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virulence, detoxification, adaptation
information pathways
cell wall and cell processes
stable RNAs
insertion seqs and phages
PE/PPE
intermediary metabolism and respiration
unknown
regulatory proteins
conserved hypotheticals
lipid metabolism
pseudogenes
General annotation
TypeCDS
FunctionInvolved in glyoxal pathway. Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid [catalytic activity: (S)-(2-hydroxyacyl)glutathione + H(2)O = glutathione + a 2-hydroxy acid anion].
ProductPossible glyoxalase II (hydroxyacylglutathione hydrolase) (GLX II)
CommentsRv2581c, (MTCY227.20), len: 224 aa. Possible glyoxalase II, equivalent to Q49649|YP81_MYCLE|ML0493|MLCB1259.11|B1177_C3_247 hypothetical 23.9 KDA protein from Mycobacterium leprae (218 aa), FASTA scores: opt: 1264, E(): 7.8e-73, (82.0% identity in 222 aa overlap). Also highly similar to Q9KXP1|SC9C5.33c possible hydrolase from Streptomyces coelicolor (235 aa), FASTA scores: opt: 654, E(): 2.9e-34, (46.8% identity in 220 aa overlap); and similar to Q9CI24|YFCI hypothetical protein from Lactococcus lactis (subsp. lactis) (Streptococcus lactis) (210 aa), FASTA scores: opt: 360, E(): 9.9e-16, (35.0% identity in 217 aa overlap); AAK75726|SP1646 metallo-beta-lactamase superfamily protein from Streptococcus pneumoniae (209 aa), FASTA scores: opt: 320, E(): 3.3e-13, (35.85% identity in 198 aa overlap); AAK80229|CAC2272 predicted Zn-dependent hydrolase of metallo-beta-lactamase superfamily from Clostridium acetobutylicum (199 aa), FASTA scores: opt: 282, E(): 8e-11, (32.7% identity in 217 aa overlap); etc. Equivalent to AAK46971 from Mycobacterium tuberculosis strain CDC1551 (246 aa) but shorter 22 aa. Belongs to the glyoxalase II family. Cofactor: binds two zinc ions.
Functional categoryVirulence, detoxification, adaptation
ProteomicsIdentified by proteomics at the Statens Serum Institute (Denmark) (See Rosenkrands et al., 2000). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the membrane protein fraction and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza et al., 2011). Translational start site supported by proteomics data (See Kelkar et al., 2011).
MutantNon-essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Essential gene domain for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011).
Check for mutants available at TARGET website
Coordinates
TypeStartEndOrientation
CDS29060892906763-
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2581c|Rv2581c
VLITGFPAGLLACNCYVLAERPGTDAVIVDPGQGAMGTLRRILDKNRLTPAAVLLTHGHIDHIWSAQKVSDTFGCPTYVHPADRFMLTDPIYGLGPRIAQLVAGAFFREPKQVVELDRDGDKIDLGGISVNIDHTPGHTRGSVVFRVLQATNNDKDIVFTGDTLFERAIGRTDLAGGSGRDLLRSIVDKLLVLDDSTVVLPGHGNSTTIGAERRFNPFLEGLSR