources5
Helixi250 – 254Combined sources5
Turni255 – 258Combined sources4
Beta strandi260 – 262Combined sources3
Helixi269 – 281Combined sources13
Beta strandi287 – 294Combined sources8
Helixi296 – 299Combined sources4
Turni300 – 305Combined sources6
Helixi307 – 326Combined sources20
Beta strandi332 – 337Combined sources6
Beta strandi339 – 341Combined sources3
Beta strandi346 – 350Combined sources5
Beta strandi356 – 361Combined sources6
Helixi378 – 387Combined sources10
Helixi399 – 402Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3M7VX-ray2.00A/B2-403[»]
4N7TX-ray2.00A/B2-403[»]
ProteinModelPortaliQ8DTU0.
SMRiQ8DTU0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8DTU0.

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphopentomutase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CZG. Bacteria.
COG1015. LUCA.
KOiK01839.
OMAiYLGNCHA.
PhylomeDBiQ8DTU0.

Family and domain databases

Gene3Di3.30.70.1250. 1 hit.
3.40.720.10. 2 hits.
HAMAPiMF_00740. Phosphopentomut. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR010045. DeoB.
IPR006124. Metalloenzyme.
IPR024052. Phosphopentomutase_DeoB_cap.
[Graphical view]
PfamiPF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF001491. Ppentomutase. 1 hit.
SUPFAMiSSF143856. SSF143856. 1 hit.
SSF53649. SSF53649. 2 hits.
TIGRFAMsiTIGR01696. deoB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8DTU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTFNRIHLV VLDSVGIGAA PDANNFSNAG VPDGASDTLG HISKTVGLNV
60 70 80 90 100
PNMAKIGLGN IPRDTPLKTV PAENHPTGYV TKLEEVSLGK DTMTGHWEIM
110 120 130 140 150
GLNITEPFDT FWNGFPEEII SKIEKFSGRK VIREANKPYS GTAVIDDFGP
160 170 180 190 200
RQMETGELII YTSADPVLQI AAHEDVIPLD ELYRICEYAR SITLERPALL
210 220 230 240 250
GRIIARPYVG KPRNFTRTAN RHDYALSPFA PTVLNKLADA GVSTYAVGKI
260 270 280 290 300
NDIFNGSGIT NDMGHNKSNS HGVDTLIKTM GLSAFTKGFS FTNLVDFDAL
310 320 330 340 350
YGHRRNAHGY RDCLHEFDER LPEIIAAMKV DDLLLITADH GNDPTYAGTD
360 370 380 390 400
HTREYVPLLA YSPSFTGNGV LPVGHYADIS ATIADNFGVD TAMIGESFLD

KLI
Length:403
Mass (Da):43,956
Last modified:March 1, 2003 - v1
Checksum:iB5484DA8AA5B8E0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014133 Genomic DNA. Translation: AAN58918.1.
RefSeqiNP_721612.1. NC_004350.2.
WP_002263210.1. NC_004350.2.

Genome annotation databases

EnsemblBacteriaiAAN58918; AAN58918; SMU_1233.
GeneIDi1028530.
KEGGismu:SMU_1233.
PATRICi19664553. VBIStrMut61772_1106.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014133 Genomic DNA. Translation: AAN58918.1.
RefSeqiNP_721612.1. NC_004350.2.
WP_002263210.1. NC_004350.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3M7VX-ray2.00A/B2-403[»]
4N7TX-ray2.00A/B2-403[»]
ProteinModelPortaliQ8DTU0.
SMRiQ8DTU0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi210007.SMU_1233.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN58918; AAN58918; SMU_1233.
GeneIDi1028530.
KEGGismu:SMU_1233.
PATRICi19664553. VBIStrMut61772_1106.

Phylogenomic databases

eggNOGiENOG4105CZG. Bacteria.
COG1015. LUCA.
KOiK01839.
OMAiYLGNCHA.
PhylomeDBiQ8DTU0.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00173.

Miscellaneous databases

EvolutionaryTraceiQ8DTU0.

Family and domain databases

Gene3Di3.30.70.1250. 1 hit.
3.40.720.10. 2 hits.
HAMAPiMF_00740. Phosphopentomut. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR010045. DeoB.
IPR006124. Metalloenzyme.
IPR024052. Phosphopentomutase_DeoB_cap.
[Graphical view]
PfamiPF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF001491. Ppentomutase. 1 hit.
SUPFAMiSSF143856. SSF143856. 1 hit.
SSF53649. SSF53649. 2 hits.
TIGRFAMsiTIGR01696. deoB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDEOB_STRMU
AccessioniPrimary (citable) accession number: Q8DTU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.