Y1279_MYCTO
ID Y1279_MYCTO Reviewed; 528 AA.
AC P9WMV4; L0T7T5; P64263; Q11038;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Uncharacterized GMC-type oxidoreductase MT1316;
DE EC=1.1.-.-;
GN OrderedLocusNames=MT1316;
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 ---------------------------------------------------------------------------
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; AAK45577.1; -; Genomic_DNA.
DR PIR; G70755; G70755.
DR RefSeq; WP_003406598.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMV4; -.
DR SMR; P9WMV4; -.
DR EnsemblBacteria; AAK45577; AAK45577; MT1316.
DR KEGG; mtc:MT1316; -.
DR PATRIC; fig|83331.31.peg.1422; -.
DR HOGENOM; CLU_002865_7_2_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; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..528
FT /note="Uncharacterized GMC-type oxidoreductase MT1316"
FT /id="PRO_0000427236"
FT ACT_SITE 468
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 6..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 528 AA; 57331 MW; 9177AD391F994CB6 CRC64;
MDTQSDYVVV GTGSAGAVVA SRLSTDPATT VVALEAGPRD KNRFIGVPAA FSKLFRSEID
WDYLTEPQPE LDGREIYWPR GKVLGGSSSM NAMMWVRGFA SDYDEWAARA GPRWSYADVL
GYFRRIENVT AAWHFVSGDD SGVTGPLHIS RQRSPRSVTA AWLAAARECG FAAARPNSPR
PEGFCETVVT QRRGARFSTA DAYLKPAMRR KNLRVLTGAT ATRVVIDGDR AVGVEYQSDG
QTRIVYARRE VVLCAGAVNS PQLLMLSGIG DRDHLAEHDI DTVYHAPEVG CNLLDHLVTV
LGFDVEKDSL FAAEKPGQLI SYLLRRRGML TSNVGEAYGF VRSRPELKLP DLELIFAPAP
FYDEALVPPA GHGVVFGPIL VAPQSRGQIT LRSADPHAKP VIEPRYLSDL GGVDRAAMMA
GLRICARIAQ ARPLRDLLGS IARPRNSTEL DEATLELALA TCSHTLYHPM GTCRMGSDEA
SVVDPQLRVR GVDGLRVADA SVMPSTVRGH THAPSVLIGE KAADLIRS