ID A0A0R2TZP4_9GAMM Unreviewed; 408 AA.
AC A0A0R2TZP4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 08-NOV-2023, entry version 18.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KRO92545.1};
GN ORFNames=ABS24_02600 {ECO:0000313|EMBL:KRO92545.1};
OS SAR92 bacterium BACL26 MAG-121220-bin70.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Porticoccaceae; SAR92 clade.
OX NCBI_TaxID=1655626 {ECO:0000313|EMBL:KRO92545.1, ECO:0000313|Proteomes:UP000051213};
RN [1] {ECO:0000313|EMBL:KRO92545.1, ECO:0000313|Proteomes:UP000051213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL26 MAG-121220-bin70 {ECO:0000313|EMBL:KRO92545.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KRO92545.1}.
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DR EMBL; LICA01000324; KRO92545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2TZP4; -.
DR Proteomes; UP000051213; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; 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 PANTHER; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 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, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT DOMAIN 7..127
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 131..225
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 237..387
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 408 AA; 44841 MW; 42BBCBEF0323E34C CRC64;
MDFNDTHQEA AFRATCRDWL EENARLKGGA GNDQRYGKVD EQDFLNSARA WQKKKFDAGW
AMLHWPKHYG GLEASAIERI IWSQEEAKFN VPHGVYEIGL GMAGPVMMQY ASDQQKSRYL
PPMAAGEEIW CQLFSEPSAG SDVAGLRSKA VQDGDDWIIN GQKVWTSGAH FCDYGIIVVR
HDPNVEKHAG MTFFFIDMKS PGIDIKPIKQ ITGGSSFNEV YFNDVRIPDS QRLGAIGDGW
RVAITTLMNE RLAVGDANGT DAKEAFEWAQ GQDDHGQPLI KNRGVRESIA DWYCQASGLK
NTKLRTMSAL SKGDTPGPEA SITKVVSANK LQAIGNFGID SLDMAGMLKT DDADVQSFHD
AWLGSAGLRI AGGTDEILRN IIAERVLGLP QDPRADKGLA FKDIPSGN
//
