ID H0Q2U4_9RHOO Unreviewed; 433 AA.
AC H0Q2U4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=D-amino acid dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01202};
DE EC=1.4.99.- {ECO:0000256|HAMAP-Rule:MF_01202};
GN Name=dadA {ECO:0000256|HAMAP-Rule:MF_01202};
GN ORFNames=AZKH_0393 {ECO:0000313|EMBL:BAL22739.1};
OS Azoarcus sp. KH32C.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL22739.1, ECO:0000313|Proteomes:UP000007106};
RN [1] {ECO:0000313|EMBL:BAL22739.1, ECO:0000313|Proteomes:UP000007106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH32C {ECO:0000313|EMBL:BAL22739.1,
RC ECO:0000313|Proteomes:UP000007106};
RA Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S.,
RA Senoo K.;
RT "Complete genome sequence of Azoarcus sp. KH32C.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxidative deamination of D-amino acids. {ECO:0000256|HAMAP-
CC Rule:MF_01202}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + a D-alpha-amino acid + H2O = a 2-oxocarboxylate + AH2 +
CC NH4(+); Xref=Rhea:RHEA:18125, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59871; Evidence={ECO:0000256|ARBA:ARBA00000728,
CC ECO:0000256|HAMAP-Rule:MF_01202};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_01202};
CC -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00009410, ECO:0000256|HAMAP-Rule:MF_01202}.
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DR EMBL; AP012304; BAL22739.1; -; Genomic_DNA.
DR RefSeq; WP_015434047.1; NC_020516.1.
DR AlphaFoldDB; H0Q2U4; -.
DR STRING; 748247.AZKH_0393; -.
DR KEGG; aza:AZKH_0393; -.
DR PATRIC; fig|748247.4.peg.399; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_4; -.
DR OrthoDB; 18526at2; -.
DR Proteomes; UP000007106; Chromosome.
DR GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR HAMAP; MF_01202; DadA; 1.
DR InterPro; IPR023080; DadA.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13847:SF280; D-AMINO ACID DEHYDROGENASE; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|HAMAP-Rule:MF_01202};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01202};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01202};
KW Reference proteome {ECO:0000313|Proteomes:UP000007106}.
FT DOMAIN 2..398
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01202"
SQ SEQUENCE 433 AA; 47049 MW; F76906DCA67ABD67 CRC64;
MRVLVLGSGV VGTTTAWYLA RRGAKVTVID RQPGSALETS YANAGQVSPG YSTPWAAPGI
PLKAMKWLFQ RHSPLSIRPD GSLFQLRWMA QMLRNCTADR YAVNKERMMR LSEYSRDCLR
ALRADTGIQY EERTLGTLQL FRSQAQVDAA ARDIQVLEEC GVPYELLDRD QLGRVEPALA
RVSHKLAGGL RLPNDETGDC HLFTTRLAEK ARELGVEFRY GQDIREVMVG GGDVIGVQVG
NEVLAADRYV LALGSYSRQM LAPLGLDLPV YPLKGYSLTV PLIDAAAAPV STVLDETYKI
AITRFADRIR VGGMAELGGF DLALNPRRRE TLEMVVSDLF PGGGDVPKAE FWTGLRPMTP
DGTPVVGATA YPDLFVSTGH GTLGWTMACG SGQLMADLVT GHQPAIRHQD LGLARYGKVA
ASRSQGLNLS PAA
//
