TRLR_MYCTU
ID TRLR_MYCTU Reviewed; 207 AA.
AC O53193; F2GHK3; I6Y9D7; L0TBA9;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Thioredoxin-like reductase Rv2466c {ECO:0000303|PubMed:24877756};
GN OrderedLocusNames=Rv2466c {ECO:0000312|EMBL:CCP45259.1},
GN RVBD_2466c {ECO:0000312|EMBL:AFN50432.1};
GN ORFNames=LH57_13485 {ECO:0000312|EMBL:AIR15233.1},
GN P425_02568 {ECO:0000312|EMBL:KBJ30793.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RG The Broad Institute Genome Sequencing Platform;
RA Galagan J., Kreiswirth B., Dobos K., Fortune S., Fitzgerald M., Young S.K.,
RA Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Kreiswirth B., Gomez J., Victor T., Desjardins C., Abeel T.,
RA Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Murphy C., Naylor J., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA Monaco A., King S., Sohrabi A.;
RT "Phylogenetic analysis of Mycobacterial species using whole genome
RT sequences.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-28.
RC STRAIN=H37Rv;
RX PubMed=24877756; DOI=10.1021/cb500149m;
RA Albesa-Jove D., Chiarelli L.R., Makarov V., Pasca M.R., Urresti S.,
RA Mori G., Salina E., Vocat A., Comino N., Mohorko E., Ryabova S.,
RA Pfieiffer B., Lopes Ribeiro A.L., Rodrigo-Unzueta A., Tersa M., Zanoni G.,
RA Buroni S., Altmann K.H., Hartkoorn R.C., Glockshuber R., Cole S.T.,
RA Riccardi G., Guerin M.E.;
RT "Rv2466c mediates the activation of TP053 to kill replicating and non-
RT replicating Mycobacterium tuberculosis.";
RL ACS Chem. Biol. 9:1567-1575(2014).
CC -!- FUNCTION: In vitro, the reduced form of Rv2466c catalyzes the reduction
CC and activation of TP053, which is a thienopyrimidine derivative drug
CC that can kill both replicating and non-replicating M.tuberculosis.
CC {ECO:0000269|PubMed:24877756}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 0.0403 sec(-1). {ECO:0000269|PubMed:24877756};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24877756}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24877756}.
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; AL123456; CCP45259.1; -; Genomic_DNA.
DR EMBL; CP003248; AFN50432.1; -; Genomic_DNA.
DR EMBL; JLDD01000032; KBJ30793.1; -; Genomic_DNA.
DR EMBL; CP009480; AIR15233.1; -; Genomic_DNA.
DR RefSeq; NP_216982.1; NC_000962.3.
DR RefSeq; WP_003412664.1; NZ_NVQJ01000024.1.
DR PDB; 4NXI; X-ray; 1.70 A; A/B=1-207.
DR PDB; 4ZIL; X-ray; 1.51 A; A/B=1-207.
DR PDB; 5XUR; X-ray; 2.00 A; A/B/C/D=1-207.
DR PDBsum; 4NXI; -.
DR PDBsum; 4ZIL; -.
DR PDBsum; 5XUR; -.
DR AlphaFoldDB; O53193; -.
DR SMR; O53193; -.
DR STRING; 83332.Rv2466c; -.
DR PaxDb; O53193; -.
DR PRIDE; O53193; -.
DR DNASU; 888214; -.
DR GeneID; 45426458; -.
DR GeneID; 888214; -.
DR KEGG; mtu:Rv2466c; -.
DR KEGG; mtv:RVBD_2466c; -.
DR PATRIC; fig|83332.111.peg.2760; -.
DR TubercuList; Rv2466c; -.
DR eggNOG; COG2761; Bacteria.
DR HOGENOM; CLU_087602_1_0_11; -.
DR OMA; GMDAVGD; -.
DR PhylomeDB; O53193; -.
DR BRENDA; 1.20.4.3; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF01323; DSBA; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Oxidoreductase; Reference proteome.
FT CHAIN 1..207
FT /note="Thioredoxin-like reductase Rv2466c"
FT /id="PRO_0000433023"
FT MUTAGEN 28
FT /note="W->S: Lack of activity. Confers resistance to
FT TP053."
FT /evidence="ECO:0000269|PubMed:24877756"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:4ZIL"
FT HELIX 20..35
FT /evidence="ECO:0007829|PDB:4ZIL"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:4ZIL"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:4ZIL"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:4ZIL"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:4ZIL"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4ZIL"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:4ZIL"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:4ZIL"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:4ZIL"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:4ZIL"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:4NXI"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:4ZIL"
FT STRAND 161..170
FT /evidence="ECO:0007829|PDB:4ZIL"
FT HELIX 174..188
FT /evidence="ECO:0007829|PDB:4ZIL"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:4ZIL"
SQ SEQUENCE 207 AA; 23035 MW; DD86B7BD78C33CA9 CRC64;
MLEKAPQKSV ADFWFDPLCP WCWITSRWIL EVAKVRDIEV NFHVMSLAIL NENRDDLPEQ
YREGMARAWG PVRVAIAAEQ AHGAKVLDPL YTAMGNRIHN QGNHELDEVI TQSLADAGLP
AELAKAATSD AYDNALRKSH HAGMDAVGED VGTPTIHVNG VAFFGPVLSK IPRGEEAGKL
WDASVTFASY PHFFELKRTR TEPPQFD
