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Database: UniProt
Entry: A0A257G9V3_9SPHN
LinkDB: A0A257G9V3_9SPHN
Original site: A0A257G9V3_9SPHN 
ID   A0A257G9V3_9SPHN        Unreviewed;       384 AA.
AC   A0A257G9V3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OYU34801.1};
GN   ORFNames=CFE35_12990 {ECO:0000313|EMBL:OYU34801.1};
OS   Novosphingobium sp. PASSN1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=2015561 {ECO:0000313|EMBL:OYU34801.1, ECO:0000313|Proteomes:UP000215690};
RN   [1] {ECO:0000313|EMBL:OYU34801.1, ECO:0000313|Proteomes:UP000215690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PASSN1 {ECO:0000313|EMBL:OYU34801.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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:OYU34801.1}.
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DR   EMBL; NKIS01000007; OYU34801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257G9V3; -.
DR   Proteomes; UP000215690; 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:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 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.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 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          8..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          124..218
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          230..378
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   384 AA;  42371 MW;  A7DB52A900574460 CRC64;
     MLERKLFSPE HDMFRDSVRR FIADEIKPHH EDWQKAGITP RSLWEKAGEA GLLCTTVPEA
     FGGYGADFLY SAIVIEELAR ANTPDIAFYT HSDIATPYLI DFGTEEQKRT LLPDMVAGRK
     ICSLGMSEPD AGSDVASIKT SAVRDGDEYV INGGKVFITN GHNADMFIVA CKTDPAARAK
     GISMILVEAD RAGFRRGRLL EKIGLKAQDT AEIFFDDVRV PVSNLVGVEN QGFFHMMKSL
     PQERLVQAIR AVTASEAALD MTIDYTVQRK AFGKSVSEFQ AIQFRFATLY SEIAGQRALV
     DRCLEAHLAG ELDDFDAAVV KLSSTEVQAK VVDECVTCFG GWGYMWEYPI ARAYADARAA
     RLAGGTTDIM KLIIGRRLVA SRSQ
//
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