ID B3RK11_TRIAD Unreviewed; 360 AA.
AC B3RK11;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=FAD dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF01266};
GN ORFNames=TRIADDRAFT_20172 {ECO:0000313|EMBL:EDV28555.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV28555.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV28555.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV28555.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000189-1};
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC {ECO:0000256|ARBA:ARBA00006730}.
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DR EMBL; DS985241; EDV28555.1; -; Genomic_DNA.
DR RefSeq; XP_002107757.1; XM_002107721.1.
DR AlphaFoldDB; B3RK11; -.
DR STRING; 10228.B3RK11; -.
DR EnsemblMetazoa; TriadT20172; TriadP20172; TriadG20172.
DR GeneID; 6749770; -.
DR KEGG; tad:TRIADDRAFT_20172; -.
DR CTD; 6749770; -.
DR eggNOG; KOG3923; Eukaryota.
DR HOGENOM; CLU_034311_0_2_1; -.
DR InParanoid; B3RK11; -.
DR OMA; LWWPYRI; -.
DR OrthoDB; 5359at2759; -.
DR PhylomeDB; B3RK11; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0019478; P:D-amino acid catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006181; D-amino_acid_oxidase_CS.
DR InterPro; IPR023209; DAO.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR PANTHER; PTHR11530:SF11; D-ASPARTATE OXIDASE; 1.
DR Pfam; PF01266; DAO; 1.
DR PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00677; DAO; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000189-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000189-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT DOMAIN 6..328
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 170
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 314..319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ SEQUENCE 360 AA; 40830 MW; 067EBB8DDD22C249 CRC64;
MANTKKVCVV GAGVVGLSTA YCLANCGGNI EVTVIAEKFS PNTTGDGAAG KWYPSHLSQT
PEIDQRRWGS ITYQWLLDLT FSDLADSVGV SLVSGYHFFE YYPKDPHWKD MVLFFRRATN
REIEKINENG YYVVKTGWFY TTFFLNCETY LPWLMAKFRK LGGKVIQRRV ESLSELGGKY
DCIVNCSGLG SYQLADDKSL YPIWGQLARV NAPWIKHFIS FYSKEKKDAY IMPRATDVVL
GIYNEPHRWE NKVDDEIHEE TMQRIYSVMP SLKNAKVTWK WSGLRPARPA VRLENDQLNV
NGKKLPIIHN YGHGGSGITL HLGCALNATK LVIEALGMQS PGINYSYNFP RISQNYSSKL
//
