ID A0A1Z8TI63_9PROT Unreviewed; 386 AA.
AC A0A1Z8TI63;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RPF99353.1};
GN ORFNames=CBC11_010220 {ECO:0000313|EMBL:RPF99353.1};
OS Proteobacteria bacterium TMED51.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1986847 {ECO:0000313|EMBL:RPF99353.1, ECO:0000313|Proteomes:UP000196292};
RN [1] {ECO:0000313|EMBL:RPF99353.1, ECO:0000313|Proteomes:UP000196292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED51 {ECO:0000313|EMBL:RPF99353.1};
RX PubMed=28713657; DOI=10.7717/peerj.3558;
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 metagenome-assembled genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL PeerJ 5:e3558-e3558(2017).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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:RPF99353.1}.
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DR EMBL; NHDE02000043; RPF99353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z8TI63; -.
DR Proteomes; UP000196292; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR006089; Acyl-CoA_DH_CS.
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 PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF43; ACYL-COA DEHYDROGENASE; 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 PIRSF; PIRSF016578; HsaA; 3.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT DOMAIN 6..117
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 121..220
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 233..380
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 386 AA; 43370 MW; FD989BAECBF22B0D CRC64;
MDFALSEEQQ MLIDSARTFA EKELYPYEDE VESSDEVRPE LAQQIRDRAI EQGFYAANMP
EELGGGGLDS VSLSLVEREL GRANFALQYL VGRPSNILQA CVGEQRERYL FPCIRGEKTD
CLAMTEPGAG SDLRSMQCRA ERDGDDYIIN GTKHFISHAD IADFVILFAA TGEEASSRGP
RKLISSFLVD KGTSGFTVRR GYHSVSHRGY HNCILEFENC RVPASQMLGA EHQGFNVAND
WLGATRLQVA AMCLGRAYRA LEHATDWAAE RQQFGQFIGR FQGIGFKLAE MKMQLEAAEL
LTLKAAWKTD HGTATDTDYA MAKLHATEML AFVADEAIQI HGGMGLMSDL PLERIWRDAR
VERIWEGTSE IQRHIISRDM LRPRWT
//
