ID   A0A0P7ZRX4_9RHOB        Unreviewed;       420 AA.
AC   A0A0P7ZRX4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=D-amino-acid dehydrogenase {ECO:0000313|EMBL:KPQ05193.1};
DE            EC=1.4.99.6 {ECO:0000313|EMBL:KPQ05193.1};
GN   Name=dadA {ECO:0000313|EMBL:KPQ05193.1};
GN   ORFNames=HLUCCA12_15690 {ECO:0000313|EMBL:KPQ05193.1};
OS   Rhodobacteraceae bacterium HLUCCA12.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1666916 {ECO:0000313|EMBL:KPQ05193.1, ECO:0000313|Proteomes:UP000050476};
RN   [1] {ECO:0000313|EMBL:KPQ05193.1, ECO:0000313|Proteomes:UP000050476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLUCCA12 {ECO:0000313|EMBL:KPQ05193.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00009410}.
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:KPQ05193.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LJSV01000022; KPQ05193.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7ZRX4; -.
DR   STRING; 1666916.HLUCCA12_15690; -.
DR   PATRIC; fig|1666916.3.peg.1228; -.
DR   Proteomes; UP000050476; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   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   Oxidoreductase {ECO:0000313|EMBL:KPQ05193.1}.
FT   DOMAIN          4..395
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   420 AA;  44266 MW;  02B71E942544AA0D CRC64;
     MGAIAVIGAG VIGRTLALEL ASDGHEVLLV APEAEPHMAS TGNAAIIADY AIDPVATPQV
     LRSLPSMLVD PLGPLAIHRP SAPRLTPWLA RFAWQCLPAN ARRNRQALLP LLAGTGADWV
     ALAGRIGAGD LFRRRGALYA FETAQACDAA RPGLARSRLH GIDAAMIDAA TLEMLEPGLP
     RGRFGGAVHY PSTLSLDDPA QMLDRIGAAG TARGVLRIDA RVSGLRRTRH GWHLTLSGEP
     PVEVAQIVIT AGAWSGQLAR LIGCKIPLDT ERGYHLEFDL ADRAIPLTRP ICPERFGFYL
     TPLSGRLRAA GTVELGGRDS APSPARWGRI EQGARSILPD LPPVSRRWMG LRPSLPDSLP
     VIGAAGPGAP GAWLAFGHGH LGLTLAPRTA SLLSALIAGR APPLDPAPYG PARFRAGLAW
//