ID A0A0D2F3T7_9EURO Unreviewed; 644 AA.
AC A0A0D2F3T7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Acyl-CoA dehydrogenase/oxidase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV05_06888 {ECO:0000313|EMBL:KIW54534.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW54534.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW54534.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW54534.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|RuleBase:RU362125}.
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DR EMBL; KN847320; KIW54534.1; -; Genomic_DNA.
DR RefSeq; XP_013315118.1; XM_013459664.1.
DR AlphaFoldDB; A0A0D2F3T7; -.
DR STRING; 348802.A0A0D2F3T7; -.
DR GeneID; 25328796; -.
DR HOGENOM; CLU_016513_1_1_1; -.
DR OrthoDB; 5489386at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 2.40.110.20; -; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR041504; AidB_N.
DR PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42707:SF2; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF18158; AidB_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT DOMAIN 25..160
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 188..302
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 311..489
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 644 AA; 72233 MW; 2A808B386B46110E CRC64;
MSAKAPLRPS TADSGFILHL PPLDNPYTSD ESYQRVLAWY LPRHVLEVVK PRLVKFADEA
VSDETNELIA NAETQQPYVK SRNVWGARYP YDRLVTSHGW KELGRWGAKN GVIALGYEEE
FKQYRRIVQH AFNYTYSASS AVYSCPVSMT SGAARLVSKQ LASVPSEHPF HEIYRILTAR
ENNWISSQWM TERPGGSDVQ NSETVAVYSP LRQKSGSHGT IEEGDYLVSG FKFFSSATDC
NMALMLAKTG SGQLSLFIAP SRKSVVIDGK KQQVTNGIRI HRLKNKMGTK ELPTAEVELK
DVRAWLIGPL NRGIATIALL LNVTRTHNFI TALSCWRRGM AIAKSFAKAR STIDQPLWTF
PMHLRLLANL EVKHRGALQL AFFTTSLLSF VDNGFPDRHV QRSGYVPLPE SGEQTEIILR
TLTATAKAVI CKTATLSLQE CQEAMGGVGY MDEPDEPEYN ISRLMRDTAA NMTWEGTTNV
LSSEVVRHLL NKDGKHLRAF GDWVRKAASH VKDTELKRAL VRAWAEFSRT MEDKCGDLMA
VLAMGRQLMF TLAWIVAGVL LALDAQRDGN AVAMEIARRW VLEGEGNIGE FHLPNVVRVS
ERVVFVADKE RINWDCRLVW GVDLPKDAAR GYRAQTADTM RPRL
//
