NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.;
"Complete sequence of chromosome 1 of Burkholderia sp. 383.";
Submitted (OCT-2005) 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

CP000151; ABB07775.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_368419.1; -.

3D structure databases

ModBase

Q39IE1.

Enzyme and pathway databases

BioCyc

BSP36773:BCEP18194_A4178-MON; -.

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).
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]

BLOCKS

Q39IE1.

Genome annotation databases

GeneID

3749371; -.

GenomeReviews

CP000151_GR; Bcep18194_A4178.

KEGG

bur:Bcep18194_A4178; -.

NMPDR

fig|269483.3.peg.5348; -.

Phylogenomic databases

HOGENOM

Q39IE1; -.

Genome annotation databases

CMR

Q39IE1; Bcep18194_A4178.

Other

ProtoNet

Q39IE1.

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`	`1 428`	`428`	`D-amino acid dehydrogenase small subunit.`	`PRO_1000066083`
`NP_BIND`	`3 17`	`15`	`FAD (Potential).`

Sequence information

Length: 428 AA [This is the length of the unprocessed precursor]

Molecular weight: 45978 Da [This is the MW of the unprocessed precursor]

CRC64: D4C011F2203689C3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRVVILGSGV VGVASAYYLA RAGHEVTVID REAGPALETS FANAGQISPG YAAPWAAPGV 

        70         80         90        100        110        120 
PLKAVKWMFE KHAPLAIRLD GTRFQLQWMY QMLRNCTAER YAVNKGRMVR LAEYSRDCLQ 

       130        140        150        160        170        180 
ALRADTGIQY EGRTGGTLQL FRTQQQLDGA AKDIAVLQEA NVPFELLSPA DLKKAEPALA 

       190        200        210        220        230        240 
AVSHKLTGGL RLPGDETGDC QLFTTRLAAL AESLGVKFRY NTPIDALAIA GGKIAGVQCG 

       250        260        270        280        290        300 
SETVRADAYV VALGSYSTSF ISNLMKIPVY PLKGYSITAP IVNEAAAPVS TVLDETYKIA 

       310        320        330        340        350        360 
ITRFDQRIRV GGMAEIVGFD KKLRAARRET LEMCVNDLFP GGGDTSKATF WTGLRPMTPD 

       370        380        390        400        410        420 
GTPIVGRTPV SNLFLNTGHG TLGWTMSCGS GQLLADLISG KMPAIQADDL SVHRYLKDVA 


GQTRPAYA

Q39IE1 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