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Database: UniProt
Entry: A0A068Y0C9_ECHMU
LinkDB: A0A068Y0C9_ECHMU
Original site: A0A068Y0C9_ECHMU 
ID   A0A068Y0C9_ECHMU        Unreviewed;       669 AA.
AC   A0A068Y0C9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Acyl-CoA dehydrogenase family member 9, mitochondrial {ECO:0000313|EMBL:CDS35579.1};
GN   ORFNames=EmuJ_000315200 {ECO:0000313|EMBL:CDS35579.1};
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS35579.1};
RN   [1] {ECO:0000313|EMBL:CDS35579.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23485966; DOI=10.1038/nature12031;
RA   Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA   Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA   Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA   De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA   Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA   Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA   Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA   Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA   Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA   Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA   Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA   Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA   Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT   "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL   Nature 496:57-63(2013).
RN   [2] {ECO:0000313|EMBL:CDS35579.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-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}.
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DR   EMBL; LN902253; CDS35579.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068Y0C9; -.
DR   STRING; 6211.A0A068Y0C9; -.
DR   eggNOG; KOG0137; Eukaryota.
DR   OMA; GPHEDKM; -.
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; 2.
DR   InterPro; IPR049448; ACAD9/ACADV-like_C.
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; 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}.
FT   DOMAIN          115..204
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          208..310
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          334..470
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          567..631
FT                   /note="ACAD9/ACADV-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21343"
SQ   SEQUENCE   669 AA;  74229 MW;  F014D90376852EEE CRC64;
     MLHRVMAIAS RRGHQHCVFF STTAETPTAS QKELDDERLI LPSLKKLVNH SKVAMQMPDM
     TRKYAVSDAP LIPSYFLGKL QLELLEYPEL PTKEEVIQIN NLFTTVEDWV TKVDSKSIDE
     KGAIPEEVLR DCKIMGLFGQ RVNPSYGGLD MTPLESVLVA EAMGYDPSLF ATVTVHEALG
     LKGLQLVGTE AQKEKYLPAL ASGEKIAAFC LTEVSSGATS TQSQTRAVLS PDSRHYILNG
     RKAWVVNGSR ADVFTVFALT SIPNEKGENE DRLSAFLVER GFEGTIEVQP PLERIGLRGL
     DLVDVTFKDV QVPVENVLGA LGSGTELSGR IACSERYLVG GLCVGLCRNV LDALTEHCSM
     RHQFGRPLSH FGVVQRRLAH AAAQLYAMES VTYLVAGFLT SRPQRDLAIE SSAVKLFATE
     TTLTLLNDCV ALAGALGFTK QLPLERYLRD SRVLTSFMGV NDLLRIYIAS TSLSKVGKEL
     RHFVECARSP SQHMWYMLRE AWRKDWRTAI LTRLWGISPS IVTAATMETE RGIRASTRVG
     DHLHPNLQAL GDRLARLVVQ TYELTRQVFI LHANTVNEDQ FSLWLLSDLA VGLFTATAVL
     SRASRAKSIG VRYHNNELEL AELFTLETLD RLQGELSSFK QKANLRKRIA SVMVKESGYA
     SASPLSRVW
//
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