Skip Header

Contribute Send feedback
Read comments (?) or add your own

P99102 (DEOC1_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxyribose-phosphate aldolase 1

Short name=DERA 1
EC=4.1.2.4
Alternative name(s):
2-deoxy-D-ribose 5-phosphate aldolase 1
Phosphodeoxyriboaldolase 1
Short name=Deoxyriboaldolase 1
Gene names
Name:deoC1
Synonyms:dra
Ordered Locus Names:SA0133
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate By similarity. HAMAP MF_00114

Catalytic activity

2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. HAMAP MF_00114

Pathway

Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2. HAMAP MF_00114

Subcellular location

Cytoplasm By similarity HAMAP MF_00114.

Sequence similarities

Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processdeoxyribonucleotide catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondeoxyribose-phosphate aldolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Deoxyribose-phosphate aldolase 1 HAMAP MF_00114
PRO_0000057259

Sites

Active site1511Schiff-base intermediate with acetaldehyde By similarity
Active site1801 By similarity

Sequences

Sequence LengthMass (Da)Tools
P99102 [UniParc].

Last modified April 26, 2004. Version 1.
Checksum: A77DAC561C6B70A3

FASTA22023,472
        10         20         30         40         50         60 
MKFEKYIDHT LLKPESTRTQ IDQIIDEAKA YNFKSVCVNP THVKYAAERL ADSEVLVCTV 

        70         80         90        100        110        120 
IGFPLGASTT ATKAFETEDA IQNGADEIDM VINIGALKDG RFDDVQQDIE AVVKAAKGHT 

       130        140        150        160        170        180 
VKVIIETVLL DHDEIVKASE LTKAAGADFV KTSTGFAGGG ATAEDVKLMK DTVGADVEVK 

       190        200        210        220 
ASGGVRNLED FNKMVEAGAT RIGASAGVQI MQGLEADSDY 

« Hide

References

« Hide 'large scale' references
[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.
[2]"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth."
Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.
J. Microbiol. Methods 60:247-257(2005) [PubMed: 15590099] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Strain: N315.
[3]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000018 Genomic DNA. Translation: BAB41353.1.
PIRF89774.
RefSeqNP_373375.1. NC_002745.2.

3D structure databases

ProteinModelPortalP99102.
SMRP99102. Positions 2-217.
ModBaseSearch...

Protein-protein interaction databases

STRINGP99102.

2D gel databases

SWISS-2DPAGEP99102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000000767; EBSTAP00000000767; EBSTAG00000000767.
GeneID1122908.
GenomeReviewsGene locus SA0133 in contig BA000018_GR.
KEGGsau:SA0133.
PATRIC19572297. VBIStaAur116463_0138.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0274.
GeneTreeEBGT00050000024092.
HOGENOMHBG636421.
OMAIDHTNLK.
PhylomeDBP99102.
ProtClustDBPRK00507.

Enzyme and pathway databases

BioCycSAUR158879:SA0133-MONOMER.

Family and domain databases

HAMAPMF_00114. DeoC_type1.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/AroFGH_arch.
IPR022979. Deoxyribose_phosphate_aldo_1.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK01619.
PANTHERPTHR10889. DeoC. 1 hit.
PfamPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFPIRSF001357. DeoC. 1 hit.
TIGRFAMsTIGR00126. DeoC. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEOC1_STAAN
AccessionPrimary (citable) accession number: P99102
Secondary accession number(s): Q99X77
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families