NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Garcia E., Richardson P.;
"Complete sequence of chromosome 1 of Ochrobactrum anthropi ATCC 49188.";
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.

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.
COFACTOR: FAD (By similarity).
PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and pyruvate from D-alanine: step 1/1 .
SUBUNIT: Heterodimer of a small and a large subunit (By similarity).
SIMILARITY: Belongs to the dadA oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000758; ABS14161.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001369990.1; -.

3D structure databases

ModBase

A6WYV7.

Ontologies

GO:0008718;	Molecular function: D-amino-acid dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0006524;	Biological process: alanine catabolic process (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01202; -; 1.
PBIL [Tree]

InterPro

IPR006076; FAD-dep_OxRdtase.
Graphical view of domain structure.

Pfam

PF01266; DAO; 1.
Pfam graphical view of domain structure.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

ProtoNet

A6WYV7.

Genome annotation databases

GeneID

5380437; -.

GenomeReviews

CP000758_GR; Oant_1444.

KEGG

oan:Oant_1444; -.

CMR

A6WYV7; Oant_1444.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; FAD; Flavoprotein; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 416`	`416`	`D-amino acid dehydrogenase small subunit.`	`PRO_1000066102`
`NP_BIND`	`3 17`	`15`	`FAD (Potential).`

Sequence information

Length: 416 AA [This is the length of the unprocessed precursor]

Molecular weight: 45136 Da [This is the MW of the unprocessed precursor]

CRC64: D535372236B10A2B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQITILGSGV IGVTTAYYLA KLGHEVTVVD REEGPALETS FANAGQVSPG YASPWAAPGI 

        70         80         90        100        110        120 
PFKAAKWLFQ KHAPLVLRPT CDPVQYSWLL QMLANCTDSR YKVNKTRMVR VAEYARDCLV 

       130        140        150        160        170        180 
DLRKETGIEY DQRMQGTLQL FREQYQLDGI GKDIEVLRQD GVPFEVLDRE GCAKVEPALA 

       190        200        210        220        230        240 
RVKDKFVGGL RLPHDETGDC FKFTNALAKI AEGLGVKFRF GVNIKSLLMS GGKVSGVETS 

       250        260        270        280        290        300 
EGVLTADRYV VALGSYTPAL VKSLGLNAPI YPVKGYSITA PIVDEDRAPV STVLDESYKI 

       310        320        330        340        350        360 
AITRLGDRIR VGGMAEVSGF TTDLPAARRA TLDLSVTDLF PGGDLKAATF WSGLRPMTPD 

       370        380        390        400        410 
STPIIGATRY DNVFINAGHG TLGWTMSCGS GKLLADLISG NKPDIRADDL GISRYE

A6WYV7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools