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P27735 (THRC_SERMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 59. 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
OrganismSerratia marcescens
Taxonomic identifier615 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Protein attributes

Sequence length429 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429Threonine synthase
PRO_0000185640

Amino acid modifications

Modified residue1071N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P27735 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: B47262DE94848015

FASTA42947,094
        10         20         30         40         50         60 
MKLYNLKDHN EQVSFAQAIK QGLGKQQGLF FPLDLPEFEL TEIDHLLEQD FVTRSSRILS 

        70         80         90        100        110        120 
AFIGEEVPET ALKKRVQAAF EFPAPVAKVT DDVSCLELFH GPTLAFKDFG GRFMAQMLAE 

       130        140        150        160        170        180 
VAGEQPVTIL TATSGDTGAA VAHAFYGLKN VRVVILYPQG KISPLQEKLF CTLGGNIHTV 

       190        200        210        220        230        240 
AIDGDFDACQ ALVKQAFDDQ ELKDALHLNS ANSINISRLL AQICYYFEAV AQLPQEARNQ 

       250        260        270        280        290        300 
LVISVPSGNF GDLTAGLLAK SLGLPVKRFI AATNANDTVP RFLTSGQWQP HATVATLSNA 

       310        320        330        340        350        360 
MDVSQPNNWP RVEELFRRKV WQLKELGHAA VSDETTKDTM RELAELGYIS EPHAAIAYRA 

       370        380        390        400        410        420 
LRDQLQEGEF GLFLGTAHPA KFKESVEAIL GQELPLPKAL ALRAELPLLS HTLPASFGEL 


RKFLMGLPA 

« Hide

References

[1]"Nucleotide sequence of the Serratia marcescens threonine operon and analysis of the threonine operon mutations which alter feedback inhibition of both aspartokinase I and homoserine dehydrogenase I."
Omori K., Suzuki S., Komatsubara S.
J. Bacteriol. 175:785-794(1993) [PubMed: 8423151] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sr41.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10387 Genomic DNA. Translation: BAA01222.1.
X60821 Genomic DNA. Translation: CAA43214.1.
PIRS16043. D47057.

3D structure databases

ProteinModelPortalP27735.
SMRP27735. Positions 1-425.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001926. PyrdxlP-dep_enz_bsu.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR004450. Thr_synthase.
[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_SERMA
AccessionPrimary (citable) accession number: P27735
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: May 31, 2011
This is version 59 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

SIMILARITY comments

Index of protein domains and families