ID A0A3R9FMY0_9VIBR Unreviewed; 816 AA.
AC A0A3R9FMY0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=EJA03_07120 {ECO:0000313|EMBL:RSD31789.1};
OS Vibrio pectenicida.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=62763 {ECO:0000313|EMBL:RSD31789.1, ECO:0000313|Proteomes:UP000269041};
RN [1] {ECO:0000313|EMBL:RSD31789.1, ECO:0000313|Proteomes:UP000269041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 594 {ECO:0000313|EMBL:RSD31789.1,
RC ECO:0000313|Proteomes:UP000269041};
RA Gomez-Gil B., Enciso-Ibarra K.;
RT "Genomic taxonomy of the Vibrionaceae family.";
RL Submitted (DEC-2018) 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:RSD31789.1}.
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DR EMBL; RSFA01000023; RSD31789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9FMY0; -.
DR OrthoDB; 9802447at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000269041; 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; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 146..234
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 816 AA; 89200 MW; 3531AFC12AA80A66 CRC64;
MDTLISILGF SAVLAVCLYH RTTLVKSMVA LTATLLVLSA LGTAGSVSWI LFIVAAAVLT
IPSIRQSLIS KKALTVFRKV LPEMSQTEKE ALDAGTVWWE AELFKGKPNW QQLHDIQAPQ
LTAEEQAFLD GPVNEVCAMV NDYQVTHELA DLPPQVWQYL KDNQFFAMII KKKYGGLEFS
AYAQSLVLQK LTGVSSVLSS TVGVPNSLGP GELLQHYGTK DQKDYYLPRL AEGKEIPCFA
LTSPEAGSDA GSIPDFGVVC KGDWEGKEVV GMRLTWNKRY ITLAPIATVL GLAFKLRDPE
GLLGDQQEMG ITCALIPTNL KGVEIGSRHF PLNVPFQNGP TRGEDLFVPL DFIIGGPKMA
GQGWRMLVEC LSVGRGITLP SNSTGGIKTA ALATGAYARI RRQFKQPIGQ MEGVEEPLAR
LGGNAYVMDA ASNLTVAGID LGEKPSVISA IVKYHCTHRG QQSIIDAMDI LGGKGICLGP
SNFLARSYQG APIAVTVEGA NILTRSMIIY GQGAIRCHPY VLEEMDAAYS EDSDALDKFD
SALAGHVSFT LSNLVRSFWL GLTDGRFSAS PVKDSTSRYY QQLNRYSANI AFLSDISMAV
LGGSLKRKER LSARLGDILS QLYLSSATLK RFENDGRIAE DLPLLHWGLQ DSLKQAEAAI
DELLVNFPNK WLGKALRVIT LPFGLVRKAP SDQLDSEVAQ ILQTPSATRE RLGRNQYFQA
SEFNPAGKVE QALHVILQAE PIFNKVCKAL DERRPFLRLD LIADMGLEKG IIDSDDAQLL
RNAEQHRLYV ISVDDFDPKD LAAMPSEVFP LMDEVA
//
