ID A0A124EQ19_9MYCO Unreviewed; 422 AA.
AC A0A124EQ19;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KUI18995.1};
GN ORFNames=AU193_07125 {ECO:0000313|EMBL:KUI18995.1};
OS Mycobacterium sp. GA-1285.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1772282 {ECO:0000313|EMBL:KUI18995.1, ECO:0000313|Proteomes:UP000053702};
RN [1] {ECO:0000313|EMBL:KUI18995.1, ECO:0000313|Proteomes:UP000053702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA-1285 {ECO:0000313|EMBL:KUI18995.1,
RC ECO:0000313|Proteomes:UP000053702};
RG TB Trials Study Group;
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E.L., Macaden R.,
RA Grewal H.M.S.;
RL Submitted (JAN-2016) 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:KUI18995.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LQIS01000017; KUI18995.1; -; Genomic_DNA.
DR RefSeq; WP_064422629.1; NZ_LQIS01000017.1.
DR AlphaFoldDB; A0A124EQ19; -.
DR STRING; 1772282.AU193_07125; -.
DR OrthoDB; 5167280at2; -.
DR Proteomes; UP000053702; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 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 19..135
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 142..232
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 245..400
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 46043 MW; 6753E5955BE37783 CRC64;
MTETTSTSAL AADTGPESVE EFAARAQTWL AENMPPIDPN NPPEHDRGEE EPWLRARELQ
KRLWEGGFAG ICFPKEYGGL GLPIAYQKAF DNVSRCYELP IILNTPTFTI CAATILDTGS
EEQKRKHISA ALRGEEVLVQ LLSEPSGGSD LAGVITRADR QGDKWVINGA KTWSTSAFAA
DYGLMLARTN WDVPKHEGLT MFLVPINSPG ITLRRIKQVN GSVEFCEEFF DNLELGDDAV
VGEVNAGWHV ASRQLYHERR AVGGGSEFAS GIGAEGKSDV PINYVELLEK LGQPDNERLR
EMAGRALVHR AVREQLIDHV YHGVLDGSLP PAAGSIIRIA HADVHHLEFD TVLAITGSAG
VVDVDGDLIR YGERYLSRQA AALGGGTTEI ARNIIGERVL GFPREPAADR GVPFKEVKRN
RG
//
