ID M9R819_9RHOB Unreviewed; 417 AA.
AC M9R819;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Putative D-amino acid dehydrogenase small subunit {ECO:0000313|EMBL:AGI68824.1};
GN ORFNames=OAN307_c33160 {ECO:0000313|EMBL:AGI68824.1};
OS Octadecabacter antarcticus 307.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI68824.1, ECO:0000313|Proteomes:UP000005307};
RN [1] {ECO:0000313|EMBL:AGI68824.1, ECO:0000313|Proteomes:UP000005307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=307 {ECO:0000313|EMBL:AGI68824.1,
RC ECO:0000313|Proteomes:UP000005307};
RX PubMed=23671678;
RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA Brinkhoff T., Simon M., Daniel R.;
RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT Plasticity and a New Type of Xanthorhodopsin.";
RL PLoS ONE 8:E63422-E63422(2013).
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}.
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DR EMBL; CP003740; AGI68824.1; -; Genomic_DNA.
DR RefSeq; WP_015500801.1; NC_020911.1.
DR AlphaFoldDB; M9R819; -.
DR STRING; 391626.OAN307_c33160; -.
DR KEGG; oat:OAN307_c33160; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_5; -.
DR OrthoDB; 9805337at2; -.
DR Proteomes; UP000005307; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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;
FT DOMAIN 4..401
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 417 AA; 45496 MW; 158040B3B57EF1A7 CRC64;
MKSIAVIGAG ITGITTAYAL LERGFDVTVF DRNRYAAMET SFANGGQLSA SNAEVWTQWS
TIIKGIKWMA SRNAPLLVNP KPSWHKYSWM AEFMSNIPNY RKNTIESVRL AINARQHLMG
HAEKEGFKFD CEHRGILHVY NCKADFDGAA KVNDMLAEGG LERHAVTPDE MKVIEPTLKG
DLYGGYFTES DFTGDIHSYA KGLGDACKKR GVVFKYGRDV ETLTARKSGG VDVGWTNTEN
SNVSDHFDGI VICAGVRSRA LAAQVGDRVN IYPVKGYSIT VQLDDDESRA ATPWVSLLDD
KAKIVTSRLG QNRFRVAGTA EFNGYNKDIR DDRIAPLTKW VENLFPDVST EHAIPWAGLR
PMMPSMMPRV GAGKAAGVFY NTGHGHLGFT LAAATAELAA DSVLQASQSN SVGAAEG
//
