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D2TQ92 (D2TQ92_CITRI) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
5-keto-4-deoxy-D-glucarate aldolase HAMAP-Rule MF_01291
Short name=KDGluc aldolase HAMAP-Rule MF_01291
Short name=KDGlucA HAMAP-Rule MF_01291
EC=4.1.2.20 HAMAP-Rule MF_01291
Alternative name(s):
2-dehydro-3-deoxy-D-glucarate aldolase HAMAP-Rule MF_01291
2-keto-3-deoxy-D-glucarate aldolase HAMAP-Rule MF_01291
5-dehydro-4-deoxy-D-glucarate aldolase HAMAP-Rule MF_01291
Alpha-keto-beta-deoxy-D-glucarate aldolase HAMAP-Rule MF_01291
Gene names
Name:garL HAMAP-Rule MF_01291 EMBL CBG91446.1
Ordered Locus Names:ROD_47531 EMBL CBG91446.1
OrganismCitrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280) [Complete proteome] [HAMAP] EMBL CBG91446.1
Taxonomic identifier637910 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Citrobacter ›

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible retro-aldol cleavage of both 5-keto-4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and tartronic semialdehyde By similarity. HAMAP-Rule MF_01291

Catalytic activity

2-dehydro-3-deoxy-D-glucarate = pyruvate + tartronate semialdehyde. HAMAP-Rule MF_01291

5-dehydro-4-deoxy-D-glucarate = pyruvate + tartronate semialdehyde. HAMAP-Rule MF_01291

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01291

Pathway

Carbohydrate acid metabolism; D-galactarate degradation; D-glycerate from D-galactarate: step 2/3. HAMAP-Rule MF_01291

Subunit structure

Homohexamer; trimer of dimers By similarity. HAMAP-Rule MF_01291

Sequence similarities

Belongs to the HpcH/HpaI aldolase family. KDGluc aldolase subfamily. HAMAP-Rule MF_01291

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site501Proton acceptor By similarity HAMAP-Rule MF_01291
Metal binding1531Magnesium By similarity HAMAP-Rule MF_01291
Metal binding1791Magnesium By similarity HAMAP-Rule MF_01291
Binding site1511Substrate By similarity HAMAP-Rule MF_01291
Binding site1781Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01291
Binding site1791Substrate By similarity HAMAP-Rule MF_01291
Site751Transition state stabilizer By similarity HAMAP-Rule MF_01291
Site891Increases basicity of active site His By similarity HAMAP-Rule MF_01291

Sequences

Sequence LengthMass (Da)Tools
D2TQ92 [UniParc].

Last modified March 2, 2010. Version 1.
Checksum: 0407C60D24E56A61

FASTA25627,350
        10         20         30         40         50         60 
MNNTIFPNKF KAALAAHQVQ IGCWSALASP ISTEVLGLAG FDWLVLDGEH APNDVSTFIP 

        70         80         90        100        110        120 
QLMALKGSAS APVVRVPTNE PVIIKRLLDI GFYNFLIPFV ETEEEAVNAV ASTRYPPEGI 

       130        140        150        160        170        180 
RGVSVSHRAN MFGTVPDYFA QSNKNITIIV QIESQQGVDN VDAIAATEGV DGIFVGPSDL 

       190        200        210        220        230        240 
AAALGHLGNA SHPDVQKAIQ HIFSRAKAHG KPCGILAPVE ADARRYLEWG ATFVAVGSDL 

       250 
GVFRSATQKL ADSFKK

« Hide

References

[1]"The Citrobacter rodentium genome sequence reveals convergent evolution with human pathogenic Escherichia coli."
Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N., Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L., Parkhill J., Dougan G., Frankel G., Thomson N.R.
J. Bacteriol. 192:525-538(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ICC168 EMBL CBG91446.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FN543502 Genomic DNA. Translation: CBG91446.1.
RefSeqYP_003368155.1. NC_013716.1.

3D structure databases

ProteinModelPortalD2TQ92.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBG91446; CBG91446; ROD_47531.
GeneID8713490.
KEGGcro:ROD_47531.
PATRIC32033158. VBICitRod33214_4525.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000179750.
KOK01630.
OMAGVSVAHR.

Enzyme and pathway databases

BioCycCROD637910:GJIG-4808-MONOMER.
UniPathwayUPA00565; UER00630.

Family and domain databases

Gene3D3.20.20.60. 1 hit.
HAMAPMF_01291. KDGluc_aldolase.
InterProIPR005000. Aldehyde-lyase_domain.
IPR017648. Dehyd-dGlucarate-aldolase_GarL.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamPF03328. HpcH_HpaI. 1 hit.
[Graphical view]
SUPFAMSSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR03239. GarL. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD2TQ92_CITRI
AccessionPrimary (citable) accession number: D2TQ92
Entry history
Integrated into UniProtKB/TrEMBL: March 2, 2010
Last sequence update: March 2, 2010
Last modified: May 29, 2013
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info