ID A0A0Q7Q762_9ACTN Unreviewed; 626 AA.
AC A0A0Q7Q762;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:KQY56048.1};
GN ORFNames=ASD11_16390 {ECO:0000313|EMBL:KQY56048.1};
OS Aeromicrobium sp. Root495.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736550 {ECO:0000313|EMBL:KQY56048.1, ECO:0000313|Proteomes:UP000051970};
RN [1] {ECO:0000313|EMBL:KQY56048.1, ECO:0000313|Proteomes:UP000051970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root495 {ECO:0000313|EMBL:KQY56048.1,
RC ECO:0000313|Proteomes:UP000051970};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY56048.1, ECO:0000313|Proteomes:UP000051970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root495 {ECO:0000313|EMBL:KQY56048.1,
RC ECO:0000313|Proteomes:UP000051970};
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 -!- 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:KQY56048.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMFJ01000002; KQY56048.1; -; Genomic_DNA.
DR RefSeq; WP_056290045.1; NZ_LMFJ01000002.1.
DR AlphaFoldDB; A0A0Q7Q762; -.
DR STRING; 1736550.ASD11_16390; -.
DR OrthoDB; 142556at2; -.
DR Proteomes; UP000051970; 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; 2.40.110.20; -; 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; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 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; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000051970}.
FT DOMAIN 3..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 163..278
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 297..464
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 484..622
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 626 AA; 68628 MW; 1912BAF1CB50743D CRC64;
MSHYKSNQRD IEFNLFELFD RGEVYGQGIF EDFDVDTAKS ILGEIERTAR EDLADSFEDS
DRNPPVYDPA THSVTMNKSF ADSYQKWMDA EWWRLQVPEA LGGQTAPNSL VWSSAEFVLG
ANPPIWMFAC GPAFARIVFE NGTQDRDVKI AQHMVDRRWG ATMVLTEPDA GSDVGAGRTK
AFPNEDGTWN IEGVKRFITS GEHDMAENIM HLVLARPQGV EGHGGPGTKG LSLFLVPKYH
FDVETGELTG ERNGAYVTNV EKKMGIKVST TCEVTFGDSS TGEGQAARGW LLGEVHDGIN
QMFRVIENAR MMVGAKAIAT LSTGYLNALE YAKERVQGAD LTQAADKTAP RVTITHHPDV
RRSLLTQKAF AEGLRSLAIY TSTWQDAITL KAKSGEDASL EEAVNDLLLP IVKGYGSERS
WVVLGTESLQ TFGGSGFLQD YPIEQYVRDA KIDTLYEGTT AIQGQDLFFR KIVKDKGRAI
GHLANEIQEF AQGDAGNGRL KVERELLAKG LEDTQAILGA VFNDLMASNP ADEKGDLKNI
YKVGLNTTRL VYVLGDLTVA WLLLRGAAVA QTALDAGATG TEQSFYEGKV AAASFFARNI
LPKLASERAL AENIDDSIME LDEAAF
//
