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P09123

- THRC_BACSL

UniProt

P09123 - THRC_BACSL

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Protein

Threonine synthase

Gene
thrC
Organism
Bacillus sp. (strain ULM1)
Status
Reviewed - 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

Pyridoxal phosphate By similarity.

Pathwayi

Sites

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

Structurei

3D structure databases

ProteinModelPortaliP09123.
SMRiP09123. Positions 2-325.

Family & Domainsi

Region

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

Sequence similaritiesi

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR026260. Thr_Synthase_bac/arc.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[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

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MYKGLLKQYA SYLPVNEKTP DVSLMEGNTP LIPLLNISKQ LGVQLYGKYE    50
GANPTGSFKD RGMVMAVAKA KEEGSEAIIC ASTGNTSASA AAYAARLGMK 100
CIIVIPEGKI AHGKLAQAVA YGAEIISIEG NFDDALKAVR NIAAEEPITL 150
VNSVNPYRIE GQKTAAFEIC DQLQNAPDVL AIPVGNAGNI TAYWKGFCEY 200
EKEKGYKKPR IHGFEAEGAA AIVKGHVIEE PETIATAIRI GNPASWSYAV 250
EAAEQSHGEI DMVSDEEILH AYRLLAKTEG VFAEPGSNAS LAGVIKHVES 300
GKIKKGETVV AVLTGNGLKD PDIAISSNQL DIASVSNDIE QIKDHIKGVI 350
MS 352
Length:352
Mass (Da):37,458
Last modified:July 1, 1989 - v1
Checksum:i192550176FAD7930
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z29562 Genomic DNA. Translation: CAA82669.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z29562 Genomic DNA. Translation: CAA82669.1 .

3D structure databases

ProteinModelPortali P09123.
SMRi P09123. Positions 2-325.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00050 ; UER00065 .

Family and domain databases

InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR026260. Thr_Synthase_bac/arc.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
[Graphical view ]
PIRSFi PIRSF038945. Thr_synthase. 1 hit.
SUPFAMi SSF53686. SSF53686. 1 hit.
TIGRFAMsi TIGR00260. thrC. 1 hit.
PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 74 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 (1 Publication) thought to originate from B.lactofermentum=C.glutamicum.

Documents

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

External Data

Dasty 3

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