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Search term: Rv0489

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namegpm1
Rv numberRv0489
Synonym(s)gpm
TypeCDS
FunctionInvolved in glycolysis [catalytic activity: 1,3-diphosphoglycerate + 3-phosphoglycerate = 2,3-diphosphoglycerate + 3-phosphoglycerate].
ProductProbable phosphoglycerate mutase 1 Gpm1 (phosphoglyceromutase) (PGAM) (BPG-dependent PGAM)
CommentsRv0489, (MTCY20G9.15), len: 249 aa. Probable gpm1, phosphoglycerate mutase 1, equivalent to P53531|PMGY_MYCLE phosphoglycerate mutase from Mycobacterium leprae (247 aa). Also highly similar to others e.g. PMG1_ECOLI|P31217 (249 aa), FASTA scores: opt: 805, E(): 0, (51.4% identity in 245 aa overlap); etc. Contains PS00175 Phosphoglycerate mutase family phosphohistidine signature, and PS00017 ATP/GTP-binding site motif A (P-loop). Belongs to the phosphoglycerate mutase family. Note that previously known as gpm.
Molecular mass (Da)27215.8
Isoelectric point5.3443
Gene length (bp)750
Protein length249
Location (kb)578.426


Functional categoryintermediary metabolism and respiration


ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Detected by 2-DE and MS in M. tuberculosis H37Rv purified from phagosomes of infected murine bone marrow macrophages but not in H37Rv broth-cultures (See Mattow et al., 2006). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the culture filtrate, membrane protein fraction, and whole cell lysates of M. tuberculosis H37Rv (See de Souza et al., 2011). Translational start site supported by proteomics data (See de Souza et al., 2011) (See Kelkar et al., 2011).
MutationEssential gene for in vitro growth of H37Rv, by sequencing of Himar1-based transposon mutagenesis (See Griffin et al., 2011). Check for mutants available at TARGET website


Coordinates
TypeStartEndOrientation
CDS578426579175+


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv0489|gpm1
MANTGSLVLLRHGESDWNALNLFTGWVDVGLTDKGQAEAVRSGELIAEHDLLPDVLYTSL
LRRAITTAHLALDSADRLWIPVRRSWRLNERHYGALQGLDKAETKARYGEEQFMAWRRSY
DTPPPPIERGSQFSQDADPRYADIGGGPLTECLADVVARFLPYFTDVIVGDLRVGKTVLI
VAHGNSLRALVKHLDQMSDDEIVGLNIPTGIPLRYDLDSAMRPLVRGGTYLDPEAAAAGA
AAVAGQGRG
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

Add extra bases upstream (5') and downstream (3')



Structural information
PFAMP0A5R6
Protein Data Bank1RII


Orthologs/Cross-references
CDC1551MT0508
Enzyme Classification5.4.2.1
Gene Ontologyglycolysis
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
M. bovisMb0499
M. lepraeML2441
M. marinumMMAR_0814
M. smegmatisMSMEG_0935
UniProtP0A5R6
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv0489


Expression Data
TBDBRv0489


Bibliography
Gu S, Chen J, Dobos KM, Bradbury EM, Belisle JT, Chen X,
Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain.
Mol Cell Proteomics (2003) 2(12):1284-96
Cited for: Proteomics
Muller P, Sawaya MR, Pashkov I, Chan S, Nguyen C, Wu Y, Perry LJ, Eisenberg D,
The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase.
Acta Crystallogr D Biol Crystallogr (2005) 61(Pt 3):309-15
Cited for: Structure
Mattow J, Siejak F, Hagens K, Becher D, Albrecht D, Krah A, Schmidt F, Jungblut PR, Kaufmann SH, Schaible UE,
Proteins unique to intraphagosomally grown Mycobacterium tuberculosis.
Proteomics (2006) 6(8):2485-94
Cited for: Proteomics
Malen H, Pathak S, Softeland T, de Souza GA, Wiker HG,
Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv.
BMC Microbiol (2010) 10:132
Cited for: Proteomics
de Souza GA, Arntzen MO, Fortuin S, Schurch AC, Malen H, McEvoy CR, van Soolingen D, Thiede B, Warren RM, Wiker HG,
Proteogenomic analysis of polymorphisms and gene annotation divergences in prokaryotes using a clustered mass spectrometry-friendly database.
Mol Cell Proteomics (2011) 10(1):M110.002527
Cited for: Proteomics/Sequence
de Souza GA, Leversen NA, Malen H, Wiker HG,
Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway.
J Proteomics (2011) 75(2):502-10
Cited for: Proteomics
Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A,
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol Cell Proteomics (2011) 10(12):M111.011627
Cited for: Proteomics/Sequence
Griffin JE, Gawronski JD, Dejesus MA, Ioerger TR, Akerley BJ, Sassetti CM,
High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism.
PLoS Pathog (2011) 7(9):e1002251
Cited for: Mutant