ID A0A024K1K7_9MYCO Unreviewed; 386 AA.
AC A0A024K1K7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:CDO89679.1};
GN ORFNames=BN973_04059 {ECO:0000313|EMBL:CDO89679.1};
OS Mycobacterium triplex.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO89679.1};
RN [1] {ECO:0000313|EMBL:CDO89679.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO89679.1};
RX PubMed=24874681; DOI=10.1128/genomeA.00499-14;
RA Sassi M., Croce O., Robert C., Raoult D., Drancourt M.;
RT "Draft Genome Sequence of Mycobacterium triplex DSM 44626.";
RL Genome Announc. Announc.2:e00499-e00414(2014).
RN [2] {ECO:0000313|EMBL:CDO89679.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO89679.1};
RA Xu Y.W., Yang Q.;
RL Submitted (APR-2014) 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}.
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DR EMBL; HG964446; CDO89679.1; -; Genomic_DNA.
DR RefSeq; WP_036470353.1; NZ_LQPY01000030.1.
DR AlphaFoldDB; A0A024K1K7; -.
DR STRING; 47839.BN973_04059; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_9_0_11; -.
DR OrthoDB; 3964153at2; -.
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:SF3; ACYL-COA DEHYDROGENASE FADE29; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125}.
FT DOMAIN 6..120
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 126..221
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 233..383
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 386 AA; 42416 MW; 4DE0EF76254E8505 CRC64;
MQLALTPEEA AFRDELRNIF TTKIPQDARD RVRQGSAEVV HDDVVTSHKI LHEHGLAVPS
WPVEWGGKDW TPTQHQIWAD EMQLACVPEP LNFNTKMVGP VIAEFGSQEI KERFLPPTAS
LDIWWCQGFS EPEAGSDLAS LRTTAVRDGD SYVVNGQKTW TTLGQYADWI FCLVRTDPQA
PKRQAGISFL LFDMKTPGIT VRPIKTIDGG HEVNELFFED VRVPANQLVG EENKGWTYAK
FLLGNERTGI AGVGRTKVRL AEVKKFAAQA GVLDDPLFAA RLAEAENELL ALELTQSRVV
TDSADGQPNP ASSVLKLRGS QLQQIATELL VEVAGADALA ADGDGVASPD WARHSAPRYL
NYRKTSIYGG SSEVQRNIIA STILGL
//
