ID A0A0B8ZZV5_9SPHN Unreviewed; 389 AA.
AC A0A0B8ZZV5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KHS42624.1};
GN ORFNames=NJ75_04061 {ECO:0000313|EMBL:KHS42624.1};
OS Novosphingobium subterraneum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=48936 {ECO:0000313|EMBL:KHS42624.1, ECO:0000313|Proteomes:UP000031338};
RN [1] {ECO:0000313|EMBL:KHS42624.1, ECO:0000313|Proteomes:UP000031338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12447 {ECO:0000313|EMBL:KHS42624.1,
RC ECO:0000313|Proteomes:UP000031338};
RA Gan H.M., Gan H.Y., Savka M.A.;
RT "Draft genome sequence of Novosphingobium subterraneum DSM 12447.";
RL Submitted (OCT-2014) 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:KHS42624.1}.
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DR EMBL; JRVC01000027; KHS42624.1; -; Genomic_DNA.
DR RefSeq; WP_039337691.1; NZ_JRVC01000027.1.
DR AlphaFoldDB; A0A0B8ZZV5; -.
DR STRING; 48936.NJ75_04061; -.
DR PATRIC; fig|48936.3.peg.4092; -.
DR Proteomes; UP000031338; 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 PIRSF; PIRSF016578; HsaA; 2.
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|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 123..222
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 234..367
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 389 AA; 43024 MW; DF6EBA30A51FD35B CRC64;
MILSPYDSED HGEIREGVRK LCAQFPGEYW RKLDEKRQYP TEFVNALTQA GWLSVLIPEE
YGGSGLGLGA AAAILETIQA EGGNGGACHA QMYIMGTILR HGSEEQKCQY LPKIASGELR
LQAFGVTEPT SGTDTTSLRT FARREGDEYV VNGQKIWTSR AEHSDLMLLL ARTTPREELA
KKTDGLSVFI VDMREVVGRS LTIRPIRTMM NHATTEVFFD NMRIPAANLL GEEGKGFRYI
LSGMNAERVL IAAECVGDAK WFTQRSVEYA KERQVFGRAI GANQGVAFPI AKAYAQMRAA
ELMVREAARM YEAGLPMGAE ANMAKMLAAD ASWEAGNACV QTHGGFGFAE EYDVERKLRE
TRLYQVAPIS TNLILSFLAE HVLGLPRSY
//
