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Database: UniProt
Entry: X8CVL0_MYCIT
LinkDB: X8CVL0_MYCIT
Original site: X8CVL0_MYCIT 
ID   X8CVL0_MYCIT            Unreviewed;       649 AA.
AC   X8CVL0;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Thi4 family protein {ECO:0000313|EMBL:EUA59498.1};
GN   ORFNames=I550_2646 {ECO:0000313|EMBL:EUA59498.1};
OS   Mycobacterium intracellulare 1956.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1299331 {ECO:0000313|EMBL:EUA59498.1, ECO:0000313|Proteomes:UP000020825};
RN   [1] {ECO:0000313|EMBL:EUA59498.1, ECO:0000313|Proteomes:UP000020825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1956 {ECO:0000313|EMBL:EUA59498.1,
RC   ECO:0000313|Proteomes:UP000020825};
RA   Zelazny A., Olivier K., Holland S., Lenaerts A., Ordway D., DeGroote M.A.,
RA   Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA   Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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:EUA59498.1}.
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DR   EMBL; JAOG01000001; EUA59498.1; -; Genomic_DNA.
DR   AlphaFoldDB; X8CVL0; -.
DR   PATRIC; fig|1299331.3.peg.2577; -.
DR   Proteomes; UP000020825; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR42877; -; 1.
DR   PANTHER; PTHR42877:SF5; L-ORNITHINE N(5)-OXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   649 AA;  73209 MW;  EEB519EA6D301C47 CRC64;
     MRSRYAGDPF TTSTPEIAAA LEDVSIPTLL LSLVHITGDP RFIRDYKQMG IFLNEVQGFM
     SEEDKARARA EALTVITEYR DRGCPEPAPL SPELIREMMD WAACEHVPDD YLSLVSEELD
     LAGVDPRRPA ALPAERAAQL PVLVVGCGES GILAGVRLKQ ANIPFTIVEK NAGPGGTWWE
     NRYPGARVDV ANHFYCYSFE PNNDWTHFFA EQNELQDYFT KVIDEHDLAD RIRWQTEVLA
     AEWDDDDGTW TVSLRSADGR RSTLRARALI TAVGQLNRPN IPEFAGAQTF RGPSFHSAAW
     DHSVDLKGKR VALVGAGASG FQIAPAIAEE VERLTVFQRT AQWMFPNPMY HDEVGDGVRW
     AMRHLPFYGR WYRFLVLWPG SDKGLDAAEG DPNYADQDHA VSDINAGAHM MFSQWITSQV
     GEDSPLLAKV LPDYPACGKR TLQDNGSWLR TLQRDNVELV RTPIDRITPQ GIVTEDGVAH
     DVDVIVYATG FRHTDVLWPL KITGRNGVDL HKMWGSRPYA YLGITVPQFP NFFIVYGPGT
     HLAHGGSLIF QSELQMRYID QCLARLAEAD VHSVEPKLDA ATDWHRRTQT QIKKMVWSHP
     AVKHSYFKNA DGEIHTVSPW RLNEYWSAVR EPDWSQFVVR QKDQARQGK
//
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