ID A0A1A2ZWG5_9MYCO Unreviewed; 394 AA.
AC A0A1A2ZWG5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Monooxygenase {ECO:0000313|EMBL:OBI54053.1};
GN ORFNames=A5705_01590 {ECO:0000313|EMBL:OBI54053.1};
OS Mycobacterium sp. E787.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834150 {ECO:0000313|EMBL:OBI54053.1, ECO:0000313|Proteomes:UP000092152};
RN [1] {ECO:0000313|Proteomes:UP000092152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E787 {ECO:0000313|Proteomes:UP000092152};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Sam S., Sreng N.,
RA Him V., Kerleguer A., Cheng S.;
RL Submitted (JUN-2016) 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:OBI54053.1}.
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DR EMBL; LZKL01000042; OBI54053.1; -; Genomic_DNA.
DR RefSeq; WP_067873074.1; NZ_LZKL01000042.1.
DR AlphaFoldDB; A0A1A2ZWG5; -.
DR Proteomes; UP000092152; 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:OBI54053.1};
KW Oxidoreductase {ECO:0000313|EMBL:OBI54053.1}.
FT DOMAIN 23..99
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 240..372
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 394 AA; 43121 MW; B43CC7296E50EA7C CRC64;
MTSIQQRDAQ SVLAAIDDLL PRIAGRAQAT EDLRRLPDET VQELEEVGFF TLLQPEQWGG
LQCDPALFYE AVRRLASACG STGWVSSIIG VHNWHLALFD QRAQEEVWGE DPKTRISSSY
APMGAGVVTD GGYLVNGSWN WSSGCDHATW TFVGGPVIKD GRPVDFGSFL IPRSEYRIDD
VWHVVGLRGT GSNTLVVKDV FVPRHRFLSY KAMNDGTAGG YETNSAPVYK MPWGTMHPTT
ISAPIVGMAY GAYAAHVEHQ GKRVRAAFAG EKAKDDPFAK VRIAEAASDI DAAWRQLSGN
VADEYALLSA GKDIPFELRA RARRDQVRAT GRSIAAIDRL FEASGATALA NDQPVQRFWR
DAHAGRVHAA NDPERAYVIF GNNEFGLPPG DTMV
//
