ID A0A0F8AYD4_CERFI Unreviewed; 455 AA.
AC A0A0F8AYD4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acyl-CoA dehydrogenase family member 11 {ECO:0000313|EMBL:KKF93301.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:KKF93301.1};
GN Name=ACAD11_2 {ECO:0000313|EMBL:KKF93301.1};
GN ORFNames=CFO_g4341 {ECO:0000313|EMBL:KKF93301.1};
OS Ceratocystis fimbriata f. sp. platani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF93301.1, ECO:0000313|Proteomes:UP000034841};
RN [1] {ECO:0000313|EMBL:KKF93301.1, ECO:0000313|Proteomes:UP000034841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFO {ECO:0000313|EMBL:KKF93301.1,
RC ECO:0000313|Proteomes:UP000034841};
RA Belbahri L.;
RT "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT trees.";
RL Submitted (APR-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:KKF93301.1}.
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; LBBL01000256; KKF93301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8AYD4; -.
DR Proteomes; UP000034841; 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:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 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 ECO:0000313|EMBL:KKF93301.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034841}.
FT DOMAIN 47..139
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 144..246
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 260..409
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 455 AA; 50061 MW; C9977F8F3E21B191 CRC64;
MSDRIPALVR DKVSERAKKT LDLVAKFVVD ECIPADPVLN AQIGVGDARW ESHPAVIEEL
KTKAREQGLW NLFLPTGTYS QGAGFTNLEY GLMAEWTGRS HVAAEAMNCA APDTGNMEVL
AKYGNDAQKA RWLEPLLQGH IRSAFLMTEP AVASSDATNI ELSIRKDGDY FVLNGQKWWS
SGAGDPRCKL YIVMGKTDAK NPSPYKQQSV ILVPSDTPGI TINRMLSVYG YDDAPHGHGH
ITFKDVRVPA ANLVLGEGCG FEIIQGRLGP GRIHHAMRTI GAAEQALDWM IMRINDTKRT
PFGKLLKEHG VVLEWVARSR LEIDAARLIV LNAAIQMDEL GPKKALKEIA EAKILAPKTA
LDVIDRAVQA FGAAGVSQDT PLAASWAGIR TLRIADGPDE VHLQQMGRNE AKRGTEVAET
ILRQKRKTEE LLKAWKVERN EPGTKIRRQR SGSKL
//
