ID   H1G0E2_9GAMM            Unreviewed;       418 AA.
AC   H1G0E2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=D-amino acid dehydrogenase small subunit {ECO:0000313|EMBL:EHQ51279.1};
DE            EC=1.4.99.1 {ECO:0000313|EMBL:EHQ51279.1};
GN   ORFNames=ECTPHS_01224 {ECO:0000313|EMBL:EHQ51279.1};
OS   Ectothiorhodospira sp. PHS-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodospira.
OX   NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ51279.1, ECO:0000313|Proteomes:UP000005314};
RN   [1] {ECO:0000313|EMBL:EHQ51279.1, ECO:0000313|Proteomes:UP000005314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ51279.1,
RC   ECO:0000313|Proteomes:UP000005314};
RA   Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA   Hoeft S., Oremland R.S., Stolz J.;
RT   "ArxA, a new clade of arsenite oxidase within the DMSO family of molybdenum
RT   oxidoreductases.";
RL   Submitted (JAN-2012) 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:EHQ51279.1}.
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DR   EMBL; AGBG01000002; EHQ51279.1; -; Genomic_DNA.
DR   RefSeq; WP_008930846.1; NZ_AGBG01000002.1.
DR   AlphaFoldDB; H1G0E2; -.
DR   STRING; 519989.ECTPHS_01224; -.
DR   PATRIC; fig|519989.5.peg.245; -.
DR   eggNOG; COG0665; Bacteria.
DR   OrthoDB; 9805337at2; -.
DR   Proteomes; UP000005314; 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:EHQ51279.1}.
FT   DOMAIN          2..399
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   418 AA;  45581 MW;  F0B2B64BE60E0ACA CRC64;
     MKVLVLGSGV IGVTSAWYLA RAGHEVTVID RLEEPAMETS HANAGMLSFD HSTPWAAPGV
     PFKAIRWLTQ DLAPLYINPR AIDIRALGFL VRMLGQCTSS AFTVNKERML RVARYSAECF
     KALREELPLH YDGRQKGTLE LFRTEKDLAE AGDNVAILER WDIPHAVLDV DACIRHEPAL
     AHVREKIAGG VLLPGDETGD CRKFTLALAK ACETLGVTFL MNTSVEAIDT GNGKITGVRT
     STGTLTADRY VVALGCESPR VLGGIGIHLP IYPLKGYSLT MPILDEDRAP QSTVMDQKYK
     VAVTRFDHRI RVGGIAEIAG DNKDLPQQRR AAIEFVVRDL FPGGGAVEAA EFWTGLRPMT
     PDNVPILGGT RYDNLFLNTG HGTLGWTMSL GSARFVADLV SGRSPDIDPT GLGVDRYR
//