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C3TD52 (C3TD52_ECOLX) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 12. 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:
D-amino acid dehydrogenase small subunit 1 HAMAP MF_01202

EC=1.4.99.1 HAMAP MF_01202
Gene names
Name:dadA1 HAMAP MF_01202
ORF Names:ECs1684 EMBL ACI84636.1
OrganismEscherichia coli EMBL ACI84636.1
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Oxidative deamination of D-amino acids By similarity. SAAS SAAS023080 HAMAP MF_01202

Catalytic activity

A D-amino acid + H2O + acceptor = a 2-oxo acid + NH3 + reduced acceptor. SAAS SAAS023080 HAMAP MF_01202

Cofactor

FAD By similarity. SAAS SAAS023080 HAMAP MF_01202

Pathway

Amino-acid degradation; D-alanine degradation; NH(3) and pyruvate from D-alanine: step 1/1. HAMAP MF_01202

Subunit structure

Heterodimer of a small and a large subunit By similarity. SAAS SAAS023080 HAMAP MF_01202

Sequence similarities

Belongs to the DadA oxidoreductase family. HAMAP MF_01202

Sequences

Sequence LengthMass (Da)Tools
C3TD52 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: EE747358845B6280

FASTA43247,607
        10         20         30         40         50         60 
MRVVILGSGV VGVASAWYLN QAGHEVTVID REPGAALETS AANAGQISPG YAAPWAAPGV 

        70         80         90        100        110        120 
PLKAIKWMFQ RHAPLAVRLD GTQFQLKWMW QMLRNCDTSH YMENKGRMVR LAEYSRDCLK 

       130        140        150        160        170        180 
ALRAETNIQY EGRQGGTLQL FRTEQQYENA TRDIAVLEDA GVPYQLLESS RLAEVEPALA 

       190        200        210        220        230        240 
EVAHKLTGGL QLPNDETGDC QLFTQNLARM AEQAGVKFRF NTPVDQLLCD GEQIYGVKCG 

       250        260        270        280        290        300 
DEVIKADAYV MAFGSYSTAM LKGIVDIPVY PLKGYSLTIP IAQEDGAPVS TILDETYKIA 

       310        320        330        340        350        360 
ITRFDNRIRV GGMAEIVGFN TELLQPRRET LEMVVRDLYP RGGHVEQATF WTGLRPMTPD 

       370        380        390        400        410        420 
GTPVVGRTRF KNLWLNTGHG TLGWTMACGS GQLLSDLLSG RTPAIPYEDL SVARYSRGFT 

       430 
PSRPGHLHGA HS 

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References

[1]"A precise reconstruction of the emergence and constrained radiations of Escherichia coli O157 portrayed by backbone concatenomic analysis."
Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J., Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E., Sawyer S.A., Whittam T.S., Tarr P.I.
Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009) [PubMed: 19439656] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 493/89 EMBL ACI84636.1, 86-24 EMBL ACI84637.1, 87-14 EMBL ACI84638.1 and TW14359 EMBL ACI84640.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EU902090 Genomic DNA. Translation: ACI84636.1.
EU902091 Genomic DNA. Translation: ACI84637.1.
EU902092 Genomic DNA. Translation: ACI84638.1.
EU902094 Genomic DNA. Translation: ACI84640.1.

3D structure databases

ProteinModelPortalC3TD52.
SMRC3TD52. Positions 2-34, 200-257.
ModBaseSearch...

Proteomic databases

PRIDEC3TD52.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01202. DadA.
[Tree]
InterProIPR023080. D-aa_DH_ssu_DadA.
IPR006076. FAD-dep_OxRdtase.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC3TD52_ECOLX
AccessionPrimary (citable) accession number: C3TD52
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: January 25, 2012
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)