ID A0A3D9SN49_9ACTN Unreviewed; 596 AA.
AC A0A3D9SN49;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:REE95850.1};
GN ORFNames=DFJ69_1264 {ECO:0000313|EMBL:REE95850.1};
OS Thermomonospora umbrina.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=111806 {ECO:0000313|EMBL:REE95850.1, ECO:0000313|Proteomes:UP000256661};
RN [1] {ECO:0000313|EMBL:REE95850.1, ECO:0000313|Proteomes:UP000256661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43927 {ECO:0000313|EMBL:REE95850.1,
RC ECO:0000313|Proteomes:UP000256661};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:REE95850.1}.
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DR EMBL; QTTT01000001; REE95850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9SN49; -.
DR OrthoDB; 2769798at2; -.
DR Proteomes; UP000256661; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF3; ACYL-COA DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12418; AcylCoA_DH_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000256661}.
FT DOMAIN 6..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 82..157
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 163..263
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 293..458
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 478..592
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 596 AA; 65012 MW; C7067DC9781D9F07 CRC64;
MSSLLLSRRD LEFLLYEWLD VTALTRRERY AEHSRETFDA VLELGERIAD EHFAGHNKLA
DVNEPTMDGD GRVVLIPEVK AALDVFARAG LLAAEFDEAL GGMQLPNVVS KAVLSWFQAA
NVGTSAYPFL TIANANLLVA HGSPEQVERW VRPMAEGRFF GTMCLSEPQA GSSLADITTR
AEPQEDGTHR LTGTKMWISA GDHELSENIV HLVLAKIPGG PPGVKGISLF IVPKVLLDED
GGLGERNDVA LVGLNHKMGY RGTVNTVLNF GEGVHTPGGS PGAVGYLVGE PHKGLIYMFH
MMNEARIGVG LDASALGYTG YLHALDYAKV RLQGRPLAGK DPSAPPVPLI EHVDVRRMLL
AQKSYVEGGL ALGLYCSRLV DEERTAENEA DRRRASLLLD VLTPIAKSWP SQWCLAANDL
AIQVHGGYGY TREYNVEQFY RDNRLNPIHE GTHGVQGLDL LGRKVVAQGG EGLRVLGEAI
AATVSRAPAT AQAEAERLTA AFDRLAAVTA RLWSTGDAEV ALANASVYLE AAGHIVVAWI
WLEQLVAAAD REGDFYTGKR RAARYFFRYE LPRTGPQLDL LDSLDRTTLD MDPAWF
//
