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Database: UniProt
Entry: A0A437MA00_9SPHN
LinkDB: A0A437MA00_9SPHN
Original site: A0A437MA00_9SPHN 
ID   A0A437MA00_9SPHN        Unreviewed;       388 AA.
AC   A0A437MA00;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RVT94454.1};
GN   ORFNames=EOD43_11645 {ECO:0000313|EMBL:RVT94454.1};
OS   Sphingomonas crocodyli.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1979270 {ECO:0000313|EMBL:RVT94454.1, ECO:0000313|Proteomes:UP000282971};
RN   [1] {ECO:0000313|EMBL:RVT94454.1, ECO:0000313|Proteomes:UP000282971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCP-7 {ECO:0000313|EMBL:RVT94454.1,
RC   ECO:0000313|Proteomes:UP000282971};
RA   Chen W.-M.;
RL   Submitted (JAN-2019) 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:RVT94454.1}.
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DR   EMBL; SACN01000001; RVT94454.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A437MA00; -.
DR   OrthoDB; 9780544at2; -.
DR   Proteomes; UP000282971; 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:SF3; ACYL-COA DEHYDROGENASE FADE29; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN          39..127
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          132..224
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          237..382
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   388 AA;  42842 MW;  7D048F29BF7AFFC1 CRC64;
     MSELDDFRAE TRAWLEANCP QSRRGAFRGF STFNYWGGRK AEFQDEDQKV WFERMRDKGW
     TVPEWPVEYG GAGLDKHRAG ILQQELRRIQ AQPPLQSLGI WMLGPALLHF GTPEQKAEHL
     PKIARGEIRW AQGYSEPGAG SDLASLSTKG ELKDGQWVIN GSKIWTTNGD KCDMIFALVR
     TEPDAPKHQG ISFILVDMDQ PGVTTKPITL INGDAPFVQT FFDNATAPEG NVVGPRGKGW
     DVTKYLLGHE REMIGSSMTN SVTETVSSVA KAKLGADGLK ADPSLRMAIA NHEIESWVLG
     IAVERLKDMG KAKQFSQFAP SVLKLMGTEL NYRRGELLMS ISGFDAVNDL FSEPVHSYLH
     APANCIAGGS NEVQLNILSK RALGLPEL
//
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