ID A0A0Q4G119_9BURK Unreviewed; 411 AA.
AC A0A0Q4G119;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Monooxygenase {ECO:0000313|EMBL:KQM71118.1};
GN ORFNames=ASE76_07815 {ECO:0000313|EMBL:KQM71118.1};
OS Xylophilus sp. Leaf220.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Xylophilus.
OX NCBI_TaxID=1735686 {ECO:0000313|EMBL:KQM71118.1, ECO:0000313|Proteomes:UP000051325};
RN [1] {ECO:0000313|EMBL:KQM71118.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM71118.1,
RC ECO:0000313|Proteomes:UP000051325};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM71118.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM71118.1,
RC ECO:0000313|Proteomes:UP000051325};
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 -!- 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:KQM71118.1}.
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DR EMBL; LMKO01000022; KQM71118.1; -; Genomic_DNA.
DR RefSeq; WP_055839882.1; NZ_LMKO01000022.1.
DR AlphaFoldDB; A0A0Q4G119; -.
DR STRING; 1735686.ASE76_07815; -.
DR OrthoDB; 7316074at2; -.
DR Proteomes; UP000051325; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_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; PF08028; Acyl-CoA_dh_2; 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.
PE 4: Predicted;
KW Monooxygenase {ECO:0000313|EMBL:KQM71118.1};
KW Oxidoreductase {ECO:0000313|EMBL:KQM71118.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051325}.
FT DOMAIN 36..102
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 255..390
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 42969 MW; 6976059B02402E64 CRC64;
MSCVLSSDPV HTLSPAPQRP SAGELQARMH ALLPAIKARA AATERMGRIP AESLAELHDA
GLFRVVQPRM FGGHEHDFDV LVDLVMTLGR ACASTAWVYG LYAAHQWLVA SFDAAAQHDV
WSDDADAVVC GSYAPAGQAV AEQGGYRLTG RWAFASGCDG AQWAVCASVL PAADGAPPPG
PAFFLVPAID YRIDGDWEVV GLAGTGSRTL VLDGAFVPQH RILTFKETTS GCTPGRRLHD
NPGFGIPMLS NIPSCLAATA VGAAAGALED YLAMTGQRVT RGAVAGGNNR MAEFPTIQLR
VAEAAASVDA AREVLLRDLR ARAATVRTGG TVDVDERIAS RRGQAFAVSL AIRGAEALNA
STGGQGLVLS NPVQRAWRDA NAVGRHISLN WDAVGTMAGQ NALGLAPKGQ Y
//
