ID M3V523_9ACTN Unreviewed; 393 AA.
AC M3V523;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:GAC84717.1};
GN Name=fadE {ECO:0000313|EMBL:GAC84717.1};
GN ORFNames=GP2_025_00360 {ECO:0000313|EMBL:GAC84717.1};
OS Gordonia paraffinivorans NBRC 108238.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223543 {ECO:0000313|EMBL:GAC84717.1, ECO:0000313|Proteomes:UP000035021};
RN [1] {ECO:0000313|EMBL:GAC84717.1, ECO:0000313|Proteomes:UP000035021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108238 {ECO:0000313|EMBL:GAC84717.1,
RC ECO:0000313|Proteomes:UP000035021};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia paraffinivorans NBRC 108238.";
RL Submitted (FEB-2013) 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:GAC84717.1}.
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DR EMBL; BAOQ01000025; GAC84717.1; -; Genomic_DNA.
DR RefSeq; WP_006900945.1; NZ_BAOQ01000025.1.
DR AlphaFoldDB; M3V523; -.
DR STRING; 1223543.GP2_025_00360; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000035021; 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; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR48083:SF1; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G06510)-RELATED; 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 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|RuleBase:RU362125}.
FT DOMAIN 40..116
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 128..227
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 241..388
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 393 AA; 42068 MW; AC270E3C34E315B4 CRC64;
MTVAPVPNLN PDSRELVASI FEAVEGISAA FPRSLFLQRA RDGGHARELW DALVAADLLA
IGVPESLGGA GGGLTGTTAV MEALARKGIP PLQYSLTTFC REAILRHGSE QQIKDHVVTS
VTGRRKICLG VTEPEAGTNS FAARTYARKT ADGSYRITGQ KVFISGADES DHILLLARTA
PPGEPLSRRS GFGLFIVDLS LPGIELRQLD IEWYAPENQF EVFFDDVEVP QDALIGTEGL
GFDHILSCLN QERVTVAAWA LGLGEYALQK AVEYAKVRAP FGTPIGTHQA VAHPLALARA
EMEAARQVMY SAAASYDSGV DAGDQANMAK LLGSRAALAA VDSAIQTHGG SAFVYESDVV
TIWPMVRILQ IAPLNNESIL NYISERVLGL PRS
//
