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P74193 (THRC_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:sll1172
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length382 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
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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Threonine synthase
PRO_0000185641

Regions

Region219 – 2235Pyridoxal phosphate binding By similarity

Sites

Binding site1191Pyridoxal phosphate By similarity
Binding site3471Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue931N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P74193 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: FBC9AEEC2B7F6F35

FASTA38240,414
        10         20         30         40         50         60 
MISCHSFTMT PSAPNSTVLP SATPVCPQSS ACRWRGLIET YRPYLPVSDQ TPVVTLLEGN 

        70         80         90        100        110        120 
TPLIPAPAIA KRIGKDVRVF VKYDGLNPTG SFKDRGMTMA ISKAKEAGAK AVICASTGNT 

       130        140        150        160        170        180 
SAAAAAYARR AGLRAFVIIP DGYVALGKLG QALIYGAEVI AIDGNFDDAL TTVRQLSEHY 

       190        200        210        220        230        240 
PVTLVNSVNP YRLEGQKTAA FEIVDVLGQA PDWLCIPVGN AGNITAYWMG FCQYKELGKG 

       250        260        270        280        290        300 
DRLPRMMGFQ AAGSAPFIQG QPISHPETLA TAIRIGNPAN WDKAWAASRE SNGEFHPVTD 

       310        320        330        340        350        360 
AEILEAYRIL AAEEGVFCEP ASAASVAGLL KQKDQVPAGA TVVCVLTGNG LKDPDCAVQN 

       370        380 
SGNQVKAGLK PDLEIVAKAM GF 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA18282.1.
PIRS75823.
RefSeqNP_441602.1. NC_000911.1.
YP_005651660.1. NC_017277.1.
YP_007451484.1. NC_020286.1.

3D structure databases

ProteinModelPortalP74193.
SMRP74193. Positions 36-382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP74193. 1 interaction.
STRING1148.sll1172.

Proteomic databases

PaxDbP74193.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA18282; BAA18282; BAA18282.
GeneID953074.
KEGGsyn:sll1172.
syy:SYNGTS_1707.
syz:MYO_117250.
PATRIC23840641. VBISynSp132158_1875.

Phylogenomic databases

eggNOGCOG0498.
HOGENOMHOG000076503.
KOK01733.
OMARYASMLP.
OrthoDBEOG6HMX9M.
PhylomeDBP74193.

Enzyme and pathway databases

UniPathwayUPA00050; UER00065.

Family and domain databases

InterProIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR026260. Thr_Synthase_Gram_pos_bac.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
PIRSFPIRSF038945. Thr_synthase. 1 hit.
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR00260. thrC. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHRC_SYNY3
AccessionPrimary (citable) accession number: P74193
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways