ID A0A178GIY4_9GAMM Unreviewed; 834 AA.
AC A0A178GIY4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=AY605_04355 {ECO:0000313|EMBL:OAL84883.1};
OS Acinetobacter sp. SFD.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1805635 {ECO:0000313|EMBL:OAL84883.1, ECO:0000313|Proteomes:UP000186186};
RN [1] {ECO:0000313|EMBL:OAL84883.1, ECO:0000313|Proteomes:UP000186186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFD {ECO:0000313|EMBL:OAL84883.1,
RC ECO:0000313|Proteomes:UP000186186};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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}.
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:OAL84883.1}.
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DR EMBL; LSZJ01000011; OAL84883.1; -; Genomic_DNA.
DR RefSeq; WP_064095512.1; NZ_LSZJ01000011.1.
DR AlphaFoldDB; A0A178GIY4; -.
DR STRING; 1805635.AY605_04355; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000186186; Unassembled WGS sequence.
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; 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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 139..233
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 359..499
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 513..797
FT /note="Acyl-CoA dehydrogenase C-terminal bacterial-type"
FT /evidence="ECO:0000259|Pfam:PF09317"
SQ SEQUENCE 834 AA; 92837 MW; AA63E77ACC66166C CRC64;
MLFIFAVLLL LLSLWAVFYF QLSRSAGAIT LIIMSVVCAF ISPWSLILGI PLILISLVVM
IEPLRMSFIS KPAYKALANA MPSISPTERE ALDSGTSWWE KELFMGAPNW ETFNNYPYPK
LSLEEQAFLD NEVEILCSML DEWEIHEQKA LPEHIWQYIK DHGFLGLIIP KEYGGRAFSS
FAQSRVMSKI SSRSLTTAVS CMVPNSLGPG ELLLHYGTEE QKNRYLPGLA RGEEIPCFGL
TSPEAGSDAG AIPDTGVVCY GQFEGQEVLG LRMNFSKRWI TLAPIATVVG LAFKMYDPDH
LLGEQTEYGI TCALLPASHE GVIVGPRHNP GPPFMNGTVE GKDVFIPLDW IIGGVKNAGK
GWRMLMECLA VGRGISLPAL STSTAEMTYL NVGAFSRIRQ QFKISVGKFE GVQEANSEIA
SDTYMLEAFR YLVTCGLNQG GKPAVMTAIA KYYATEGMRK VVNHGMDVVG GRAIQMGPRN
FLAPYYQAIP VSITVEGANI LSRSLMIFGQ GSMRCHPYLY EELQLLQAED RAAALNPFDD
LLFKHLGYTF NRTARSFAYA FTGGSSAAPQ SAVDFTRPYY KVINRLSANF ALTADMCLGL
LAGDIKRKEM LSGRLADIHA HLFIASAILK FFEHSKKTED ERLHAQLAVE KSLYTAQEAF
FDLFANFPSG AAAGMVKLLC FPFGRPVQKP SDQLKQQVAN SMMEDNAFRQ SLKKHVYYNI
NENDVTGRME STFNLLLEIE KLWDRFKKAE NKGQFKGLSF AEHVADAHQQ GFINDQEAEK
LLHYNARRYD SMLTDVFDLH LNEVLELENP YLIKEDAKGT DTSVQTDPSH SVSP
//
