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Database: UniProt
Entry: A0A091H243_BUCRH
LinkDB: A0A091H243_BUCRH
Original site: A0A091H243_BUCRH 
ID   A0A091H243_BUCRH        Unreviewed;       577 AA.
AC   A0A091H243;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Acyl-CoA dehydrogenase family member 9, mitochondrial {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=N320_05858 {ECO:0000313|EMBL:KFO88877.1};
OS   Buceros rhinoceros silvestris.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX   NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO88877.1, ECO:0000313|Proteomes:UP000054064};
RN   [1] {ECO:0000313|EMBL:KFO88877.1, ECO:0000313|Proteomes:UP000054064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO88877.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer
CC         flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:61526;
CC         Evidence={ECO:0000256|ARBA:ARBA00001337};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449;
CC         Evidence={ECO:0000256|ARBA:ARBA00001337};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + octadecanoyl-CoA + oxidized [electron-transfer
CC         flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:47240, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:71412;
CC         Evidence={ECO:0000256|ARBA:ARBA00000364};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241;
CC         Evidence={ECO:0000256|ARBA:ARBA00000364};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC         tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:47316, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61405;
CC         Evidence={ECO:0000256|ARBA:ARBA00001236};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317;
CC         Evidence={ECO:0000256|ARBA:ARBA00001236};
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   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; KL518608; KFO88877.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091H243; -.
DR   Proteomes; UP000054064; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01161; VLCAD; 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   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 2.
DR   InterPro; IPR049448; ACAD9/ACADV-like_C.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF21343; ACAD9-ACADV_C; 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; 2.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054064};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          15..123
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          127..227
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          240..393
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          464..534
FT                   /note="ACAD9/ACADV-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21343"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO88877.1"
FT   NON_TER         577
FT                   /evidence="ECO:0000313|EMBL:KFO88877.1"
SQ   SEQUENCE   577 AA;  63745 MW;  091438F8BCE8C59C CRC64;
     EEVFPYPEIS NEELEEINQF VGPVEKFFNE KVDSKKIDQD AKIPAETLEG LKDLGLFGMQ
     IPEEYGGLGL SNTMYARLGE ITSLDGSIAV TLAAHQAIGL KGILIAGTDD QKAKYLPRLA
     SGEHIAAFCL TEPGSGSDAA SIQTRATLSE DGKYFLLNGS KVWISNGGLA HIFTVFARTE
     VVDKDGQLKD KITAFIVERD FGGVTHGKPE DKLGIRGSNT CEVHFENTKV PIENVIGEVG
     GGFKVAMNIL NSGRFSMGSA SAGMIKKLIE MTAEYACTRK QFNKRLSDFG LIQEKFCYMA
     VKAYVMESMA YLTAGMMDRP GFPDCSVEAA MVKVFSSEGA WACVSEALQI LGGLGYMKDY
     PYERYLRDTR ILLIFEASTD TLGTNEILRM YIALTGMQYA GKILTDKIKE IRKGNVGMAL
     GEFLSKLRDA MGRKVDYGLV GDRGVVHPSL QESGKKLEEN IYYFGTTVKG LLSRFGKTIV
     DEQLILKRVA DIVINLYAMK AAISRASRSI SIGLRNHDHE VLLTNIFCTE AYFKNNYAMA
     QLEKYADENL DDCIKKAAKQ VLEKRSYICS HPLDRTF
//
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