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Database: UniProt
Entry: A0A3S4SCG2_MYCCI
LinkDB: A0A3S4SCG2_MYCCI
Original site: A0A3S4SCG2_MYCCI 
ID   A0A3S4SCG2_MYCCI        Unreviewed;       736 AA.
AC   A0A3S4SCG2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Acyl-CoA dehydrogenase FadE6 {ECO:0000313|EMBL:VEG50027.1};
DE            EC=1.3.8.1 {ECO:0000313|EMBL:VEG50027.1};
GN   Name=fadE6 {ECO:0000313|EMBL:VEG50027.1};
GN   ORFNames=NCTC10485_04343 {ECO:0000313|EMBL:VEG50027.1};
OS   Mycolicibacterium chitae (Mycobacterium chitae).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1792 {ECO:0000313|EMBL:VEG50027.1, ECO:0000313|Proteomes:UP000282551};
RN   [1] {ECO:0000313|EMBL:VEG50027.1, ECO:0000313|Proteomes:UP000282551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10485 {ECO:0000313|EMBL:VEG50027.1,
RC   ECO:0000313|Proteomes:UP000282551};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) 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}.
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DR   EMBL; LR134355; VEG50027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S4SCG2; -.
DR   OrthoDB; 3964153at2; -.
DR   Proteomes; UP000282551; Chromosome 1.
DR   GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; 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};
KW   Oxidoreductase {ECO:0000313|EMBL:VEG50027.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282551}.
FT   DOMAIN          6..99
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          221..345
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          383..474
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          478..568
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          584..730
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   736 AA;  78136 MW;  B84AAB14C1D94C17 CRC64;
     MPIAISPEHV DLADSVRALV ARVAPAEVLH EALETPIPNP PPYWKAAAEQ GLQGLHLAES
     VGGQGFGILE LSVVLAEFGY GAVPGPFVPS AIASALIAAH DPNAQVLSGL AAGETIAAYA
     IDSGLTATRQ GDALVIRGEV RAVPAAAQAS VLVLPVAGLD SATSGAEWVV LDADTLEIEP
     VQSVDPLRPV AHVRANAVEV GDDRVLSNLS RSAAHALMST LLSAEAVGVA RWATDTASAY
     AKIREQFGRP IGQFQAVKHK CANMIAVTER ATAAAWDAAR AIDEVARGDS DLEGAHIDFA
     AAVAATLAPA AAQRCAEDCI QVHGGIGFTW EHDTNVYYRR ALVIAASFGR AADYPQRVVD
     AATATGMRGI DIDLDPDTEK LREEIRAEVA ALKAIAREER NTAIAEAGWV QPHLPKPWGR
     AATPIEQIII AQEFATGRVK RPQMGIAAWI IPSIVAFGTD EQKQRFLPPT FRGEMIWCQL
     FSEPGAGSDL ASLSTKATKV DGGWRITGQK IWTTGAQFSQ WGALLARTNP SAPKHNGITY
     FLLDMASEGV EVKPLRELTG NAMFNTVFID DVFVPDDMVL GEVDRGWEVS RNTLTAERVS
     IGSSEPPFLP SLDKFVEFVG EGHFDQIEQN RAGQLIAEGH AAKLLNMRST LLTLAGGDAM
     PSAAISKLLS MKTGQGYAEF AVSSFGTDGV LGDEQTPQGI WAQFLLASRA TTIYGGTSEV
     QLNIIAERLL GLPRDP
//
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