ID A0A0S9NXD5_9BURK Unreviewed; 407 AA.
AC A0A0S9NXD5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Monooxygenase {ECO:0000313|EMBL:KQP49849.1};
GN ORFNames=ASF44_04570 {ECO:0000313|EMBL:KQP49849.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP49849.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP49849.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP49849.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP49849.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP49849.1,
RC ECO:0000313|Proteomes:UP000051759};
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:KQP49849.1}.
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DR EMBL; LMNA01000001; KQP49849.1; -; Genomic_DNA.
DR RefSeq; WP_056897928.1; NZ_LMNA01000001.1.
DR AlphaFoldDB; A0A0S9NXD5; -.
DR STRING; 1736318.ASF44_04570; -.
DR OrthoDB; 571684at2; -.
DR Proteomes; UP000051759; 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:KQP49849.1};
KW Oxidoreductase {ECO:0000313|EMBL:KQP49849.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051759}.
FT DOMAIN 32..127
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 246..382
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 44176 MW; 1B08A600D893D31D CRC64;
MSSTALASAP APAAAPADAR DPAAALQRAQ ALATRFAATA AERDRRGGTP KAERDALRDS
GLLALSIPRA YGGHGADWQL TLRVVRVLAA ADSSLAHVFG FHHLMLATVR LFGQRAQWEP
WFAQTARHAW FWGNALNPLD ERTVATPQDG WHAFTGQKSF CSGALDSQML VASALHADTR
QLLVAAVPTA RSGIHAAPDW DNMGQRQTDS GSVTFEKVRV EAAELLTDPG PLSTPFACLR
PLVAQLVLAN VYLGIAENAF EDARRYTLHE ARPWPASPAA QAGDDPYVLA HYGEFWVGLE
GVRALAERAA ERLDTAWRRG EQLDAATRGE AAVAIAAAKV AATRVGLDLC TRMFDVAGAR
ATHGGLRLDR HWRNLRTQSL HDPADYKLRE LGEWALKRQH PHASFYT
//
