ID A0A0M8N0T6_9HYPO Unreviewed; 514 AA.
AC A0A0M8N0T6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Very long-chain specific acyl-CoA dehydrogenase {ECO:0000313|EMBL:KOS22778.1};
GN ORFNames=ESCO_003519 {ECO:0000313|EMBL:KOS22778.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS22778.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS22778.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:KOS22778.1}.
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DR EMBL; LGSR01000002; KOS22778.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8N0T6; -.
DR STRING; 150374.A0A0M8N0T6; -.
DR OrthoDB; 294001at2759; -.
DR Proteomes; UP000053831; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR PANTHER; PTHR48083:SF28; ACYL-COA DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10880); 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831}.
FT DOMAIN 5..80
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 514 AA; 56835 MW; 10E54634558DAB08 CRC64;
MAPPAKTYTR EEVRDHTSDD SLWCIIDSIV YDLTDFVDAH PGGESVLKQI AGQDATTAFY
NLHRQEVLAK YADLAIGTVA GESPQVIVPR PGDLSAVPYA EPLWLNPTFK SPYYNDSHHR
LARALRVFTD TYITPEANEA EASGRFVSQE LIDRMSRAGI LHMRLGPGKH LRGVELMGGA
VKPDEYDYFH DLVLSQELVR PMMRGFADGN MSGMTIGLSA VLNFARDEAW KKRIADEVFS
GKKKLCLAIT EAFAGSDVAG LRTTAEKTPD GKHYIVNGTK KWITNGAFSD YFVTGVRTAK
GLSVLLIERG EGVSTKPIKT SYSPAAGTAY VTFDNVRVPA ANLLGDEDRG IHVILSNFNH
ERWMMACGSA RAARFVVEEC LKWANQRLVF GKRLVDQPVV RQKLARMIAL VEANQAYLET
VTYQMCHMPY AQQARHLAGP VGLLKMSVTR AAHEIADESV QIFGGRALTQ SGMGKYIEMF
NRTYKFDAIL GGAEEILADL GVRQAMKDFP KAML
//
