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B5Y8P0 (B5Y8P0_COPPD) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Phosphopentomutase HAMAP-Rule MF_00740

EC=5.4.2.7 HAMAP-Rule MF_00740
Alternative name(s):
Phosphodeoxyribomutase HAMAP-Rule MF_00740
Gene names
Name:deoB HAMAP-Rule MF_00740 EMBL ACI18211.1
Ordered Locus Names:COPRO5265_0790 EMBL ACI18211.1
OrganismCoprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / BT) [Complete proteome] [HAMAP] EMBL ACI18211.1
Taxonomic identifier309798 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermodesulfobiaceaeCoprothermobacter

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Phosphotransfer between the C1 and C5 carbon atoms of pentose By similarity. HAMAP-Rule MF_00740 SAAS SAAS006124

Catalytic activity

2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-alpha-D-ribose 5-phosphate. HAMAP-Rule MF_00740 SAAS SAAS006124

Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate. HAMAP-Rule MF_00740 SAAS SAAS006124

Cofactor

Binds 1 or 2 manganese ions By similarity. HAMAP-Rule MF_00740 SAAS SAAS006124

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-Rule MF_00740 SAAS SAAS006124

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00740 SAAS SAAS006124.

Sequence similarities

Belongs to the phosphopentomutase family. HAMAP-Rule MF_00740

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding171Manganese By similarity HAMAP-Rule MF_00740
Metal binding2901Manganese By similarity HAMAP-Rule MF_00740
Metal binding3261Manganese By similarity HAMAP-Rule MF_00740
Metal binding3271Manganese By similarity HAMAP-Rule MF_00740
Metal binding3391Manganese By similarity HAMAP-Rule MF_00740

Sequences

Sequence LengthMass (Da)Tools
B5Y8P0 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: A46D958A29C535D6

FASTA39343,934
        10         20         30         40         50         60 
MTMKEKVFKR VFLVVIDSFG VGAEPDWAEY GDDPSLNTAL HVIDDRPAPS FLWSRGLGYL 

        70         80         90        100        110        120 
LKEEPIKQPS VVAKLQELSK GKDSTTGHWE IAGLVMTTPF PTYPHGFPPE VMEEFERRIG 

       130        140        150        160        170        180 
TKTLGNFPAS GTEIIKQLGE EHMRTGYPIV YTSADSVFQI AAHEDVIPVE DLYRMCEIAR 

       190        200        210        220        230        240 
ELLTGDHAVA RVIARPFAGK PGEFYRTPRR RDFSLPPLGH TILDELVEKG IPVVAVGKIH 

       250        260        270        280        290        300 
DLFAGRGISQ SVHTENDAEG IKALQELSKT FQQRGLVFAN LVDSDMIYGH RRNVEGYYQN 

       310        320        330        340        350        360 
IMMIDEGLSL LYDNLTNEDL LIVTADHGND PTFPKHTDHT REYVSFIACS PSFTEGSFLG 

       370        380        390 
TLRGYVHIAQ TVIEALGVES ARKWGRTLLK EDV 

« Hide

References

[1]"The complete genome sequence of Coprothermobacter proteolyticus strain ATCC 5245 / DSM 5265 / BT."
Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35245 / DSM 5265 / BT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001145 Genomic DNA. Translation: ACI18211.1.
RefSeqYP_002247137.1. NC_011295.1.

3D structure databases

ProteinModelPortalB5Y8P0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING309798.COPRO5265_0790.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI18211; ACI18211; COPRO5265_0790.
GeneID6943937.
KEGGcpo:COPRO5265_0790.
PATRIC21474414. VBICopPro72829_0750.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1015.
HOGENOMHOG000008159.
KOK01839.
OMAIRTKDNM.
OrthoDBEOG6R5C7J.

Enzyme and pathway databases

BioCycCPRO309798:GH7M-783-MONOMER.
UniPathwayUPA00087; UER00173.

Family and domain databases

Gene3D3.30.70.1250. 1 hit.
3.40.720.10. 2 hits.
HAMAPMF_00740. Phosphopentomut.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR010045. DeoB.
IPR006124. Metalloenzyme.
IPR024052. Phosphopentomutase_DeoB_cap.
[Graphical view]
PfamPF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFPIRSF001491. Ppentomutase. 1 hit.
SUPFAMSSF143856. SSF143856. 1 hit.
SSF53649. SSF53649. 2 hits.
TIGRFAMsTIGR01696. deoB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB5Y8P0_COPPD
AccessionPrimary (citable) accession number: B5Y8P0
Entry history
Integrated into UniProtKB/TrEMBL: November 25, 2008
Last sequence update: November 25, 2008
Last modified: June 11, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)