ID A0A024UE53_9STRA Unreviewed; 688 AA.
AC A0A024UE53;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Acyl-CoA dehydrogenase family member 11 {ECO:0000256|ARBA:ARBA00040622};
GN ORFNames=H310_03778 {ECO:0000313|EMBL:ETW04549.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW04549.1};
RN [1] {ECO:0000313|EMBL:ETW04549.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW04549.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexacosanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexacosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48216, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:64868, ChEBI:CHEBI:74281;
CC Evidence={ECO:0000256|ARBA:ARBA00036134};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48217;
CC Evidence={ECO:0000256|ARBA:ARBA00036134};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47232, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693;
CC Evidence={ECO:0000256|ARBA:ARBA00001765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233;
CC Evidence={ECO:0000256|ARBA:ARBA00001765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC tricosanoyl-CoA = (2E)-tricosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48220, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:90118, ChEBI:CHEBI:90119;
CC Evidence={ECO:0000256|ARBA:ARBA00036394};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48221;
CC Evidence={ECO:0000256|ARBA:ARBA00036394};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:44704, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:58856, ChEBI:CHEBI:65111;
CC Evidence={ECO:0000256|ARBA:ARBA00036627};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44705;
CC Evidence={ECO:0000256|ARBA:ARBA00036627};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-docosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47228, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:65059, ChEBI:CHEBI:74692;
CC Evidence={ECO:0000256|ARBA:ARBA00000286};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229;
CC Evidence={ECO:0000256|ARBA:ARBA00000286};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:74691;
CC Evidence={ECO:0000256|ARBA:ARBA00000733};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237;
CC Evidence={ECO:0000256|ARBA:ARBA00000733};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; KI913957; ETW04548.1; -; Genomic_DNA.
DR EMBL; KI913957; ETW04549.1; -; Genomic_DNA.
DR RefSeq; XP_008865986.1; XM_008867764.1.
DR RefSeq; XP_008865987.1; XM_008867765.1.
DR AlphaFoldDB; A0A024UE53; -.
DR EnsemblFungi; H310_03778-t26_2; H310_03778-t26_2-p1; H310_03778.
DR EnsemblFungi; H310_03778-t26_3; H310_03778-t26_3-p1; H310_03778.
DR EnsemblProtists; ETW04548; ETW04548; H310_03778.
DR EnsemblProtists; ETW04549; ETW04549; H310_03778.
DR GeneID; 20080828; -.
DR VEuPathDB; FungiDB:H310_03778; -.
DR OrthoDB; 276350at2759; -.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
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; cd05154; ACAD10_11_N-like; 1.
DR Gene3D; 3.90.1200.10; -; 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 InterPro; IPR041726; ACAD10_11_N.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
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; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_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 Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU362125};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Flavoprotein {ECO:0000256|RuleBase:RU362125};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT DOMAIN 40..282
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT DOMAIN 456..517
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 522..619
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 637..670
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 688 AA; 76063 MW; 66B744A9FD09D648 CRC64;
MSHDAGADVE PMRQPLDLDR LRVYLEGHFS LEGKNVPLSV NQFKHGQSNP TYLVEFGAKR
LVLRKKPAGN ILPSAHAVDR EYRVMEALQT TAVPVPRMVS FCNDPSVLGT TFFLMEYVPG
RVFKDPSLPN MSPTERYAIY HALVDVLATL HSLDPASLGL EDFGKAQNYG QRVLRTWTRQ
YNAQGDVLTQ HAVSIGGDRD MLAVSDYLHS AVDSIQDESS IVHGDFRLDN AIFHPTEPRI
VALLDWELST IGHPLSDVAT LCSFYRVPST SQMIPGLAKR NLQHLGIPTE AEVVRTYCKR
MQRYPLADST WRFFLALVFF RLAVILQGVY SRQVLGNASS AHAGVAKDCY VLFMQVGATI
AREDSAGNSI ASTPNPSVLG LPMSDYALEL YGKLTRFCEA RVFPSEVVHM KELAALRKAG
KTWTSVPPIV ETLKEEAKAL GLWNLFLAPV TLPNGKSYGA KLSNVEYGIM CELMGRCVTL
APEVFNCAAP DTGNMEILSR FGTPDQQAQW LVPLCEGTIR SCFAMTERYV ASSDATNVCT
QFEKRDDGYV INGDKWYISG AGDPRCQLII VMGKIKTHAK LSSFRQQSMI LVPMNARGVA
VKRPMHVFGY DDAPHGHMEV SFRDVRVPLT SILLGDGRGF EIAQARLGPG RIHHCMRAIG
MAERCMDLMV TNIGALFKSD EYSAGPSS
//
