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Database: UniProt
Entry: A0A0F0IHW5_ASPPU
LinkDB: A0A0F0IHW5_ASPPU
Original site: A0A0F0IHW5_ASPPU 
ID   A0A0F0IHW5_ASPPU        Unreviewed;       574 AA.
AC   A0A0F0IHW5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Acyl-CoA dehydrogenase C-terminal domain protein {ECO:0000313|EMBL:KJK66776.1};
GN   ORFNames=P875_00127775 {ECO:0000313|EMBL:KJK66776.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK66776.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK66776.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-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:KJK66776.1}.
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DR   EMBL; JZEE01000232; KJK66776.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0IHW5; -.
DR   STRING; 1403190.A0A0F0IHW5; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 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   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   PANTHER; PTHR48083:SF20; LONG-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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   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; PS50255; CYTOCHROME_B5_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT   DOMAIN          2..109
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   REGION          110..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  64180 MW;  C78090796ED7812E CRC64;
     MSKTFSKEDV ASHNKPDNLW VVIDEDVYDL TKFQDEHPGM FEQFRGSWKK EYVIVSLFIF
     GHGRSADADY APLVLSRVGG KDASKQFWKY HNEGILKKYK SKLQVGSLNT KAADAPAPEP
     AAAKETPKPQ QAAPVDVGSA KSSEPQDPYG DLIPFADPSW YQGYSSPYFN QTHAALRAEV
     RQWVESEIEP YVTEWDEAKN VPDHIYKQMG ERGYLAGLLG GKFPVDHTKN RVQSVAPENW
     DLFHEMLLTD ELSRAGSGGL VWNLIGGYGI GCPPLVKYGK KPLVDRILPG ILNGDKRICL
     AITEPDAGSD VANLTCEAKL TPDGKHYIVN GEKKWITNGV YADYFTTAVR TGGPGMNGLS
     VLLIEREHGG VSTRRMDCQG VWSSGTTYVT FEDVKVPVEN LIGKENQGFK VIMTNFNHER
     IGIVIQCCRF ARVCYEEAVK YAHKRRTFGK RLIDHPVIRM KLAHMARQIE ATYNWLENII
     YQCQSMDETE AMLKLGGAIA SLKAQSTTTF EFCAREASQI FGGLSYSRGG QGGKVERLYR
     DVRAYAIPGG SEEIMLDLSM RQSLRVHKMF GMKL
//
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