ID   Y2280_MYCTO             Reviewed;         459 AA.
AC   P9WIT0; L0TBU2; Q50685; Q7D7C5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Uncharacterized FAD-linked oxidoreductase MT2338;
DE            EC=1.-.-.-;
GN   OrderedLocusNames=MT2338;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK46622.1; -; Genomic_DNA.
DR   PIR; D70731; D70731.
DR   RefSeq; WP_003411690.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIT0; -.
DR   EnsemblBacteria; AAK46622; AAK46622; MT2338.
DR   KEGG; mtc:MT2338; -.
DR   PATRIC; fig|83331.31.peg.2515; -.
DR   HOGENOM; CLU_017779_9_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..459
FT                   /note="Uncharacterized FAD-linked oxidoreductase MT2338"
FT                   /id="PRO_0000427951"
FT   DOMAIN          35..214
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   REGION          28..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   459 AA;  48052 MW;  5301BAD1396B4B0F CRC64;
     MSEMTARFSE IVGNANLLTG DAIPEDYAHD EELTGPPQKP AYAAKPATPE EVAQLLKAAS
     ENGVPVTARG SGCGLSGAAR PVEGGLLISF DRMNKVLEVD TANQVAVVQP GVALTDLDAA
     TADTGLRYTV YPGELSSSVG GNVGTNAGGM RAVKYGVARH NVLGLQAVLP TGEIIRTGGR
     MAKVSTGYDL TQLIIGSEGT LALVTEVIVK LHPRLDHNAS VLAPFADFDQ VMAAVPKILA
     SGLAPDILEY IDNTSMAALI STQNLELGIP DQIRDSCEAY LLVALENRIA DRLFEDIQTV
     GEMLMELGAV DAYVLEGGSA RKLIEAREKA FWAAKALGAD DIIDTVVPRA SMPKFLSTAR
     GLAAAADGAA VGCGHAGDGN VHMAIACKDP EKKKKLMTDI FALAMELGGA ISGEHGVGRA
     KTGYFLELED PVKISLMRRI KQSFDPAGIL NPGVVFGDT