ID A0A1W9IKN0_9PROT Unreviewed; 756 AA.
AC A0A1W9IKN0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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:OQW60236.1};
GN ORFNames=A4S14_19000 {ECO:0000313|EMBL:OQW60236.1};
OS Proteobacteria bacterium SG_bin9.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1827385 {ECO:0000313|EMBL:OQW60236.1, ECO:0000313|Proteomes:UP000192684};
RN [1] {ECO:0000313|EMBL:OQW60236.1, ECO:0000313|Proteomes:UP000192684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG_bin9 {ECO:0000313|EMBL:OQW60236.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQW60236.1}.
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DR EMBL; LWDM01000017; OQW60236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9IKN0; -.
DR STRING; 1827385.A4S14_19000; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000192684; Unassembled WGS sequence.
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; 2.
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 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; 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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 88..175
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 180..270
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 303..450
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 457..729
FT /note="Acyl-CoA dehydrogenase C-terminal bacterial-type"
FT /evidence="ECO:0000259|Pfam:PF09317"
FT REGION 735..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 83417 MW; 0A764E74274203E3 CRC64;
MTAFSLRRDL LSRPILSWAR KAMPAMSDTE REALEAGDVW WDADLFTGTP DWDKLLAYPQ
ATLTAEEEAF LNGPVDELCN MLDDWKINWE LRDLPPEVWD FIKAKRFFGM IIPKEYGGLG
FSPYAHSEVV RKVSSRSCAA AVTVMVPNSL GPGELLMRFG TKEQQDRWLP RLADGRDIPC
FGLTSPEAGS DAASMIDTGI ICKGQFEGRE VIGLKLNWHK RYITLGPVAT LLGLAFKAYD
PDHLIGSEED LGITVALIPT DLPGVEIGRR HLPAMQVFQN GPNWGRDVFI PTDYIIGGQE
RLGQGWKMLM TALAAGRGIS LPSLSAAAAA YSARTTGAYA RIREQFGISI SKFEGIEEPL
ARIAAFAYQI DAARRLTCSA LNQGNHPAVI SGIMKLHATE RMRIAIDDAM DVHGGKAVID
GPQNYLGNLY RAVPVGITVE GANILTRNLI VFGQGAIRAH PYMLEELTAI GDPDKAKGLE
AFDKVFWKHV GHAFKNVFVA WGRSWSRGAF APAPDAGLAT RYYRKLSRYS VAFALCADMA
LLTLGGALKR KEMLSARFGD ILSELYLMSA VLKRWNDEGR QQEDFAAVQW CMSNGSRIID
QRFCEILANL PNRFVAFFLK IIVQPFGARV LGPSDDIVHR CAQLVLSPSA ARERLTSGLS
HVDDDGPIAR LERAFKLVTG NEDIEHKMKA ARQRDWKAAL KAGVITAADG ERMQAADDAI
SKVINVDDFA PEALSPIDRK RDQRFPQEVS PHRAAS
//
