ID A0A1X0H178_9MYCO Unreviewed; 394 AA.
AC A0A1X0H178;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Monooxygenase {ECO:0000313|EMBL:ORB20062.1};
GN ORFNames=BST36_19910 {ECO:0000313|EMBL:ORB20062.1};
OS Mycolicibacterium moriokaense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=39691 {ECO:0000313|EMBL:ORB20062.1, ECO:0000313|Proteomes:UP000192354};
RN [1] {ECO:0000313|EMBL:ORB20062.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP105393 {ECO:0000313|EMBL:ORB20062.1};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (FEB-2017) 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:ORB20062.1}.
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DR EMBL; MVIB01000021; ORB20062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0H178; -.
DR OrthoDB; 3404950at2; -.
DR Proteomes; UP000192354; 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:ORB20062.1};
KW Oxidoreductase {ECO:0000313|EMBL:ORB20062.1}.
FT DOMAIN 23..104
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; 43039 MW; 9BCF2A5C136C8717 CRC64;
MTSIEQRDVQ SVLAGVDDLL PLIAKRAQAT EELRRLPDET VAELNEVGFF KLLQPEQWGG
LQCDPTLFYE AVRRIASACG STGWVASIIG VHNWHLALFD QQAQEDVWGD DPSVRISSSY
APMGAGTVVD GGYLVNGSWN WSSGCDHATW TFVGGPVIKD GKPVDFGSFL LPLGDYTIDD
VWHVVGLKGT GSNTLVVKDV FVPRHRFLSY KAMNDRTAGG LKTNTAPVYK MPWGTVHPTT
ISAPIVGMAY GAYDAHVEHQ GKRVRAAFAG EKAKDDPFAK VRIAEAASDI DAAWRQLMGN
VGDEYALLKA GQEIPFELRA RARRDQVRAT GRAIASIDRL FEASGATALS LDAPVQRFWR
DAHAGRVHAA NDPERAYLIF GNNEFGLPPQ DTMV
//
