ID A0A1Q5TCR4_9EURO Unreviewed; 452 AA.
AC A0A1Q5TCR4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OKO98013.1};
GN ORFNames=PENSUB_9593 {ECO:0000313|EMBL:OKO98013.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO98013.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKO98013.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO98013.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) 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|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:OKO98013.1}.
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DR EMBL; MNBE01000682; OKO98013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5TCR4; -.
DR STRING; 1316194.A0A1Q5TCR4; -.
DR OrthoDB; 2782405at2759; -.
DR Proteomes; UP000186955; 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; 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:SF34; BLR2947 PROTEIN; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 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:UP000186955}.
FT DOMAIN 157..251
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 263..429
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 452 AA; 51095 MW; E54D2B99542016F1 CRC64;
MNFELPNELK AHIQSIDSFI QSTILPLQHS NDNNRFFDHR REHARTDWDN DGNPRPEWEN
LLTQARVLAD EAGFYRFALP KQYGGQEHPH TNLWMSAIRF HLASVHGGGL GLANDLQNEH
SIVGNFPDLL MLHHFGSEAQ RQTLIPARLR GEFRATFGLT EPDHGSDATF MSTVAKRQRG
GFEITGAKKW QTGAHHCTHF LIFARTSGNA GSAKGITAFL IPRDTPGVKI ASYEWTLNMP
TDHATVEFDR VWVPESAVLG TVDQGLAIAQ TFVHENRIRQ AASSCGAAKF CLERSIVRAR
SRKIWGEGKM LADNQAIQFP VVELMTQVEM LRLLILKTSC DMDRIVASSK AGETSQPPWV
TIERQLSDKV AMCNFWANRL CCQAADRAIQ IHGGDGYSRH YPFEHIYRHF RRYRITEGAE
EIQMRKVAAY IFGFAGPRKK ELEATEQTKA KI
//