ID A0A0F7M1X6_9GAMM Unreviewed; 812 AA.
AC A0A0F7M1X6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 ORFNames=IMCC21906_00596 {ECO:0000313|EMBL:AKH68289.1};
OS Spongiibacter sp. IMCC21906.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Spongiibacter.
OX NCBI_TaxID=1620392 {ECO:0000313|EMBL:AKH68289.1, ECO:0000313|Proteomes:UP000035013};
RN [1] {ECO:0000313|EMBL:AKH68289.1, ECO:0000313|Proteomes:UP000035013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC21906 {ECO:0000313|EMBL:AKH68289.1,
RC ECO:0000313|Proteomes:UP000035013};
RA Cho J.-C., Yang S.-J., Kang I.;
RT "Complete genome sequence of IMCC21906 belonging to the
RT Gammaproteobacteria.";
RL Submitted (MAY-2015) 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; CP011477; AKH68289.1; -; Genomic_DNA.
DR RefSeq; WP_047010913.1; NZ_CP011477.1.
DR AlphaFoldDB; A0A0F7M1X6; -.
DR STRING; 1620392.IMCC21906_00596; -.
DR KEGG; spoi:IMCC21906_00596; -.
DR PATRIC; fig|1620392.3.peg.642; -.
DR OrthoDB; 6138585at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000035013; 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 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; 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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:AKH68289.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035013};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 130..236
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 240..334
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 362..508
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 515..798
FT /note="Acyl-CoA dehydrogenase C-terminal bacterial-type"
FT /evidence="ECO:0000259|Pfam:PF09317"
SQ SEQUENCE 812 AA; 89469 MW; 96F929D19CFB637C CRC64;
MTGLLSVLFL LVVFMSIFYL GLSLRRGSAV FFLAWLLAGS GCEFFLHPLS LLLLLAVLAV
LNVQSLRMRF LSAPAKKMLA GMMPSLGDTE REALEAGTTW WEKDMFSGRP DWDKFAAIDL
PVMTPAEQSF IDNEVEELCA MLDEWDIYHR RKDLPEEVWQ YIKDKGFLGL IIPEEYGGKH
FSPYAQSRTV GKIASRSTVA AVSVMVPNSL GPGELLVKYG TDEQKQYWLP KLAVGEEVPC
FGLTSPEAGS DAGAIPDVGI VCRQEYEGQD TLGVKLSFSK RWITLAPIAT VVGLAFKLRD
PEGLIGDQVE RGITCALVPA SQPGMEIGRR HNPGSPFMNG PMTGVEVFIP MSMLIGGQER
VGQGWRMLVE CLGAGRGVSL PALSTAGGEM SYLMVGAFAR IRRQFGISVG KFEGVQEATA
DIAASGYTLE AYRAFVTRAL EDGAPSVLTA MAKYHATEMM REVVNDSMDV LGGRGIQMGP
RNFMALVYQS IPIAITVEGA NILTRSMIIF GQGAIRCHPY LAEELVVIQE EGEEALLRFD
ELLTAHLGHA IGVICRAIAK GVTAGWLAAP KKDTAFSKRW YRYLDRYSAA LAASADIALA
TLGGDLKRKE LLSARLGDVH SQLVIACALL KYQESLPDTE ANRLHAEYSL RRCFKALNIS
LNAFYDNLPV PGLGMVMRRL FFPWGTPVPT LRDSQIRRLG SLIMEPNDVR KALSEAVFIS
KDPEDSTGRV NVTYQELIEL EDDYDRFLKA ESKGELSGKS VDDRIDNAAE KGLFSAEMAE
RLKRYEARRY DCLLTDAFDP TLENVDIRIA RP
//