ID A0A1V8TU97_9PEZI Unreviewed; 412 AA.
AC A0A1V8TU97;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B0A48_00299 {ECO:0000313|EMBL:OQO14917.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO14917.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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:OQO14917.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NAJO01000001; OQO14917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8TU97; -.
DR STRING; 1507870.A0A1V8TU97; -.
DR InParanoid; A0A1V8TU97; -.
DR OrthoDB; 2784945at2759; -.
DR Proteomes; UP000192596; 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 CDD; cd00567; ACAD; 1.
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 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; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_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:UP000192596}.
FT DOMAIN 30..142
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 147..243
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 257..404
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 412 AA; 45676 MW; E4C40F3FDC3CB9F0 CRC64;
MRPSQLTQLN NRRLFVAKAT DYLPAYADYT DSQLTVREAI AKICSNFPDS YWLNIDNTAT
WPTEFQQAIA RAGWLGIMMP SQYGGSELGL AEATIMMQTI AESGGGYTAS SCVHMNIFGL
APVVKYGSEE QKARFLPPLI EGRERACFAV TEPNTGLDTL KLQSLATRDG DEYVLKGSKI
WTSTAQVAEK ILILVRTTPL EDVKKPSEGL TLFYTDLDRS QVSVTEIKKM GRAAVDTNSL
YFDGWRIPAT DRIGNEGDGF KMIMHGMNAE RILIAGEAIG LGIAAIRHAA RYARERVVFG
RPIGQNQGIA HPLAKAWCEL ESTRLMTMQA AKMWDEGFAT GEYANACKYL AGEHAFTACE
TAVCSMGGMG YAKEYHVERF LREVIIPRLA PVSREMILNY ISEKVLDLPR SY
//