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Q9ZMX5 (THRC_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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:jhp_0090
OrganismHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity.

Pathway

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

Sequence similarities

Belongs to the threonine synthase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Threonine biosynthesis
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processthreonine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionpyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

threonine synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Threonine synthase
PRO_0000185634

Amino acid modifications

Modified residue1091N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZMX5 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 3A3C66613ADB4920

FASTA48654,654
        10         20         30         40         50         60 
MPFVPTRSLK ERKIDFIEAV LNPNAPKGGL YTLEHFETLE WQDCLGMSYS ELVEHVFELL 

        70         80         90        100        110        120 
NLEIPKNLLA SALKRYENFD NPKNPAPIFA LNERLFVQEL YHGPSLAFKD MALQPLASLF 

       130        140        150        160        170        180 
SNLAVGKNEK YLVLVSTSGD TGPATLEGLA GMPNVFVVCL YPKDGTSLVQ KLQMVTQNAS 

       190        200        210        220        230        240 
NLKVFGVSGD FDDAQNALKN LLKDDDFNEA LKARQLKLSV ANSVNFGRIA FQIVYHIWGF 

       250        260        270        280        290        300 
LELYKKGAIN SKEKITLAIP SGNFGNALGA FYAKKMGLNI AKIKVVTNSN DVLREFIETG 

       310        320        330        340        350        360 
RYDLTKRSLK QTFSPAMDIL KSSNVERALF SLFGFERTLE LMQALEEEKF YALKPKELAL 

       370        380        390        400        410        420 
LQEHFSCASC SDEDCLKTIQ EVYAEHQYLI DPHTATALNA SLKTHEKTLV SATASYEKFP 

       430        440        450        460        470        480 
KTTLLALNEQ KKNDDDKAAL ETLKNSYNTP DSQRLDDLFE RGIKHQEVLK LNEIKSSILL 


WLENTH 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99 / ATCC 700824.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001439 Genomic DNA. Translation: AAD05671.1.
PIRA71975.
RefSeqNP_222811.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZMX5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING85963.jhp0090.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD05671; AAD05671; jhp_0090.
GeneID889337.
KEGGhpj:jhp0090.
PATRIC20604784. VBIHelPyl98156_0104.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0498.
KOK01733.
OMAILLWLES.
OrthoDBEOG65BDJX.

Enzyme and pathway databases

BioCycHPYL85963:GJB9-97-MONOMER.
UniPathwayUPA00050; UER00065.

Family and domain databases

Gene3D3.90.1380.10. 1 hit.
InterProIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR029144. Thr_synth_N.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR00260. thrC. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHRC_HELPJ
AccessionPrimary (citable) accession number: Q9ZMX5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: June 11, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways