ID   Y492_MYCTO              Reviewed;         629 AA.
AC   P9WMV6; L0T3X0; Q11157;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Uncharacterized GMC-type oxidoreductase MT0511/MT0512;
DE            EC=1.1.-.-;
GN   OrderedLocusNames=MT0511/MT0512;
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 GMC oxidoreductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK44735.1; Type=Frameshift; Evidence={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; AAK44734.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AE000516; AAK44735.1; ALT_FRAME; Genomic_DNA.
DR   PIR; G70744; G70744.
DR   RefSeq; WP_003908534.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMV6; -.
DR   SMR; P9WMV6; -.
DR   EnsemblBacteria; AAK44734; AAK44734; MT0511.
DR   EnsemblBacteria; AAK44735; AAK44735; MT0512.
DR   KEGG; mtc:MT0511; -.
DR   KEGG; mtc:MT0512; -.
DR   PATRIC; fig|83331.31.peg.541; -.
DR   HOGENOM; CLU_008878_3_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..629
FT                   /note="Uncharacterized GMC-type oxidoreductase
FT                   MT0511/MT0512"
FT                   /id="PRO_0000427235"
FT   ACT_SITE        562
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
SQ   SEQUENCE   629 AA;  66154 MW;  A3F62AFCDA03D23C CRC64;
     MSRLADRAKS YPLASFGAAL LPPELGGPLP AQFVQRVDRY VTRLPATSRF AVRAGLASLA
     AASYLTTGRS LPRLHPDERA RVLHRIAALS PEVAAAVEGL KAIVLLANGA DTYAHELLAR
     AQEHDAARPD AELTVILSAD SPSVTRADAV VVGSGAGGAM VARTLARAGL DVVVLEEGRR
     WTVEEFRSTH PVDRYAGLYR GAGATVALGR PAVVLPMGRA VGGTTVVNSG TCFRPSLAVQ
     RRWRDEFGLG LADPDQLGRR LDDAEQTLRV APVPLEIMGR NGRLLLQAAK SLGWRAAPIP
     RNAPGCRGCC QCAIGCPSNA KFGVHLNALP QACAAGARII SWARVERILH RAGRAYGVRA
     RRPDGTTLDV LADAVVVAAG ATETPGLLRR SGLGGHPRLG HNLALHPATM LAGLFDDDVF
     AWRGVLQSAA VHEFHESDGV LIEATSTPPG MGSMVFPGYG AELLRWLDRA PQIATFGAMV
     ADRGVGTVRS VRGETVVRYD IAPGEIAKLR VALQAIGRLL FAAGAVEVLT GIPGAPPMRS
     LPELQDVLRR ANPRSLHLAA FHPTGTAAAG ADEQLCPVDA TGRLRGVEGV WVADASILPS
     CPEVNPQLSI MAMALAVADQ TVAKVVGVR