ID I4VPC2_9GAMM Unreviewed; 416 AA.
AC I4VPC2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=UU9_10472 {ECO:0000313|EMBL:EIL89063.1};
OS Rhodanobacter fulvus Jip2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163408 {ECO:0000313|EMBL:EIL89063.1, ECO:0000313|Proteomes:UP000004210};
RN [1] {ECO:0000313|EMBL:EIL89063.1, ECO:0000313|Proteomes:UP000004210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jip2T {ECO:0000313|Proteomes:UP000004210};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:EIL89063.1}.
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DR EMBL; AJXU01000042; EIL89063.1; -; Genomic_DNA.
DR AlphaFoldDB; I4VPC2; -.
DR STRING; 1163408.UU9_10472; -.
DR PATRIC; fig|1163408.3.peg.2147; -.
DR eggNOG; COG0665; Bacteria.
DR Proteomes; UP000004210; 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:EIL89063.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004210}.
FT DOMAIN 1..389
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 416 AA; 45433 MW; 40EC1E1B604475A5 CRC64;
MIGTCSAWYL ARAGFEVTVV DRQPAPGQET SFANAGQISP GYASPWAAPG VPLKALKWLF
MRHAPLAIRP GLDPQQYLWL LQMLRNCTAS RYAINKARMV RLSEYSRDCL DELRTETGLE
YEGRQLGTMQ VFRTQAQLDG ADKDTAVLDQ YGVPYELLDR AGIVRFEPAL AGVVDQLSGA
LRLPHDETGD CELFTRRLAE RAQAAGVEFR FGATIEKFEH DGGRITGVQI DGQMERADRY
VLALGSYSPR LLAPLGIRLP VYPLKGYSLT VPITDPAMAP TSTILDETYK VAVTRLGQRI
RVGGMAEVAG FDLSLSPRRR ATLEKVINDL YPQGGDLTRA TFWTGLRPAT PDGTPVVGAT
RLDNLYLNTG HGTLGWTMAC GSGRYLADLM TGRPPQISGE GLDISRYGMR AAGTAA
//
