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Database: UniProt
Entry: A0A1E3TGU7_MYCSH
LinkDB: A0A1E3TGU7_MYCSH
Original site: A0A1E3TGU7_MYCSH 
ID   A0A1E3TGU7_MYCSH        Unreviewed;       388 AA.
AC   A0A1E3TGU7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Butyryl-CoA dehydrogenase [Frankia symbiont of Datisca glomerata] {ECO:0000313|EMBL:SRX93685.1};
GN   ORFNames=MSP7336_01928 {ECO:0000313|EMBL:SRX93685.1};
OS   Mycobacterium shimoidei.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=29313 {ECO:0000313|EMBL:SRX93685.1, ECO:0000313|Proteomes:UP000252015};
RN   [1] {ECO:0000313|EMBL:SRX93685.1, ECO:0000313|Proteomes:UP000252015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P7336 {ECO:0000313|EMBL:SRX93685.1,
RC   ECO:0000313|Proteomes:UP000252015};
RG   IHU Genomes;
RL   Submitted (MAY-2018) 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; UEGW01000001; SRX93685.1; -; Genomic_DNA.
DR   RefSeq; WP_069395899.1; NZ_UEGW01000001.1.
DR   AlphaFoldDB; A0A1E3TGU7; -.
DR   STRING; 29313.BHQ16_10055; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000252015; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR006089; Acyl-CoA_DH_CS.
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   PIRSF; PIRSF016578; HsaA; 3.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN          6..119
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          123..220
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          233..367
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   388 AA;  43217 MW;  CE46D7D686426C86 CRC64;
     MNFELTEDQE LIRRSVAELA QKFDDHYWME RDQAHEFPSE FYRAIADGGW LGMTIPVEYG
     GHGLGITEAT LLAEEVAKSG GGMNAASSIH LSIFGMQPVV KYGSAELKAR TLPRVATGDL
     HVCFGVTEPG AGLDTSRIST FAKRQGDRYV VNGRKVWISK AQESEKILLL TRTQHYDEVT
     KKTDGMTLFL TDLDRDHVDI RPIRKMGRNA VSSNEVFIDN LEVPVEDRVG EEGKGFHYIL
     DGLNPERMLI AAEALGIGRV ALDKAVKYAT DREVFGRPIG MNQGIQFPLA DSLTRLDAAE
     LMLRKATWLY DNGKPCGREA NTAKYLCADA GFTAADRALQ THGGMGYAEE YNVARYFREA
     RLMKIAPISQ EMILNFLGSH TLKLPRSY
//
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