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Reviewed, UniProtKB/Swiss-Prot Q7NWR6 (DADA_CHRVO)

Last modified June 16, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    D-amino acid dehydrogenase small subunit
    EC=1.4.99.1
Gene names
Name: dadA
Synonyms: dadA2
Ordered Locus Names: CV_1914
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Oxidative deamination of D-amino acids By similarity.

Catalytic activity

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

Cofactor

FAD By similarity.

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.

Sequence similarities

Belongs to the dadA oxidoreductase family.

Ontologies

Keywords
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processalanine catabolic process

Inferred from electronic annotation. Source: HAMAP

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionD-amino-acid dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 435435D-amino acid dehydrogenase small subunit HAMAP MF_01202
PRO_0000166130

Regions

Nucleotide binding3 – 1715FAD Potential

Sequences

Sequence LengthMass (Da)Tools
Q7NWR6-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 2B7D97491596355D

FASTA43546,873
        10         20         30         40         50         60 
MKVIVLGGGV LGVSTAWYLA KAGCQVTVLE RQDGVALETS FGNAGQISPG YSAPWAAPGI 

        70         80         90        100        110        120 
PLKGLKWMFQ RHAPLAITPD GSLYQLQWIA KMLANCNEKA YAVNKGRMMR LAEYSRDKIK 

       130        140        150        160        170        180 
ELRAETGLQY EGRQGGTLQL LRSQAQVEGM AKDIAVLREC GVDFNVLDPD GCARVEPALA 

       190        200        210        220        230        240 
AVKHKLAGGL QLPNDETGDC NLFTSRLAEL ARDKGVEFRF GVTVDGIEND GKRITGVRIG 

       250        260        270        280        290        300 
DELLRADHYV VAMGSYSRDM VKELGIDIPV YPVKGYSLTV PITNPDGAPT STILDETYKV 

       310        320        330        340        350        360 
AITRFDNRIR VGGMAELSGY NLELNPRRRE TLEMVVGDLY PNGGDIKAAS FWTGLRPMTP 

       370        380        390        400        410        420 
DGTPIIGGTR FANLSLNTGH GTLGWTMCAG SGKVLADIIT GAKPEISVDG LSMQRYAKQG 

       430 
ETLVVPVIRP AVQGA 

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

Cross-references

Sequence databases

AE016825 Genomic DNA. Translation: AAQ59588.1.
RefSeqNP_901584.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2546976.
GenomeReviewsGene locus CV_1914 in contig AE016825_GR.
KEGGcvi:CV_1914.
NMPDRfig|243365.1.peg.1914.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7NWR6.
OMAQ7NWR6. MFQKHAP.

Enzyme and pathway databases

BioCycCVIO243365:CV_1914-MON.
BRENDA1.4.99.1. 415.

Family and domain databases

HAMAPMF_01202.
[Tree]
InterProIPR006076. FAD-dep_OxRdtase.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameDADA_CHRVO
AccessionPrimary (citable) accession number: Q7NWR6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: December 15, 2003
Last modified: June 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents