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Protein

Threonine synthase

Gene

thrC

Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. Does not catalyze the conversion of O-acetyl-L-homoserine into threonine.1 Publication

Catalytic activityi

O-phospho-L-homoserine + H2O = L-threonine + phosphate.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301Pyridoxal phosphateBy similarity
Binding sitei369 – 3691Pyridoxal 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

BioCyciMACE188937:GI2O-1626-MONOMER.
UniPathwayiUPA00050; UER00065.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine synthase (EC:4.2.3.1)
Short name:
TS
Gene namesi
Name:thrC
Ordered Locus Names:MA_1610
OrganismiMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifieri188937 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
ProteomesiUP000002487: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 405405Threonine synthasePRO_0000392651Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiQ8TQD4.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

STRINGi188937.MA1610.

Structurei

3D structure databases

ProteinModelPortaliQ8TQD4.
SMRiQ8TQD4. Positions 51-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni231 – 2355Pyridoxal phosphate bindingBy similarity

Domaini

The N-terminal 41 amino acids are required for activity.1 Publication

Sequence similaritiesi

Belongs to the threonine synthase family.Curated

Phylogenomic databases

eggNOGiCOG0498.
InParanoidiQ8TQD4.
KOiK01733.
OMAiQSHHADP.
PhylomeDBiQ8TQD4.

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.

Q8TQD4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYHLKCIECG AEYSRDEVIY TCSKCDGLLD VIYDYSSIKI DMEKLKTECP
60 70 80 90 100
SVWKYAKLLP VEREPVTIQE GGTPLYKCDR LAEKIGIKKL YVKHEGMNPT
110 120 130 140 150
GSFKDRGMTV GVTKALELGM NTVACASTGN TSAALAIYGA KAGIPVVVLL
160 170 180 190 200
PAGKVALGKV AQALMHGAKV LSIRGNFDDA LALVRTLCSQ EKIYLLNSIN
210 220 230 240 250
PYRLEGQKTI GFEIADQLDF KVPDRIVLPV GNAGNITAIY KGFREFKILG
260 270 280 290 300
ITDSLPKMTG IQAEGSCPIV KAIKSGAPAI TPEENPETVA TAIRIGNPVN
310 320 330 340 350
ATKALSAIRE SGGTAESVTD EEILAAQKDL ARLEGIGVEP ASAASVAGLR
360 370 380 390 400
KLVDMGVIGR DETVVCITTG HLLKDPQTVI DVCEEPTVVD ANIDAIREAI

FGKAK
Length:405
Mass (Da):43,285
Last modified:June 1, 2002 - v1
Checksum:i3D2A303B42A4D942
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM05023.1.
RefSeqiNP_616543.1. NC_003552.1.

Genome annotation databases

EnsemblBacteriaiAAM05023; AAM05023; MA_1610.
GeneIDi1473498.
KEGGimac:MA1610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM05023.1.
RefSeqiNP_616543.1. NC_003552.1.

3D structure databases

ProteinModelPortaliQ8TQD4.
SMRiQ8TQD4. Positions 51-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi188937.MA1610.

Proteomic databases

PRIDEiQ8TQD4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM05023; AAM05023; MA_1610.
GeneIDi1473498.
KEGGimac:MA1610.

Phylogenomic databases

eggNOGiCOG0498.
InParanoidiQ8TQD4.
KOiK01733.
OMAiQSHHADP.
PhylomeDBiQ8TQD4.

Enzyme and pathway databases

UniPathwayiUPA00050; UER00065.
BioCyciMACE188937:GI2O-1626-MONOMER.

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

« Hide 'large scale' publications
  1. "The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity."
    Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.
    , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.
    Genome Res. 12:532-542(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.
  2. "Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase."
    Graham D.E., Taylor S.M., Wolf R.Z., Namboori S.C.
    Biochem. J. 424:467-478(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, SUBUNIT.

Entry informationi

Entry nameiTHRC_METAC
AccessioniPrimary (citable) accession number: Q8TQD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: June 1, 2002
Last modified: February 4, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.