ID E0VYW7_PEDHC Unreviewed; 338 AA.
AC E0VYW7;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=D-aspartate oxidase, putative {ECO:0000313|EMBL:EEB18573.1, ECO:0000313|EnsemblMetazoa:PHUM521090-PA};
DE EC=1.4.3.1 {ECO:0000313|EMBL:EEB18573.1};
GN Name=8231693 {ECO:0000313|EnsemblMetazoa:PHUM521090-PA};
GN ORFNames=Phum_PHUM521090 {ECO:0000313|EMBL:EEB18573.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB18573.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB18573.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB18573.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB18573.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM521090-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM521090-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC {ECO:0000256|ARBA:ARBA00006730}.
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DR EMBL; AAZO01006328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235848; EEB18573.1; -; Genomic_DNA.
DR RefSeq; XP_002431311.1; XM_002431266.1.
DR AlphaFoldDB; E0VYW7; -.
DR STRING; 121224.E0VYW7; -.
DR EnsemblMetazoa; PHUM521090-RA; PHUM521090-PA; PHUM521090.
DR GeneID; 8231693; -.
DR KEGG; phu:Phum_PHUM521090; -.
DR CTD; 8231693; -.
DR VEuPathDB; VectorBase:PHUM521090; -.
DR eggNOG; KOG3923; Eukaryota.
DR HOGENOM; CLU_034311_0_2_1; -.
DR InParanoid; E0VYW7; -.
DR OMA; CHGGWKY; -.
DR OrthoDB; 5359at2759; -.
DR Proteomes; UP000009046; Unassembled WGS sequence.
DR GO; GO:0008445; F:D-aspartate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:InterPro.
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; IPR023209; DAO.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR PANTHER; PTHR11530:SF17; RE49860P; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:EEB18573.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009046}.
FT DOMAIN 8..326
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 338 AA; 38299 MW; 241185FE1D3C8DFA CRC64;
MSGIKFGVLG AGVVGMTTCL ELQSQYPNSD IYLIADKFNE ETTSDGAAGI FRPGTSFSIY
PEEYTKFVIE ESYCYYDEIR KKINPFVSGV SEISGYIFSS NNSSLVKNDL IDKIVPVYRS
ANDDELSICP GKWLYGSYFV TLLTECRKFL PWTLLRFKEN GGRVIMKKIN SINDLGEYKF
DLIFNCSGFG AKYIFNDRKL VPIRGQVIKV KAPWLKNFFY ADYDTYVIPG LENVTLGGCR
HYDSYDLNIN PYDSAAIWNR CVQLVPGLKN VKIEKEWVGL RPHRDPVRIQ IESVKLNDKY
LKCVHNYGHG GYGVTTAPGS AKLAVKLATD YFKKNSKM
//
