ID A0A024K586_9MYCO Unreviewed; 651 AA.
AC A0A024K586;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:CDO90727.1};
GN ORFNames=BN973_05126 {ECO:0000313|EMBL:CDO90727.1};
OS Mycobacterium triplex.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO90727.1};
RN [1] {ECO:0000313|EMBL:CDO90727.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO90727.1};
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:CDO90727.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO90727.1};
RA Xu Y.W., Yang Q.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + a 2,3-saturated acyl-CoA = a 2,3-dehydroacyl-CoA + AH2;
CC Xref=Rhea:RHEA:48608, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:60015, ChEBI:CHEBI:65111;
CC Evidence={ECO:0000256|ARBA:ARBA00043783};
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; CDO90727.1; -; Genomic_DNA.
DR RefSeq; WP_036471431.1; NZ_LQPY01000007.1.
DR AlphaFoldDB; A0A024K586; -.
DR STRING; 47839.BN973_05126; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_11_1_11; -.
DR OrthoDB; 8876745at2; -.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, 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 58..163
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 167..263
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 277..435
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 651 AA; 70836 MW; C1E882AF6EE0A281 CRC64;
MAQQAQVTEE QARALAEESR ESGWDKPSFA KELFLGHFPL ELIHPFPKPS DADEARTREF
LARVREFLNT VDGGLIERDA QIPDEYVKGL AELGCFGMKI PSEYGGLNMS QVAYNRALMM
ISSVHPSLGA LLSAHQSIGV PEPLKLAGTD EQKRKFLPRC AAGAISAFLL TEPDVGSDPA
RLACTATPVD GGRAYELEGV KLWTTNGVVA ELLVVMARVP KSDGHRGGIS AFVVEADSPG
ITVERRNKFM GLRGIENGVT RLHAVRVPSE NLIGREGDGL KIALTTLNAG RLSIPANATG
SSKWALKIAR EWSGERVQWG KPLAKHEAVA RKISFIAATN YALDAVLELS GQMADEGRND
IRIEAALAKL WSSEMACLIA DELVQIRGGR GYETSESLAA RGERAVPAEQ AVRDLRINRI
FEGSSEIMRL LIAREAVDAH LSAAGDLAKP DTGLREKAAA AVGASGFYAK WLPQLVFGEG
QRPRAYSEFG PLAAHLRFVE RSTRKLARNT FYGMARWQAK LEQKQGFLGR IVDIGAELFA
MSAACVRAEG QRVADPELGQ QAYELAEAFC QQATLRVDAL FDGLWTNTDT SDVQLTHEVL
EGRYRWLEDG IVDQSEGTGP WIAHWEAGES TEANLARRFL TASASTGSIA K
//
