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P45837 (THRC_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 90. 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:ML1130
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length360 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.

Subunit structure

Homodimer By similarity.

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 – 360360Threonine synthase
PRO_0000185636

Regions

Region196 – 2005Pyridoxal phosphate binding By similarity

Sites

Binding site951Pyridoxal phosphate By similarity
Binding site3261Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P45837 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 96A06F7B17B2688B

FASTA36037,385
        10         20         30         40         50         60 
MSGQQTTTHQ PWPGVIAAYR DRLPVGDDWT PVTLLEGGTP LIAAPRLSEQ TGCTIHLKVE 

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

       130        140        150        160        170        180 
AMGKLAQAVM HGAKIIQIDG NFDDCLELAR KMAADFPMIS LVNSVNPVRI EGQKTAVFEI 

       190        200        210        220        230        240 
VDALGTAPHV HALPVGNAGN ITAYWKGYTE YHADGLIDRL PRMLGTQAAG AAPLVLGEPV 

       250        260        270        280        290        300 
SHPETIATAI RIGSPASWTS AVEAQQQSKG RFLAATDEEI LAAYHLVARA EGVFVEPASA 

       310        320        330        340        350        360 
ASIAGLLKAI DGGWVARGST VVCTITGNGL KDPDTALKDM PSVSPVPVDA VAVVEQLGLV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U15186 Genomic DNA. Translation: AAA63090.1.
AL583920 Genomic DNA. Translation: CAC31511.1.
PIRT09991.
RefSeqNP_301824.1. NC_002677.1.

3D structure databases

ProteinModelPortalP45837.
SMRP45837. Positions 10-358.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML1130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC31511; CAC31511; CAC31511.
GeneID910224.
KEGGmle:ML1130.
PATRIC18054215. VBIMycLep78757_2052.

Organism-specific databases

LepromaML1130.
CMRSearch...

Phylogenomic databases

eggNOGCOG0498.
HOGENOMHOG000076503.
KOK01733.
OMAGLKDPDW.
OrthoDBEOG6HMX9M.
ProtClustDBPRK07409.

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_MYCLE
AccessionPrimary (citable) accession number: P45837
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 13, 2013
This is version 90 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