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P29363 (THRC_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Threonine synthase
Short name=TS
EC=4.2.3.1
Gene names
Name:thrC
Ordered Locus Names:PA3735
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length469 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.

Sequence caution

The sequence CAA46168.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Threonine biosynthesis
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical termComplete proteome
Reference 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Threonine synthase
PRO_0000185639

Amino acid modifications

Modified residue1121N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict88 – 10114VAPLR…NEWVL → SGAAAPVERRTNGCV Ref.1
Sequence conflict151 – 1555GCRRC → AAAVA in CAA46168. Ref.1
Sequence conflict163 – 1642MH → ID in CAA46168. Ref.1
Sequence conflict1731Q → E in CAA46168. Ref.1
Sequence conflict1811L → H in CAA46168. Ref.1
Sequence conflict2801T → R in CAA46168. Ref.1
Sequence conflict294 – 30411RYDKDTLHPSL → ASTRHTLTPSV in CAA46168. Ref.1
Sequence conflict4651R → P in CAA46168. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29363 [UniParc].

Last modified January 11, 2001. Version 3.
Checksum: 224032B86272C79C

FASTA46951,795
        10         20         30         40         50         60 
MRYISTRGQA PALNFEDVLL AGLASDGGLY VPENLPRFTL EEIASWVGLP YHELAFRVMR 

        70         80         90        100        110        120 
PFVAGSIADA DFKKILEETY GVFAHDAVAP LRQLNGNEWV LELFHGPTLA FKDFALQLLG 

       130        140        150        160        170        180 
RLLDHVLAKR GERVVIMGAT SGDTGSAAIE GCRRCDNVDI FIMHPHNRVS EVQRRQMTTI 

       190        200        210        220        230        240 
LGDNIHNIAI EGNFDDCQEM VKASFADQGF LKGTRLVAVN SINWARIMAQ IVYYFHAALQ 

       250        260        270        280        290        300 
LGAPHRSVAF SVPTGNFGDI FAGYLARNMG LPVSQLIVAT NRNDILHRFM SGNRYDKDTL 

       310        320        330        340        350        360 
HPSLSPSMDI MVSSNFERLL FDLHGRNGKA VAELLDAFKA SGKLSVEDQR WTEARKLFDS 

       370        380        390        400        410        420 
LAVSDEQTCE TIAEVYRSSG ELLDPHTAIG VRAARECRRS LSVPMVTLGT AHPVKFPEAV 

       430        440        450        460 
EKAGIGQAPA LPAHLADLFE REERCTVLPN ELAKVQAFVS QHGNRGKPL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X65033 Genomic DNA. Translation: CAA46168.1. Different initiation.
AE004091 Genomic DNA. Translation: AAG07122.1.
PIRG83179.
SYPSRA. S27980.
RefSeqNP_252424.1. NC_002516.2.

3D structure databases

ProteinModelPortalP29363.
SMRP29363. Positions 1-462.
ModBaseSearch...

Protein-protein interaction databases

STRING208964.PA3735.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID880336.
KEGGpae:PA3735.
PATRIC19842099. VBIPseAer58763_3907.

Organism-specific databases

PseudoCAPPA3735.

Phylogenomic databases

eggNOGCOG0498.
HOGENOMHOG000230745.
KOK01733.
OMAEEIASWA.
ProtClustDBPRK09225.

Enzyme and pathway databases

UniPathwayUPA00050; UER00065.

Family and domain databases

InterProIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
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_PSEAE
AccessionPrimary (citable) accession number: P29363
Secondary accession number(s): Q9HXQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 11, 2001
Last modified: May 1, 2013
This is version 90 of the entry and version 3 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

SIMILARITY comments

Index of protein domains and families

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