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Database: UniProt
Entry: A0A0B4XN37_9GAMM
LinkDB: A0A0B4XN37_9GAMM
Original site: A0A0B4XN37_9GAMM 
ID   A0A0B4XN37_9GAMM        Unreviewed;       386 AA.
AC   A0A0B4XN37;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:AJD48471.1};
GN   ORFNames=S7S_10295 {ECO:0000313|EMBL:AJD48471.1};
OS   Isoalcanivorax pacificus W11-5.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Isoalcanivorax.
OX   NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD48471.1, ECO:0000313|Proteomes:UP000006764};
RN   [1] {ECO:0000313|EMBL:AJD48471.1, ECO:0000313|Proteomes:UP000006764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W11-5 {ECO:0000313|EMBL:AJD48471.1,
RC   ECO:0000313|Proteomes:UP000006764};
RX   PubMed=23209202; DOI=10.1128/JB.01845-12;
RA   Lai Q., Shao Z.;
RT   "Genome sequence of an alkane-degrading bacterium, Alcanivorax pacificus
RT   type strain W11-5, isolated from deep sea sediment.";
RL   J. Bacteriol. 194:6936-6936(2012).
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; CP004387; AJD48471.1; -; Genomic_DNA.
DR   RefSeq; WP_008735211.1; NZ_CP004387.1.
DR   AlphaFoldDB; A0A0B4XN37; -.
DR   STRING; 391936.S7S_10295; -.
DR   KEGG; apac:S7S_10295; -.
DR   HOGENOM; CLU_018204_0_3_6; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000006764; 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   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   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006764}.
FT   DOMAIN          4..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          123..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..376
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   386 AA;  42892 MW;  497A3AFFCFF3088B CRC64;
     MLFTQEHEEL RRTVRNFVEK EINPYVDEWE NSPPFPAHEL FKKLGNLGLL GISKPVEYGG
     MGLDYTYSIV ASEEFGGIRC GGVPMAIGVQ TDMATPALAR FGSDELRREF LAPAIAGDMV
     ASIAVSEPHA GSDVANIKTT ARKDGDDYVI NGTKMWITNS TQNDFFCLLA NTGDGPKHMN
     KSLIVVPKKT PGISVSEPLN KLGMRSSDTA QVFFDDVRVP QRYCIGQEGM GFMMQMMQFQ
     EERLFAAANS LRGMDVAIAE TIDYCRTRQV FDMPLIDNQV VHFRLAELKS EVELLRALIY
     QASEEYVNGK DVLQKASIAK LKAGRLAREV YDSCLQYWGG QGFMWDSMVA RGYRDCRLGS
     IGGGADEIML GIICKTMDIL PGKKKK
//
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