ID M3VJ44_9ACTN Unreviewed; 400 AA.
AC M3VJ44;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:GAC84829.1};
GN ORFNames=GP2_026_00660 {ECO:0000313|EMBL:GAC84829.1};
OS Gordonia paraffinivorans NBRC 108238.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223543 {ECO:0000313|EMBL:GAC84829.1, ECO:0000313|Proteomes:UP000035021};
RN [1] {ECO:0000313|EMBL:GAC84829.1, ECO:0000313|Proteomes:UP000035021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108238 {ECO:0000313|EMBL:GAC84829.1,
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:GAC84829.1}.
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DR EMBL; BAOQ01000026; GAC84829.1; -; Genomic_DNA.
DR RefSeq; WP_006901055.1; NZ_BAOQ01000026.1.
DR AlphaFoldDB; M3VJ44; -.
DR STRING; 1223543.GP2_026_00660; -.
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 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:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 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 8..127
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 133..233
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 245..393
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 400 AA; 44252 MW; 3F2D61A165C16AE5 CRC64;
MDFAYSDRTR ELAAKLEAFM ADHVLPAEKI YDEQIAANEN PHEQPQIMRD LQKKARELGL
WNLFMTHGDL GAGLTNLEYA PLAEIVGRSI IGNEAINCSA PDTGNMEILA LYGTEKQKEQ
WLKPLLDCSI RSAFAMTEPA VASSDATNIT STIRRDGDHY VLNGRKWYTS GILDPDCKLI
IFMGKSDPDG PTYRQQSMIL VPRDTPGIEV IRDLPMFGFT DRLGHGEVQF TDVRVPVENM
LGEEGDGFAI AQGRLGPGRM HYAMRAVGMA ERALDLMCRR AQERVAFGGP LASRGVVREW
IARSRIEIDQ IRLLVLYASW LMDTQGNAAA RSEVAAIKVS AMEVAHKVVD RAVQTFGAAG
VSNDTVLARL HALTRALQIA DGPNEVHLRT IARLEVKKHA
//
