ID   A0A1C1CZ11_9EURO        Unreviewed;       474 AA.
AC   A0A1C1CZ11;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Isobutyryl-CoA dehydrogenase, mitochondrial {ECO:0000313|EMBL:OCT53678.1};
GN   Name=acad8 {ECO:0000313|EMBL:OCT53678.1};
GN   ORFNames=CLCR_11401 {ECO:0000313|EMBL:OCT53678.1};
OS   Cladophialophora carrionii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT53678.1, ECO:0000313|Proteomes:UP000094526};
RN   [1] {ECO:0000313|Proteomes:UP000094526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA   Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA   Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
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         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:OCT53678.1}.
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DR   EMBL; LGRB01000008; OCT53678.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C1CZ11; -.
DR   STRING; 86049.A0A1C1CZ11; -.
DR   VEuPathDB; FungiDB:CLCR_11401; -.
DR   VEuPathDB; FungiDB:G647_00623; -.
DR   eggNOG; KOG1469; Eukaryota.
DR   Proteomes; UP000094526; 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; 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; PTHR48083:SF32; -; 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; 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:UP000094526}.
FT   DOMAIN          33..159
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          163..265
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          277..428
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   474 AA;  52630 MW;  C5BD1170425CE98D CRC64;
     MSVPYLLNSA TGHIPASERI PVIARPFVSE RAKKTLDLVE RFVEEDCVPA DAVFAQQINE
     KGHDTVSRFD SHPRVIEDLK TKARKLGLWN MFLPKNHFKE GAGFSNLEYG LMAEYLGKSV
     TASEACNCAA PDTGNMEVFA KYGTEEQKKQ WLVPLLNGEI RSAFLMTEPQ VASSDATNIE
     LSMRKDGDYY VLNGQKWWSS GAGDRRCKIY IVMGKSDPGN KNVYRQQSVI LVPADTPGIT
     IERMLSVIGF DDAPHGHGHI SFNNVRVHKS NMILGEGRGF EVVQGRLGPG RIHHAMRSVG
     AAEKALEYFL ARMNDPQRRP FGKNLSEHGI MLERVARSRI EIDSARLAVL NAAIKIDQSN
     AKDALKEIAE VKVQVPNMLL DVLDRAIQAY GGAGVSQETP LAFMWANGRT MRIVDGPDEV
     HMLQLGRNEN KRGAALLKKI EAQKAKSREL LKQYGLQARD PLELKRVSGG QSKL
//