Reviewed, UniProtKB/Swiss-Prot Q6FFR5 (DADA_ACIAD)

Names and origin

Protein names

Recommended name:
    D-amino acid dehydrogenase small subunit
    EC=1.4.99.1

Gene names

Name:	dadA
Ordered Locus Names:	ACIAD0115

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Oxidative deamination of D-amino acids By similarity.
Catalytic activity	A D-amino acid + H(2)O + acceptor = a 2-oxo acid + NH(3) + reduced acceptor.
Cofactor	FAD By similarity.
Pathway	Amino-acid degradation; D-alanine degradation; NH(3) and pyruvate from D-alanine: step 1/1.
Subunit structure	Heterodimer of a small and a large subunit By similarity.
Sequence similarities	Belongs to the dadA oxidoreductase family.

Ontologies

Keywords
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	alanine catabolic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	D-amino-acid dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 419	419	D-amino acid dehydrogenase small subunit		PRO_1000066066
Regions
	Nucleotide binding	3 – 17	15	FAD Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6FFR5-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: C8DEA58CDCF9D5D0	FASTA	419	46,299
	10 20 30 40 50 60 MRVIVLGSGV IGVASAYYLA QQGAHVTVLD RQTGPAEETS FGNAGQISPG YSTPWAAPGI 70 80 90 100 110 120 PFKAVKWMFQ HHAPLAINLD GSMWQLQWMA QMLKNCNPQS YSQNKERMMR VAEYSRDCLK 130 140 150 160 170 180 SLRETTGISY ENRAKGTLQV FRKEAQLEAV QRDIEVLQEC GVSYELLYQD DLARVEPALE 190 200 210 220 230 240 HAKDKLVGGL HLPNDETGDC YLFTNALAQK AKELGVNFQF NQNVEGLVVE GDEIKGVRVN 250 260 270 280 290 300 GQVLKADRYV LAFGSYSRDF LKPLALNLPV YPVKGYSLTI PIVQPEFAPQ STVLDETYKI 310 320 330 340 350 360 AITRFDQRIR VGGMAELSGF NLGLNQDRRA TLEMVTQDLF PGGNMAEASF WTGLRPMTPD 370 380 390 400 410 STPIIGATRF KNLFLNTGHG TLGWTMACGS GKLISDIVLS HQTEISTEGL SLQRYSTAA

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR543861 Genomic DNA. Translation: CAG67092.1.
RefSeq	YP_044914.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2878458.
GenomeReviews	Gene locus ACIAD0115 in contig CR543861_GR.
KEGG	aci:ACIAD0115.
NMPDR	fig|62977.3.peg.89.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6FFR5.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD0115-MON.
Family and domain databases
HAMAP	MF_01202. [Tree]
InterPro	IPR006076. FAD-dep_OxRdtase. [Graphical view]
Pfam	PF01266. DAO. 1 hit. [Graphical view]
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

DADA_ACIAD

Accession

Primary (citable) accession number: Q6FFR5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	July 19, 2004
Last modified:	November 4, 2008
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)