ID L7LE77_9ACTN Unreviewed; 614 AA.
AC L7LE77;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=GOHSU_72_00020 {ECO:0000313|EMBL:GAC59031.1};
OS Gordonia hirsuta DSM 44140 = NBRC 16056.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1121927 {ECO:0000313|EMBL:GAC59031.1, ECO:0000313|Proteomes:UP000053405};
RN [1] {ECO:0000313|EMBL:GAC59031.1, ECO:0000313|Proteomes:UP000053405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16056 {ECO:0000313|EMBL:GAC59031.1,
RC ECO:0000313|Proteomes:UP000053405};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia hirsuta NBRC 16056.";
RL Submitted (DEC-2012) 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:GAC59031.1}.
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DR EMBL; BANT01000072; GAC59031.1; -; Genomic_DNA.
DR RefSeq; WP_005944442.1; NZ_BANT01000072.1.
DR AlphaFoldDB; L7LE77; -.
DR STRING; 1121927.GOHSU_72_00020; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 2431337at2; -.
DR Proteomes; UP000053405; 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; 2.
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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053405}.
FT DOMAIN 115..232
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 281..359
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 363..447
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 470..609
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:GAC59031.1"
SQ SEQUENCE 614 AA; 63933 MW; 24B0D9FB22CFD588 CRC64;
GGAAAVVPAA AVAAGTPAVV HDGVVDLGPV PGFIDGALIV APLAVDGLTG WFVIPSPRVR
RAAHGQTPGP DAQGQTAAVD GTAAAVEVVL EGVDAAGLIR IDDGAALHAM LVAGLTAYQA
GVARAVLDMA VDYAKVRTQF GVPIGSFQAI KHLCADMLCR AEQLSAAAWD LAAAIDAGDP
AQRELSMLAA AVLTAELPLA NTKDAIQVLG GIGFTFEHEA HLYLRSALSA RIQLAGGAPA
REALAALGRG GARREFAVDL AAVEHRRTEI AALVAGIAAA PEDRRRAELA AAGLLMPHWP
EPYGIEADPA LQLLIDAELG RAGVRRPDLV IAGWALPTIL EHGTAAQRER FLRPTLAGDI
VWCQLFSEPE AGSDLASLRT RAERVDGGWK LTGQKIWTSA AAQARWGVAL ARTDPQAPKH
RGITYFLIDM TSPGIDVRPL REMTGRALFN EVFLDGVVVP DDCVVGEIDG GWRLARTTLA
NERVAMGGAG LGKEMDALLR QLESTGAELD TPAQQRLGAL IADAHIGRVL DARTVAQRLS
GTDPGVTSSV RKLIGVVHRQ SVPEFALDLL GPAGLKPSVA GEQFLLNRCL SIAGGTTQVL
KNAAAERILG LPRG
//
