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P23669 (THRC_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. 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:Cgl2220, cg2437
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. Ref.2

Catalytic activity

O-phospho-L-homoserine + H2O = L-threonine + phosphate. Ref.2

Cofactor

Pyridoxal phosphate. Ref.2

Pathway

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5.

Subunit structure

Monomer. Ref.2

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 – 481481Threonine synthase
PRO_0000185630

Amino acid modifications

Modified residue1181N6-(pyridoxal phosphate)lysine Probable

Experimental info

Sequence conflict611A → R in CAA39510. Ref.1
Sequence conflict1591R → A in CAA82670. Ref.2
Sequence conflict4041V → S in CAA82670. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P23669 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: BB9155C3317EE220

FASTA48152,931
        10         20         30         40         50         60 
MDYISTRDAS RTPARFSDIL LGGLAPDGGL YLPATYPQLD DAQLSKWREV LANEGYAALA 

        70         80         90        100        110        120 
AEVISLFVDD IPVEDIKAIT ARAYTYPKFN SEDIVPVTEL EDNIYLGHLS EGPTAAFKDM 

       130        140        150        160        170        180 
AMQLLGELFE YELRRRNETI NILGATSGDT GSSAEYAMRG REGIRVFMLT PAGRMTPFQQ 

       190        200        210        220        230        240 
AQMFGLDDPN IFNIALDGVF DDCQDVVKAV SADAEFKKDN RIGAVNSINW ARLMAQVVYY 

       250        260        270        280        290        300 
VSSWIRTTTS NDQKVSFSVP TGNFGDICAG HIARQMGLPI DRLIVATNEN DVLDEFFRTG 

       310        320        330        340        350        360 
DYRVRSSADT HETSSPSMDI SRASNFERFI FDLLGRDATR VNDLFGTQVR QGGFSLADDA 

       370        380        390        400        410        420 
NFEKAAAEYG FASGRSTHAD RVATIADVHS RLDVLIDPHT ADGVHVARQW RDEVNTPIIV 

       430        440        450        460        470        480 
LETALPVKFA DTIVEAIGEA PQTPERFAAI MDAPFKVSDL PNDTDAVKQY IVDAIANTSV 


K 

« Hide

References

« Hide 'large scale' references
[1]"The molecular structure of the Corynebacterium glutamicum threonine synthase gene."
Han K.S., Archer J.A.C., Sinskey A.J.
Mol. Microbiol. 4:1693-1702(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis and expression of the thrC gene of Brevibacterium lactofermentum and characterization of the encoded threonine synthase."
Malumbres M., Mateos L.M., Lumbreras M.A., Guerrero C., Martin J.F.
Appl. Environ. Microbiol. 60:2209-2219(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
Strain: ATCC 13869 / DSMZ 1412 / NCIMB 9567.
[3]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56037 Genomic DNA. Translation: CAA39510.1.
Z29563 Genomic DNA. Translation: CAA82670.1.
BA000036 Genomic DNA. Translation: BAB99613.1.
BX927154 Genomic DNA. Translation: CAF20560.1.
PIRS11979.
RefSeqNP_601423.1. NC_003450.3.
YP_226461.1. NC_006958.1.

3D structure databases

ProteinModelPortalP23669.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg2437.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB99613; BAB99613; BAB99613.
CAF20560; CAF20560; cg2437.
GeneID1020172.
KEGGcgb:cg2437.
cgl:NCgl2139.
PATRIC21496442. VBICorGlu203724_2157.

Phylogenomic databases

eggNOGCOG0498.
HOGENOMHOG000230745.
KOK01733.
OMAIANTSVK.
OrthoDBEOG65BDJX.

Enzyme and pathway databases

UniPathwayUPA00050; UER00065.

Family and domain databases

Gene3D3.90.1380.10. 1 hit.
InterProIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR029144. Thr_synth_N.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
PF14821. Thr_synth_N. 1 hit.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR00260. thrC. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHRC_CORGL
AccessionPrimary (citable) accession number: P23669
Secondary accession number(s): Q59211
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 11, 2002
Last modified: July 9, 2014
This is version 96 of the entry and version 2 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