ID X8CTF0_MYCIT Unreviewed; 772 AA.
AC X8CTF0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Acyl-CoA dehydrogenase, N-terminal domain protein {ECO:0000313|EMBL:EUA58535.1};
GN ORFNames=I550_1678 {ECO:0000313|EMBL:EUA58535.1};
OS Mycobacterium intracellulare 1956.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1299331 {ECO:0000313|EMBL:EUA58535.1, ECO:0000313|Proteomes:UP000020825};
RN [1] {ECO:0000313|EMBL:EUA58535.1, ECO:0000313|Proteomes:UP000020825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1956 {ECO:0000313|EMBL:EUA58535.1,
RC ECO:0000313|Proteomes:UP000020825};
RA Zelazny A., Olivier K., Holland S., Lenaerts A., Ordway D., DeGroote M.A.,
RA Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:EUA58535.1}.
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; JAOG01000001; EUA58535.1; -; Genomic_DNA.
DR AlphaFoldDB; X8CTF0; -.
DR PATRIC; fig|1299331.3.peg.1625; -.
DR Proteomes; UP000020825; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd00567; ACAD; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 2.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 2.
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; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 10..102
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 247..372
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 403..512
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 520..610
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 624..765
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 772 AA; 83399 MW; 58793DCCA3CB36B1 CRC64;
MTALSADERQ ELAQSVRSAC ERLASEDRVR AVAYAEGNRG GGDGHSGFDT VLWDVLCNQV
GVAGIALPEH LGGAGYGVSA LGVVAHELGR ALAPVPFVSS TVLATGLLLD LTERDPDADK
RLTGLIEGRR TAAAALTGDG GLWRRSAVTL RAARAGDDWN IDGTVRHVLG GSVADDLVVV
AIDEDGEPAV FLLDPTIDSV VAKAERVLDR TRPMATITLS SAPALRLSGD APLGDVVDRN
VDIALAVLSA EQVGACERVL EIATDYARTR EQFGRQIGSF QAIKHKCADM LVDLEWARSA
SQAALEALDD PDSAAVGEAG WRASMAKAVC SEALRNATKA NVQIHGGIGF TWEDSAHLYF
RRARTDEVLL GAPGQHWDRL STLDPSTQPP ASPEVTKELN DVDALRAEIR SFLDNAPRPA
GLRNYGPTPT ADDVEAGRVW HRYLADHGYA CLHWPREFGG AAATVTYQAV FAEECARAEV
PRQLNITGAD LVGPVLIKFG SQEQKDRYLE PIRLGDDVWC QLFSEPGAGS DLAGVRTRAE
RTTTGWRIDG QKVWSSAAAS ARFGLLLART GPDKHRDLSM FVVPMDIPGV TVRPLTQMDG
ESKFNEVFFD GAELDEDALI GEVGQGWTVA MVTLGRERLT LGSQAVSMFR LHERMVDAAR
DHDLLDPVLS RSMTRLWARM WLLRFTWQRA IDSGDLTSPA FSVLKLMTSE TDQDLGDMAT
EVLGTDACTD PEEDGLVHHM LIGRAQTILG GTSEIQRNIL GERVLGLPKE PR
//
