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Database: UniProt
Entry: I3YW13_AEQSU
LinkDB: I3YW13_AEQSU
Original site: I3YW13_AEQSU 
ID   I3YW13_AEQSU            Unreviewed;       380 AA.
AC   I3YW13;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AFL81181.1};
GN   OrderedLocusNames=Aeqsu_1700 {ECO:0000313|EMBL:AFL81181.1};
OS   Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aequorivita.
OX   NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL81181.1, ECO:0000313|Proteomes:UP000006049};
RN   [1] {ECO:0000313|EMBL:AFL81181.1, ECO:0000313|Proteomes:UP000006049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC   {ECO:0000313|Proteomes:UP000006049};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA   Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA   Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Aequorivita sublithincola DSM 14238.";
RL   Submitted (JUN-2012) 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; CP003280; AFL81181.1; -; Genomic_DNA.
DR   RefSeq; WP_014782436.1; NC_018013.1.
DR   AlphaFoldDB; I3YW13; -.
DR   STRING; 746697.Aeqsu_1700; -.
DR   KEGG; asl:Aeqsu_1700; -.
DR   PATRIC; fig|746697.3.peg.1731; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_10; -.
DR   OrthoDB; 9802867at2; -.
DR   Proteomes; UP000006049; Chromosome.
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; cd01158; SCAD_SBCAD; 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; 1.
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; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   PIRSF; PIRSF016578; HsaA; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN          6..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          231..378
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   380 AA;  41782 MW;  9C4F1AEA2BFCDFA7 CRC64;
     MDFSLSEEQM MIRDAARDFA RTELLPGVIE RDNLQKFPAE QVKKMGELGF LGMMVDPKYG
     GGGMDTMSYV LVMEELSKID ASCSVIVSVN NSLVCYGLEK YGSEDQKQKY LTKLATGEKL
     GAFCLSEPEA GSDATSQKTT AIEDGDHYII NGTKNWITNG GTADYYLVIA QTHKEKKHKG
     INAFIVEKGW EGFEIGPKED KLGIRGSDTH SLIFNDVRVP KENRIGEDGF GFSFAMKTLA
     GGRIGIAAQA LGIAAGAYDL AREYSKVRKA FGTEICNHQA IAFKLADMHT SITAARHLVM
     KAAWDKDQGN DYDMSGAMAK LFASQTAMDV SVEAVQVHGG NGFVKEYHVE RMMRDAKITQ
     IYEGTSEIQK IVISRGLLRD
//
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