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Protein

Threonine synthase

Gene

thrC

Organism
Bacillus sp. (strain ULM1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Cofactori

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei85 – 851Pyridoxal phosphateBy similarity
Binding sitei314 – 3141Pyridoxal phosphateBy similarity

GO - Molecular functioni

  1. pyridoxal phosphate binding Source: InterPro
  2. threonine synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. threonine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Threonine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00050; UER00065.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine synthase (EC:4.2.3.1)
Short name:
TS
Gene namesi
Name:thrC
OrganismiBacillus sp. (strain ULM1)
Taxonomic identifieri231717 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352Threonine synthasePRO_0000185625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591N6-(pyridoxal phosphate)lysineBy similarity

Structurei

3D structure databases

ProteinModelPortaliP09123.
SMRiP09123. Positions 2-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni185 – 1895Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Belongs to the threonine synthase family.Curated

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR026260. Thr_Synthase_bac/arc.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF038945. Thr_synthase. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09123-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYKGLLKQYA SYLPVNEKTP DVSLMEGNTP LIPLLNISKQ LGVQLYGKYE
60 70 80 90 100
GANPTGSFKD RGMVMAVAKA KEEGSEAIIC ASTGNTSASA AAYAARLGMK
110 120 130 140 150
CIIVIPEGKI AHGKLAQAVA YGAEIISIEG NFDDALKAVR NIAAEEPITL
160 170 180 190 200
VNSVNPYRIE GQKTAAFEIC DQLQNAPDVL AIPVGNAGNI TAYWKGFCEY
210 220 230 240 250
EKEKGYKKPR IHGFEAEGAA AIVKGHVIEE PETIATAIRI GNPASWSYAV
260 270 280 290 300
EAAEQSHGEI DMVSDEEILH AYRLLAKTEG VFAEPGSNAS LAGVIKHVES
310 320 330 340 350
GKIKKGETVV AVLTGNGLKD PDIAISSNQL DIASVSNDIE QIKDHIKGVI

MS
Length:352
Mass (Da):37,458
Last modified:July 1, 1989 - v1
Checksum:i192550176FAD7930
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z29562 Genomic DNA. Translation: CAA82669.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z29562 Genomic DNA. Translation: CAA82669.1.

3D structure databases

ProteinModelPortaliP09123.
SMRiP09123. Positions 2-325.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00050; UER00065.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR026260. Thr_Synthase_bac/arc.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF038945. Thr_synthase. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of the threonine synthase (thrC) gene of Brevibacterium lactofermentum."
    Malumbres M., Mateos L.M., Guerrero C., Martin J.F.
    Nucleic Acids Res. 16:9859-9859(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular cloning of the hom-thrC-thrB cluster from Bacillus sp. ULM1: expression of the thrC gene in Escherichia coli and corynebacteria, and evolutionary relationships of the threonine genes."
    Malumbres M., Mateos L.M., Guerrero C., Martin J.F.
    Folia Microbiol. (Praha) 40:595-606(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiTHRC_BACSL
AccessioniPrimary (citable) accession number: P09123
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to originate from B.lactofermentum=C.glutamicum.1 Publication

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.