ID A0A024UDR7_9STRA Unreviewed; 609 AA.
AC A0A024UDR7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Acyl-CoA dehydrogenase family member 11 {ECO:0000256|ARBA:ARBA00040622};
GN ORFNames=H310_03778 {ECO:0000313|EMBL:ETW04551.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW04551.1};
RN [1] {ECO:0000313|EMBL:ETW04551.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW04551.1};
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 -!- 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 ---------------------------------------------------------------------------
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; KI913957; ETW04550.1; -; Genomic_DNA.
DR EMBL; KI913957; ETW04551.1; -; Genomic_DNA.
DR EMBL; KI913957; ETW04552.1; -; Genomic_DNA.
DR RefSeq; XP_008865985.1; XM_008867763.1.
DR RefSeq; XP_008865988.1; XM_008867766.1.
DR RefSeq; XP_008865989.1; XM_008867767.1.
DR AlphaFoldDB; A0A024UDR7; -.
DR EnsemblFungi; H310_03778-t26_4; H310_03778-t26_4-p1; H310_03778.
DR EnsemblFungi; H310_03778-t26_5; H310_03778-t26_5-p1; H310_03778.
DR EnsemblFungi; H310_03778-t26_6; H310_03778-t26_6-p1; H310_03778.
DR EnsemblProtists; ETW04550; ETW04550; H310_03778.
DR EnsemblProtists; ETW04551; ETW04551; H310_03778.
DR EnsemblProtists; ETW04552; ETW04552; 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:InterPro.
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; 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; 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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136}.
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..598
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
SQ SEQUENCE 609 AA; 67627 MW; 047EE60B89FAB946 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 LVPMNARGRC
FQPRLVPFR
//
