ID B1KHJ6_SHEWM Unreviewed; 815 AA.
AC B1KHJ6;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
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};
DE Flags: Precursor;
GN OrderedLocusNames=Swoo_2604 {ECO:0000313|EMBL:ACA86881.1};
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA86881.1, ECO:0000313|Proteomes:UP000002168};
RN [1] {ECO:0000313|EMBL:ACA86881.1, ECO:0000313|Proteomes:UP000002168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-2008) 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; CP000961; ACA86881.1; -; Genomic_DNA.
DR RefSeq; WP_012325221.1; NC_010506.1.
DR AlphaFoldDB; B1KHJ6; -.
DR STRING; 392500.Swoo_2604; -.
DR KEGG; swd:Swoo_2604; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_012192_0_0_6; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000002168; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd00567; ACAD; 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; 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; IPR047634; FadE.
DR InterPro; IPR015396; FadE_C.
DR NCBIfam; NF038187; FadE_coli; 1.
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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002168};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..233
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 361..508
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 515..796
FT /note="Acyl-CoA dehydrogenase C-terminal bacterial-type"
FT /evidence="ECO:0000259|Pfam:PF09317"
SQ SEQUENCE 815 AA; 89553 MW; A060AA7C545E978B CRC64;
MTTLLWTLAM LFVLGALTYL RVSLLTSSFI AAIVLTIGTA AEAVSPLTWI IFLVIALPLN
ISSFRKNFLT KPMLKMYRGI MPEMSSTEKE AIEAGTTWWD ADIFAGKPDW QKLHNYPAAR
LTAEEQAFLD GPVEEVCKML NQHQVSHELG DLPQEIWQYL KDHGFFAMII KKKYGGLEYS
AYAQSRVLQK LAGVSSELAS TVGVPNSLGP GELLQHYGTP AQQDHYLPRL AKGLEVPCFA
LTSPEAGSDA GAIPDFGIVC KGQWEGEEVL GMKLTWNKRY ITLAPVATVL GLAFKLQDPD
KLLGDKEELG ITCALIPTDI DGVETGRRHF PLNCMFQNGP TRGNEVFVPL SFIIGGPEMA
GQGWRMLVEC LSVGRGITLP SNSAGGIKTA AVATGAYARI RRQFKLPIGK LEGIEEPMAR
IGGNAYLMEA VTSLTTTGID LGEKPSVISA IVKFHLTDRM QKCVIDAMDI HGGKGVCLGP
NNYLGRGYQA APIAITVEGA NILTRSMIIY GQGAIRCHPY VLAEMESAFD TDAEKGLNDF
DAAIFGHIGF TASNLVRSFW LGLTSSRFSN APYSDKTKRY YQHMNRFSAN LALLSDLAMA
TLGGDLKRKE RISARLGDLL SQLYLSSATL KRYQDEGRQT EDLALVQWAV EDSLYKLQDS
LDDLLDNFPM GLGRVLRVIM FPFGRPLKRP SDILDHKVAK IMQTPCASRD RLAKGQFLTA
CENNPVGIQE QTFKDIIACE PLHDKVCKAA GKRLPFIWLD KVAAEGKALG ILSEDEISLL
ERTEIGRMKS INVDDFDPDE LKAMVVAKTK HEQAA
//
