ID A0A0W1GN82_9SPHN Unreviewed; 429 AA.
AC A0A0W1GN82;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KTE56274.1};
GN ORFNames=ATE69_07350 {ECO:0000313|EMBL:KTE56274.1};
OS Sphingopyxis sp. H071.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1759078 {ECO:0000313|EMBL:KTE56274.1, ECO:0000313|Proteomes:UP000054127};
RN [1] {ECO:0000313|EMBL:KTE56274.1, ECO:0000313|Proteomes:UP000054127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H071 {ECO:0000313|EMBL:KTE56274.1,
RC ECO:0000313|Proteomes:UP000054127};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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|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:KTE56274.1}.
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DR EMBL; LNSF01000003; KTE56274.1; -; Genomic_DNA.
DR RefSeq; WP_058454087.1; NZ_LNSF01000003.1.
DR AlphaFoldDB; A0A0W1GN82; -.
DR OrthoDB; 9780544at2; -.
DR Proteomes; UP000054127; 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 CDD; cd00567; ACAD; 1.
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; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 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 152..249
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 263..415
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 429 AA; 48833 MW; 3B2BB8DD3F749371 CRC64;
MDFAVPADLQ AYLDELDAFI EAEIRPLENA DDNIRFFDHR REHSRTDWDN QGLPRHEWEQ
LLRQATRLAD AAGHWRFSAP KKYGGKDGSN LWMAVIREHF AAKGLGLHND LQNEHSIVGN
FPFVEMFEQF ATSEEQKQEF ILGGFEGKRR TAFGLTEPDH GSDATHMETR AVRETRDGVD
GWLINGRKMW ITGMHVATHC ATFCRTDGQD GDAKGITCLL VPTGTEGMTV DEYMWTFNMP
TDHPRMTFSG VWVPDSARLG PVGGGLSIAQ SFVHQNRIRQ AASSLGAAVY CIEESVRYAR
SRKPFGEALA KNQAIQFPLV ELATQAEMLR LLIRKTAWEM DRTPHKEIER TLSDKVSMCN
YWANRLVCEA ADRAMQVHGG IGYSRHKPFE HIYRHHRRYR ITEGAEEIQM RKVAAYLFGY
MGPRKGTLG
//
