ID A0A0Q5K955_9MICO Unreviewed; 392 AA.
AC A0A0Q5K955;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQR25897.1};
GN ORFNames=ASF76_01005 {ECO:0000313|EMBL:KQR25897.1};
OS Microbacterium sp. Leaf151.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736276 {ECO:0000313|EMBL:KQR25897.1, ECO:0000313|Proteomes:UP000051582};
RN [1] {ECO:0000313|EMBL:KQR25897.1, ECO:0000313|Proteomes:UP000051582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf151 {ECO:0000313|EMBL:KQR25897.1,
RC ECO:0000313|Proteomes:UP000051582};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR25897.1, ECO:0000313|Proteomes:UP000051582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf151 {ECO:0000313|EMBL:KQR25897.1,
RC ECO:0000313|Proteomes:UP000051582};
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:KQR25897.1}.
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DR EMBL; LMOR01000001; KQR25897.1; -; Genomic_DNA.
DR RefSeq; WP_055951646.1; NZ_LMOR01000001.1.
DR AlphaFoldDB; A0A0Q5K955; -.
DR STRING; 1736276.ASF76_01005; -.
DR OrthoDB; 2769798at2; -.
DR Proteomes; UP000051582; 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; PTHR43831; ISOBUTYRYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43831:SF1; ISOBUTYRYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 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|RuleBase:RU362125}.
FT DOMAIN 20..130
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 134..228
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 240..390
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 392 AA; 41323 MW; 0607903C8AE66DB7 CRC64;
MDATPAPALD APAAGTLSAD ERAAILDAVR DFAATELAPH TLEWDVEKHF PRDVLRRAGD
LGLGGVYVND DVGGAGLTRA DAVAIFEELA YGDPTVTAYI TIHNMVAWMI DAYGTGAQRE
RWLPGLVAME DLGAYCLTEP GAGSDAAAIT TSAIRHGDTY VLTGVKQFIS GAGEASVYVV
MARTGEPGAR GISAFLVPAD AGGLSFGPKE KKMGWNAQPT RAVVLDEVSV PAENLLGGEG
RGFSIAMTAL NGGRLNIATC SLGGARWALD RAVAYVHERF TFGEPLAEKQ SVVFAVADMA
TELEAARLLV RDAALALDAG APDTATRCAM AKRFATDVGF RVANESLQLH GGYGYLQDYG
IEKVVRDLRV HQILEGTNEI MRLIVGRSVL AA
//
