ID W9WPK3_9EURO Unreviewed; 674 AA.
AC W9WPK3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O5_10100 {ECO:0000313|EMBL:EXJ66905.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ66905.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ66905.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ66905.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={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:EXJ66905.1}.
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DR EMBL; AMGX01000018; EXJ66905.1; -; Genomic_DNA.
DR RefSeq; XP_007748868.1; XM_007750678.1.
DR AlphaFoldDB; W9WPK3; -.
DR STRING; 1182543.W9WPK3; -.
DR GeneID; 19194795; -.
DR eggNOG; KOG0137; Eukaryota.
DR HOGENOM; CLU_016513_1_1_1; -.
DR OrthoDB; 5489386at2759; -.
DR Proteomes; UP000019471; 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; 2.40.110.20; -; 1.
DR Gene3D; 6.10.250.600; -; 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; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR041504; AidB_N.
DR PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42707:SF2; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF18158; AidB_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:UP000019471}.
FT DOMAIN 59..195
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 230..346
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 356..429
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 475..535
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 75560 MW; CAE395D0166EC8BD CRC64;
MPPHFSENQE LLGDMETNKP YTTESRINSV DRPGKLDTTT SDAHHIAPSS STAGFFQSPP
QVLNQYEDDT ALRRAMKLFL PHGVQEALKA DLSAFGERVL TRQTLGWVLE AERNLPYVKS
WDTWGKRRDE LITSDGWKNL QRMGIEAGIV AIPYENSFQE FSRIYWCTKY ILWCGSSAWV
NCPSLIVDGV ASLFREHLSD DTLGDERQVL QDAYTRLVSR DGEKAWTSGQ WMTERQGGSD
VRMTETVATY APNCQSNEEE DAHGNPLGPW RLDGFKWFSS ATDANMAILL ARTQKGISLF
YAPMRRALKE KDAMGFGTAS NGVYIQRLKN KLGTKALPTA ELEIKGMRGW LVGEEGRGTK
EIATVLNVAR LHNAATAVGL WGRGLGIVRA FARVRLVGRR PLYERAGFMR NLARMHTEYR
ANVLFTFFVS GLLGCAEQEK IAKMAGEQGK GVDKMGKLPN VTDTPMAVWL LRIFTPLLKG
HCAKTGITGL QECMECLGGI GYLENDDMQF NIARLYRDAN IVPIWEGTTD MMADDAILRV
LYGKNRTEVM RALSKWVTEV LEQNAREGSD IKTVASWWTD FKQTLIDLPK SDIERHARDI
MSRLVDIVQG LLLIIDAATD GNDVAQLVKE CWFADKCEGM SLKPSSRRSS TNLQASDMRI
VFRQAKLDPL GAKI
//
