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Database: UniProt
Entry: A0A101A882_9MYCO
LinkDB: A0A101A882_9MYCO
Original site: A0A101A882_9MYCO 
ID   A0A101A882_9MYCO        Unreviewed;       493 AA.
AC   A0A101A882;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Monooxygenase {ECO:0000313|EMBL:KUI17263.1};
GN   ORFNames=AU193_02940 {ECO:0000313|EMBL:KUI17263.1};
OS   Mycobacterium sp. GA-1285.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1772282 {ECO:0000313|EMBL:KUI17263.1, ECO:0000313|Proteomes:UP000053702};
RN   [1] {ECO:0000313|EMBL:KUI17263.1, ECO:0000313|Proteomes:UP000053702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GA-1285 {ECO:0000313|EMBL:KUI17263.1,
RC   ECO:0000313|Proteomes:UP000053702};
RG   TB Trials Study Group;
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E.L., Macaden R.,
RA   Grewal H.M.S.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
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:KUI17263.1}.
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DR   EMBL; LQIS01000022; KUI17263.1; -; Genomic_DNA.
DR   RefSeq; WP_064422881.1; NZ_LQIS01000022.1.
DR   AlphaFoldDB; A0A101A882; -.
DR   STRING; 1772282.AU193_02940; -.
DR   OrthoDB; 5168853at2; -.
DR   Proteomes; UP000053702; Unassembled WGS sequence.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR43098:SF3; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF13738; Pyr_redox_3; 1.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000313|EMBL:KUI17263.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   493 AA;  55676 MW;  84613F5FC1539E55 CRC64;
     MTVPDHDTII VGAGFSGIGA GITLDKAGLG DYLIVEAGDG PGGTWYWNTY PGIAVDIPSF
     SYQFSFEQSP EWTRTYAPGH ELRAYAEHCV DKYGLRPKIR FNTKVLGAVF DDDETLWRIE
     LDSGDVVTAR FLINACGVLI TPKLPDIDGV DSFAGVTMHT ARWDHSQDLT GKRVAVIGTG
     ASAVQVIPEI APIVKQLTVF QRTPIWCFPK FDVPLSPMAR RMMRLPGGHV VQRLLSQAYV
     ELTFTLPAQY FTVNPMAKNM SKVGEAYLRK QVDDPEVRDK LTPRYAVGCK RPGFHNTYLS
     TYNRDNVELV TNPIDKITGS GVATVDGATR EADVLILATG FKVMDADDMP TYPVTGSGGR
     SWSRHWQEHR LQAYEGVSVP GFPNFFTVFG PYGYVGSSYF ALIETQTHHI VRCLKHARRR
     NARRVEVTQQ ANDRYFEEMM RKRHRQIFWQ ESCQLANSYY FDKNGDAPLR PTTTFEAYWR
     SRRFPLRDYA FSR
//
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