ID A0A0Q6FRT0_9ACTN Unreviewed; 600 AA.
AC A0A0Q6FRT0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQT93831.1};
GN ORFNames=ASG49_02360 {ECO:0000313|EMBL:KQT93831.1};
OS Marmoricola sp. Leaf446.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Marmoricola.
OX NCBI_TaxID=1736379 {ECO:0000313|EMBL:KQT93831.1, ECO:0000313|Proteomes:UP000051542};
RN [1] {ECO:0000313|EMBL:KQT93831.1, ECO:0000313|Proteomes:UP000051542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT93831.1,
RC ECO:0000313|Proteomes:UP000051542};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT93831.1, ECO:0000313|Proteomes:UP000051542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT93831.1,
RC ECO:0000313|Proteomes:UP000051542};
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|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:KQT93831.1}.
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DR EMBL; LMRF01000001; KQT93831.1; -; Genomic_DNA.
DR RefSeq; WP_056536597.1; NZ_LMRF01000001.1.
DR AlphaFoldDB; A0A0Q6FRT0; -.
DR STRING; 1736379.ASG49_02360; -.
DR OrthoDB; 142556at2; -.
DR Proteomes; UP000051542; 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; 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; 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:UP000051542}.
FT DOMAIN 6..35
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 164..263
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 293..460
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 479..596
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 600 AA; 65125 MW; 9F6F029CA9B5EDD7 CRC64;
MASSLIMSRR DLDFLLHDWL RVERLVERER YAEHDRETFD AVLDLAEQLA TEHFAPLNRE
ADTHEPYVGE DGRVVQPESV KAALAAYTAS GLPTSVFDHE LGGMQLPFVV HQAASSWFQA
ASIGAFAYPF LAEGNANLLA TYGTPEQVAT YAVPVVEGRW YGTMALSEPQ AGSSLGDITT
RAVRQDDGSY RLTGTKMWIS GGDHELAENI VHLVLARTPD ASPGTKGISL FIVPKHLPAE
DGSVGERNDV ALVGLNHKMG YRATTNTLLN FGEGLATPGG RAGAVGHLVG EEGRGLTYMF
HMMNEARVSV GAGAMALGYT GYLHSLEYAR VRTQGRPLDR KDPTTPPVPL VEHADVRRML
LAQKSYAEGA LALVLFCAHL VDESRTHPDA ETAHEAEQLL SLLTPVAKSW PSQWCLAAND
LAIQVHGGYG YTRDYVVEQL YRDNRLNPIH EGTHGIQAQD LLGRKVVEGG GRSLGVLGAR
VTATVAAARA AGGEPAAYAD RLDRTWTELL RVTGVLWEKG DPALALANAT PYLEAFGHVV
VAWLWLEQLV AVGDGDEPFH HGKRAAARYF YAFELPTTGP RLDLLASLDT TTLDLDPTVL
//
