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Database: UniProt
Entry: A0A0M2K4P2_9MYCO
LinkDB: A0A0M2K4P2_9MYCO
Original site: A0A0M2K4P2_9MYCO 
ID   A0A0M2K4P2_9MYCO        Unreviewed;       703 AA.
AC   A0A0M2K4P2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KKF02147.2};
GN   ORFNames=WN67_10060 {ECO:0000313|EMBL:KKF02147.2};
OS   Mycolicibacterium obuense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1807 {ECO:0000313|EMBL:KKF02147.2, ECO:0000313|Proteomes:UP000034150};
RN   [1] {ECO:0000313|EMBL:KKF02147.2, ECO:0000313|Proteomes:UP000034150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UC1 {ECO:0000313|EMBL:KKF02147.2,
RC   ECO:0000313|Proteomes:UP000034150};
RA   Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT   "Genome sequence of Mycobacterium obuense UC1.";
RL   Submitted (APR-2015) 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:KKF02147.2}.
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DR   EMBL; LAUZ02000021; KKF02147.2; -; Genomic_DNA.
DR   RefSeq; WP_046676554.1; NZ_LAUZ02000021.1.
DR   AlphaFoldDB; A0A0M2K4P2; -.
DR   STRING; 1807.MOBUDSM44075_00320; -.
DR   PATRIC; fig|1807.13.peg.2272; -.
DR   OrthoDB; 3964153at2; -.
DR   Proteomes; UP000034150; 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; 2.
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; 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          6..89
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          202..334
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          377..450
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          454..548
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          560..699
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   703 AA;  74019 MW;  896EF85BDC95360F CRC64;
     MPATISDEQS AARELVRDWA AGSTSLEAVR DVEQGAPDAW RAPFDALAAL GIFGVALPEE
     LGGADGTVAD LCAMLEEAAA GLIPGPVATT ALATLVLDGA QGDLVEALAS GQRTAGVALR
     AELTLTGERV SGTAATVLGA TADGVLLLPA GDTWVLLDAT ADGVVVERRK ATDFSRPLAR
     VTVDGAPATT LDVPAQRVVD LAATVAAAEA AGVARWLLTT ATEYAKVREQ FGKPIGSFQA
     IKHMCAEMLL RSEQASVAAA DAARAAGESD DQQLSIAAAL AASVGIEAAT ANAKDCIQVL
     GGIGITWEHD AHLYLRRAYG IGQFLGGRSH WLRRVAALTQ QGVRRDLHID LASVADLRPE
     IASAVADVAA APQDRRQVVM AETGLLAPHW PRPHGRDAGP AEQLLIDQEL AAAGVTRPDL
     VIGWWAVPTI LEHGSAAQVE QFVPPTLRGE LQWCQLFSEP GAGSDLAALR TKAVRAEGGW
     KLTGQKVWTS AAQKAHWGVA LARTDPDAPK HKGITYFLID MTSPGIVIRP LREITGDELF
     NEVFFDDVFV PDEMVVGAVD DGWKLARTTL ANERVAMAQG TALGNPMEEL LRALSEADVD
     DAQQDRLGAL ICTAQVGSLL DQRIAQLAVG GRDPGPQASA RKLIGVRYRQ ALAEFRMELS
     DGAGAVENQQ VHDFLNTRCL TIAGGTEQIL LTMAGERLLG LPR
//
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