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Database: UniProt
Entry: A0A0T1W6V9_9MYCO
LinkDB: A0A0T1W6V9_9MYCO
Original site: A0A0T1W6V9_9MYCO 
ID   A0A0T1W6V9_9MYCO        Unreviewed;       390 AA.
AC   A0A0T1W6V9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQY04453.1};
GN   ORFNames=ASD37_21305 {ECO:0000313|EMBL:KQY04453.1};
OS   Mycobacterium sp. Root135.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1736457 {ECO:0000313|EMBL:KQY04453.1, ECO:0000313|Proteomes:UP000051127};
RN   [1] {ECO:0000313|EMBL:KQY04453.1, ECO:0000313|Proteomes:UP000051127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root135 {ECO:0000313|EMBL:KQY04453.1,
RC   ECO:0000313|Proteomes:UP000051127};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY04453.1, ECO:0000313|Proteomes:UP000051127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root135 {ECO:0000313|EMBL:KQY04453.1,
RC   ECO:0000313|Proteomes:UP000051127};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQY04453.1}.
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DR   EMBL; LMEZ01000007; KQY04453.1; -; Genomic_DNA.
DR   RefSeq; WP_056556339.1; NZ_LMEZ01000007.1.
DR   AlphaFoldDB; A0A0T1W6V9; -.
DR   STRING; 1736457.ASD37_21305; -.
DR   OrthoDB; 3404950at2; -.
DR   Proteomes; UP000051127; 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   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; IPR013107; Acyl-CoA_DH_C.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_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; PF08028; Acyl-CoA_dh_2; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051127}.
FT   DOMAIN          19..111
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          237..368
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   390 AA;  41364 MW;  0560FAAB492D8F41 CRC64;
     MLTRNAAPRV AAEPAGAPRD RAFDAALDVL RERRDEFNAQ HYVPADFVHL LKKAGMYRAA
     TPTEFGGEPM APSTFMKLVE RISAVDPATG WVSSFGSSLV YLAALPVESQ RDIYADGPDL
     AFSAGLFPLQ EAERVPGGYL CTGVWQFASG CRGADLIGIG LTGGPETGGK PLTALVSPSD
     LEIVENWDVA GMRATGSHAL RVENLFVPEE MTFIRGGAPT IDEPLTRYPS LAYAAQVLAV
     VTLGAARGAL DYCLEVGAAH TSITGGNAKG NRPAFKAGLG KAEAELRSAR AFFYESTDEV
     WAKAVDGTTI TAQDRALLRL GATHAAHVGR RVVLEAFDLA GTGAIYENHP LQRYLRDALV
     PAQHAMLQTN TYEGAGAVML GLDAGMPSFP
//
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