ID A0A0F3KGL6_9GAMM Unreviewed; 386 AA.
AC A0A0F3KGL6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KJV30296.1};
GN ORFNames=VI08_15130 {ECO:0000313|EMBL:KJV30296.1};
OS Luteibacter yeojuensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Luteibacter.
OX NCBI_TaxID=345309 {ECO:0000313|EMBL:KJV30296.1, ECO:0000313|Proteomes:UP000033651};
RN [1] {ECO:0000313|EMBL:KJV30296.1, ECO:0000313|Proteomes:UP000033651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SU11 {ECO:0000313|EMBL:KJV30296.1,
RC ECO:0000313|Proteomes:UP000033651};
RA Sulaiman J., Priya K., Chan K.-G.;
RT "Draft genome sequence of Luteibacter yeojuensis strain SU11.";
RL Submitted (MAR-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:KJV30296.1}.
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DR EMBL; JZRB01000033; KJV30296.1; -; Genomic_DNA.
DR RefSeq; WP_045830452.1; NZ_JZRB01000033.1.
DR AlphaFoldDB; A0A0F3KGL6; -.
DR PATRIC; fig|345309.4.peg.2631; -.
DR OrthoDB; 9769473at2; -.
DR Proteomes; UP000033651; 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; 3.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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 6..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..217
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 230..381
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 386 AA; 41525 MW; 0941742447AA9C77 CRC64;
MDFRFTDDQL SIQSIARDFA QKRIAPVAAE LDARGEFPLE NIQEMGQLGL MGIEVPEEYG
GAGMDPVAYV LAMVEIAAAD AATSTIMSVN NSLFCNGILK NGTEEQKQKY VRAIASGEAI
GAYALTEPQS GSDASNMHTR AVKNADGDWV INGKKSWITS GPVARYIVLF AVTTPGIGAK
GVSAFIIDTK RPGFMAGKTE PKLGIRASAT CEIEFHDYIC PKEDLLGAEG KGFGIAMGVL
DAGRIGIASQ AVGIARAAYE ATLQWSRDRK AFGTPIGTFQ MTQAKIADMK CKLDSALLLT
LRAAWTKGQV EKTGGRFGTE ASMAKLVASE AAMWITHQAV QIHGGMGYSK EMPLERYFRD
AKITEIYEGT SEIQRLVIAR AETGLR
//
