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P66902 (THRC_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Threonine synthase
Short name=TS
EC=4.2.3.1
Gene names
Name:thrC
Ordered Locus Names:Rv1295, MT1334
ORF Names:MTCY373.15
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. Ref.5

Catalytic activity

O-phospho-L-homoserine + H2O = L-threonine + phosphate. Ref.5

Cofactor

Pyridoxal phosphate. Ref.5

Enzyme regulation

Activity is not influenced by the addition of S-adenosylmethionine, the allosteric activator of TS from Arabidopsis thaliana. Ref.5

Pathway

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5.

Subunit structure

Homodimer. Ref.5

Miscellaneous

Was identified as a high-confidence drug target.

Sequence similarities

Belongs to the threonine synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=1.2 mM for O-phospho-L-homoserine (at pH 8.4 and 25 degrees Celsius) Ref.5

pH dependence:

Optimum pH is 9.5-10.5. Is inactive at pH values of 7 or less.

Temperature dependence:

Loses less than 10% of the initial activity during a 10 minutes incubation at 65 degrees Celsius. At 80 degrees Celsius, 90% of the activity is lost over the same time period.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360Threonine synthase
PRO_0000185637

Regions

Region196 – 2005Pyridoxal phosphate binding

Sites

Binding site951Pyridoxal phosphate
Binding site3261Pyridoxal phosphate

Amino acid modifications

Modified residue691N6-(pyridoxal phosphate)lysine
Cross-link151Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Secondary structure

1 .......................................................... 360
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P66902 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 43D27F553D5774B6

FASTA36037,322
        10         20         30         40         50         60 
MTVPPTATHQ PWPGVIAAYR DRLPVGDDWT PVTLLEGGTP LIAATNLSKQ TGCTIHLKVE 

        70         80         90        100        110        120 
GLNPTGSFKD RGMTMAVTDA LAHGQRAVLC ASTGNTSASA AAYAARAGIT CAVLIPQGKI 

       130        140        150        160        170        180 
AMGKLAQAVM HGAKIIQIDG NFDDCLELAR KMAADFPTIS LVNSVNPVRI EGQKTAAFEI 

       190        200        210        220        230        240 
VDVLGTAPDV HALPVGNAGN ITAYWKGYTE YHQLGLIDKL PRMLGTQAAG AAPLVLGEPV 

       250        260        270        280        290        300 
SHPETIATAI RIGSPASWTS AVEAQQQSKG RFLAASDEEI LAAYHLVARV EGVFVEPASA 

       310        320        330        340        350        360 
ASIAGLLKAI DDGWVARGST VVCTVTGNGL KDPDTALKDM PSVSPVPVDP VAVVEKLGLA

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
[4]"Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis."
Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E., Gygi S.P., Darwin K.H.
PLoS ONE 5:E8589-E8589(2010) [PubMed: 20066036] [Abstract]
Cited for: PUPYLATION AT LYS-151, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: ATCC 25618 / H37Rv.
[5]"Structural, biochemical, and in vivo investigations of the threonine synthase from Mycobacterium tuberculosis."
Covarrubias A.S., Hogbom M., Bergfors T., Carroll P., Mannerstedt K., Oscarson S., Parish T., Jones T.A., Mowbray S.L.
J. Mol. Biol. 381:622-633(2008) [PubMed: 18621388] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PLP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, REACTION MECHANISM.
Strain: ATCC 25618 / H37Rv.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842576 Genomic DNA. Translation: CAA97760.1.
AE000516 Genomic DNA. Translation: AAK45596.1.
PIRC70773.
RefSeqNP_215811.1. NC_000962.2.
NP_335782.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D1FX-ray2.50A/B1-360[»]
ProteinModelPortalP66902.
SMRP66902. Positions 10-358.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000001817; EBMYCP00000001817; EBMYCG00000001815.
EBMYCT00000071910; EBMYCP00000069969; EBMYCG00000071905.
GeneID886957.
924736.
GenomeReviewsGene locus MT1334 in contig AE000516_GR.
Gene locus Rv1295 in contig AL123456_GR.
KEGGmtc:MT1334.
mtu:Rv1295.
PATRIC18124698. VBIMycTub22151_1467.
TIGRMT1334.

Organism-specific databases

TubercuListRv1295.

Phylogenomic databases

GeneTreeEBGT00050000015763.
HOGENOMHBG694883.
OMAQQAVLCA.
PhylomeDBP66902.
ProtClustDBPRK07409.

Family and domain databases

InterProIPR001926. PyrdxlP-dep_enz_bsu.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR004450. Thr_synthase.
[Graphical view]
KOK01733.
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMsTIGR00260. ThrC. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHRC_MYCTU
AccessionPrimary (citable) accession number: P66902
Secondary accession number(s): Q10610
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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