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A5I237 (DEOC_CLOBH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. 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

Short name=DERA
EC=4.1.2.4
Alternative name(s):
2-deoxy-D-ribose 5-phosphate aldolase
Phosphodeoxyriboaldolase
Short name=Deoxyriboaldolase
Gene names
Name:deoC
Ordered Locus Names:CBO1563, CLC_1594
OrganismClostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
Taxonomic identifier441771 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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
Reference 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 – 212212Deoxyribose-phosphate aldolase HAMAP MF_00114
PRO_1000057749

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A5I237 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 4AC30E951CCFBDCB

FASTA21223,060
        10         20         30         40         50         60 
MKLSKYIDHT LLKPQATEKD ILKLIEEAKT YDFASVCVNP SWVKLAYENL KDTDVKVCTV 

        70         80         90        100        110        120 
VGFPLGATST ASKVYETKVA IKDGADEIDM VISVGQLKSG NDEYVKEEIK KIVEASKNKL 

       130        140        150        160        170        180 
VKVIIETCLL TEEEKVKACT LSKEAGADYV KTSTGFSTGG AKPEDIKLMR ETVGKDMGVK 

       190        200        210 
ASGGIHTREE MEVMIENGAT RIGASCGVEL VK 

« Hide

References

[1]"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes."
Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. expand/collapse author list , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J.
Genome Res. 17:1082-1092(2007) [PubMed: 17519437] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.
[2]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed: 18060065] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000727 Genomic DNA. Translation: ABS38596.1.
AM412317 Genomic DNA. Translation: CAL83102.1.
RefSeqYP_001254070.1. NC_009495.1.
YP_001387454.1. NC_009698.1.

3D structure databases

ProteinModelPortalA5I237.
SMRA5I237. Positions 7-212.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5I237.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5185818.
5400733.
GenomeReviewsGene locus CBO1563 in contig AM412317_GR.
Gene locus CLC_1594 in contig CP000727_GR.
KEGGcbh:CLC_1594.
cbo:CBO1563.
PATRIC19365191. VBICloBot22612_1539.

Phylogenomic databases

eggNOGCOG0274.
HOGENOMHBG636421.
OMACLEAREN.
ProtClustDBPRK00507.

Enzyme and pathway databases

BioCycCBOT36826:CBO1563-MONOMER.
CBOT441771:CLC_1594-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 nameDEOC_CLOBH
AccessionPrimary (citable) accession number: A5I237
Secondary accession number(s): A7G3T9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 26, 2007
Last modified: December 14, 2011
This is version 36 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