ID A0A2I0MVH6_COLLI Unreviewed; 415 AA.
AC A0A2I0MVH6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=D-aspartate oxidase, transcript variant X2 {ECO:0000313|EMBL:PKK33684.1};
DE Flags: Fragment;
GN Name=DDO {ECO:0000313|EMBL:PKK33684.1};
GN ORFNames=A306_00000837 {ECO:0000313|EMBL:PKK33684.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK33684.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK33684.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK33684.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC {ECO:0000256|ARBA:ARBA00006730}.
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:PKK33684.1}.
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DR EMBL; AKCR02000002; PKK33684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0MVH6; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProt.
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 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 Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872}.
FT DOMAIN 77..398
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PKK33684.1"
SQ SEQUENCE 415 AA; 44798 MW; 6661B94A42D47012 CRC64;
PSLAEGRGAG TPGAAPGKGS CQHPLPGLPA PPRQRAPSSR APSSPAPLLR ASREGDSSSS
PGASLLRLCT LDMAAPKVAV IGAGVVGLST ALCIVETCPS CSVTVLSDQF SPNTTSNVAA
GILIPHTYPG TPIHVQKQWF KETFTYLFAL SNSNEASEAG VHLVSGWQIF KNTPTPKEEL
PFWSDVVLGF RPMSEAELQK FPQHQFGQAF TTLKCECPPY LLWLEKRLKA NGVQMYTRKV
ADLWELHSEY NIIVNCSGIG AHQLVGDEKL LPVRGQVLKV HAPWVKNFIR DGDGLTYIYP
GIYSVTLGGT REKEKWSLSP DPDTTKDIFE RCCSLEPSLW GAQDIEVKVG LRPSRWCVRL
ERQVLSRGGV KLPVVHNYGH GAGGFSVHRG TAKEAARLVG ECIAALQGSS SRAKL
//