ID A0A1J0WJU0_9RHOB Unreviewed; 754 AA.
AC A0A1J0WJU0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Acyl-coenzyme A dehydrogenase {ECO:0000256|ARBA:ARBA00020144};
DE EC=1.3.8.7 {ECO:0000256|ARBA:ARBA00012033};
DE EC=1.3.8.8 {ECO:0000256|ARBA:ARBA00012040};
GN Name=fadE {ECO:0000313|EMBL:APE44586.1};
GN ORFNames=BOO69_15070 {ECO:0000313|EMBL:APE44586.1};
OS Sulfitobacter alexandrii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1917485 {ECO:0000313|EMBL:APE44586.1, ECO:0000313|Proteomes:UP000181897};
RN [1] {ECO:0000313|EMBL:APE44586.1, ECO:0000313|Proteomes:UP000181897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM1-D1 {ECO:0000313|EMBL:APE44586.1,
RC ECO:0000313|Proteomes:UP000181897};
RA Yang Q., Zhang X., Tian X.;
RT "Complete genome sequence of Sulfitobacter sp. AM1-D1, a toxic bacteria
RT associated with marine dinoflagellate Alexandrium minutum in East China
RT Sea.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721,
CC ChEBI:CHEBI:83727; EC=1.3.8.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723,
CC ChEBI:CHEBI:83726; EC=1.3.8.7;
CC Evidence={ECO:0000256|ARBA:ARBA00034035};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; CP018076; APE44586.1; -; Genomic_DNA.
DR RefSeq; WP_071972934.1; NZ_CP018076.1.
DR AlphaFoldDB; A0A1J0WJU0; -.
DR STRING; 1917485.BOO69_15070; -.
DR KEGG; suam:BOO69_15070; -.
DR OrthoDB; 9802447at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000181897; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; 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; 1.
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 InterPro; IPR015396; FadE_C.
DR PANTHER; PTHR48083:SF18; ACYL-COENZYME A DEHYDROGENASE; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF09317; ACDH_C; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT DOMAIN 81..173
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 301..448
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 455..725
FT /note="Acyl-CoA dehydrogenase C-terminal bacterial-type"
FT /evidence="ECO:0000259|Pfam:PF09317"
FT REGION 731..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 82687 MW; 26D7573EECA24096 CRC64;
MSSIRAKYIT KPIHKWAKGA LPALSSTESE ALQAGEVWWE AELFSGNPDW KKLHAVKAPR
LSEEEQAFFD GPVQELCGMI DDWKINHEDG DLPDEVWQFL RDKKFFGMII PKSYGGLEFS
AFAHSEIVRY ISSRSVAAAV TVMVPNSLGP GELLHQFGTK EQKDHWLPRL ADGRELPAFG
LTSAEAGSDA SAMIDTGVVC KGMWEGEEVL GLRLNWAKRY ITLSPVCTVL GLAFQMRDPD
GLLGDQEDIG ITCALVPTDL DGVETGRRHL PSSTMFMNGP TTGTDVFIPL DNIIGGQEYA
GRGWMMLMSA LAAGRGISLP SMGCAAIALS AHTTGAYSRI RQQFNLPIGK FGGIQDRMGR
LAADSYAMDA ARHLTCAGLD EGRALSVISA IMKAHATFRM REALNDAMDV HSGKAVIDGP
SNYLLPLYRA VPIGITVEGA NIVTRSLIIF GQGSIRAHPH MLDNMLALQE EDEQKSLEMF
DKSFWAHVGH TTKTLFRAWG RAITGGRTGT TANFGPAKPI YQELSRWSAA YALTADFAFL
TLGGALKRKE MISARMGDIL SEMYILSAAL KRWEDEGRQE ADLPVLQYAA DAGFKRIQVA
LDEVIANMPA RWAAYILRFI TLPGATRRGP NDRLTAKVSD VIYEPSEARD RVIGRLHGGK
EGDGIHTLNA CFAKVVEMAP VMKRLRDARK TPEQAKEAGT LSDSELTQIK EMNTLVDKVV
AVDDYTPEEL SRIFKDHGAT SSDDYRATPR EAAE
//
