ID A0A080M1M6_9PROT Unreviewed; 419 AA.
AC A0A080M1M6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 ECO:0000313|EMBL:KFB74205.1};
GN ORFNames=AW09_000516 {ECO:0000313|EMBL:KFB74205.1};
OS Candidatus Accumulibacter phosphatis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=327160 {ECO:0000313|EMBL:KFB74205.1, ECO:0000313|Proteomes:UP000020077};
RN [1] {ECO:0000313|EMBL:KFB74205.1, ECO:0000313|Proteomes:UP000020077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-91 {ECO:0000313|Proteomes:UP000020077};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFB74205.1}.
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DR EMBL; JDVG02000082; KFB74205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080M1M6; -.
DR Proteomes; UP000020077; Unassembled WGS sequence.
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 ECO:0000313|EMBL:KFB74205.1}.
FT DOMAIN 3..397
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 419 AA; 45131 MW; 74125239518E7EA3 CRC64;
MKLVVLGAGV VGVTSAWYLA KAGHQVTVLD RQAAAGLETS FANGGQISVS HAEPWSNPHA
PLRALAWMRR EDAPLLFRLR CDAALLDWSL RFLCECTARR TRDNIRQIVT LALYSRRQLQ
ALRAETALAY DHLERGILHI YTDRREFASA IEAAAVMREF GCERRTVSVD ECIAIEPALA
SARPLLVGGD YTAADESGDA HRFTQQLAAL CAARGVVFRY GVAVDRLSVV AGRVAGVIAA
GELHQADVYV AALGSYTPLL LRPLGLHLPV YPAKGYSATV PLSADSIAPS VSITDDGHKI
VFSRLGQSLR IAGTAEFNGY NTDLNVVRCQ ALTKRAGELF PALRPADEAR FWCGLRPATP
SNVPLIGRSA IPNLYLNTGH GTLGWTMACG SGAALADIVS GRSPEPGFRF LPEPGFCFH
//