ID A0A0Q8V6S1_9ACTN Unreviewed; 395 AA.
AC A0A0Q8V6S1;
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=Monooxygenase {ECO:0000313|EMBL:KRC50017.1};
GN ORFNames=ASE19_15455 {ECO:0000313|EMBL:KRC50017.1};
OS Nocardioides sp. Root79.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC50017.1, ECO:0000313|Proteomes:UP000051414};
RN [1] {ECO:0000313|EMBL:KRC50017.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC50017.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC50017.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC50017.1,
RC ECO:0000313|Proteomes:UP000051414};
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:KRC50017.1}.
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DR EMBL; LMIP01000013; KRC50017.1; -; Genomic_DNA.
DR RefSeq; WP_056893486.1; NZ_LMIP01000013.1.
DR AlphaFoldDB; A0A0Q8V6S1; -.
DR OrthoDB; 3404950at2; -.
DR Proteomes; UP000051414; 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 CDD; cd01159; NcnH; 1.
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; PTHR48083:SF19; FLAVIN-DEPENDENT MONOOXYGENASE, OXYGENASE SUBUNIT HSAA; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, 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:KRC50017.1};
KW Oxidoreductase {ECO:0000313|EMBL:KRC50017.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051414}.
FT DOMAIN 8..108
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 241..373
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 395 AA; 43280 MW; D0258562CD1E89CC CRC64;
MHDDFSPEVT AVLDGVRDLL PTFRERAEEG DRLRVIPDAS IKELEETGFF RLLQPKRYGG
LEADPIAFYT AVRDIASADG STGWVSSVVG VHPWQVALFA DEAQQAVWGD DQSVRLSSSY
APTGKAVITD GGFKLSGKWS FSSGSDHCAW VLLGGLVFNE EGQVVDFRTF MVPREKYQVV
DVWNVVGLRG TGSNDIVVEE TFIPEAFTLS MGETGACRGP GQAVNTSDLY KLPFHSIFTS
TIATPIIGMA KGAYAEHVEM QQKRVRAAYL GEKASLDPFA AVRIARASSE IDAAWALLMN
NIREEQAHVA KGEQIPLELR LRVRRDQVLG TARSIEAIDA LFEASGGRAL AEGTYLQRAW
RDAHAGRVHA ANDPERALQM YGGQQFGHKV DPGMY
//
