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A0R220

- THRC_MYCS2

UniProt

A0R220 - THRC_MYCS2

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Protein

Threonine synthase

Gene

thrC

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed - Annotation score: 3 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.By similarity

Catalytic activityi

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

Cofactori

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951Pyridoxal phosphateBy similarity
Binding sitei326 – 3261Pyridoxal 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

BioCyciMSME246196:GJ4Y-4955-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:MSMEG_4956, MSMEI_4829
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000757: Chromosome, UP000006158: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360Threonine synthasePRO_0000396139Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei69 – 691N6-(pyridoxal phosphate)lysineBy similarity
Cross-linki151 – 151Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi246196.MSMEG_4956.

Structurei

3D structure databases

ProteinModelPortaliA0R220.
SMRiA0R220. Positions 10-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni196 – 2005Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Belongs to the threonine synthase family.Curated

Phylogenomic databases

eggNOGiCOG0498.
HOGENOMiHOG000076503.
KOiK01733.
OMAiDPDWAVA.
OrthoDBiEOG6HMX9M.

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.

A0R220-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAAKAAVHQ PWPGLIEAYR DRLPIGDDWT TVTLLEGGTP LIHAKRISEL
60 70 80 90 100
TGCTVHLKVE GLNPTGSFKD RGMTVAVTES LARGQQAVLC ASTGNTSASA
110 120 130 140 150
AAYAARAGIT CAVLIPQGKI AMGKLAQAVM HGAKIIQVDG NFDDCLELAR
160 170 180 190 200
KLTADFPTIA LVNSVNPYRI EGQKTAAFEI VDALGTAPDV HALPVGNAGN
210 220 230 240 250
ITAYWKGYSE YHRDGVSDRL PRMLGTQAAG AAPLVTGAPV KDPETIATAI
260 270 280 290 300
RIGSPASWNS AVEAQQQSDG RFLAATDEEI LAAYHLVART EGVFVEPASA
310 320 330 340 350
ASIAGLLKSV EDGWVKRGST VVCTVTGNGL KDPDTALKGM PQVTPVPVDP
360
SAVVAELGLS
Length:360
Mass (Da):37,443
Last modified:January 9, 2007 - v1
Checksum:iC40EF7EED839FE94
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK71073.1.
CP001663 Genomic DNA. Translation: AFP41274.1.
RefSeqiYP_006569569.1. NC_018289.1.
YP_889208.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK71073; ABK71073; MSMEG_4956.
AFP41274; AFP41274; MSMEI_4829.
GeneIDi4536683.
KEGGimsm:MSMEG_4956.
PATRICi18082211. VBIMycSme59918_4835.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK71073.1 .
CP001663 Genomic DNA. Translation: AFP41274.1 .
RefSeqi YP_006569569.1. NC_018289.1.
YP_889208.1. NC_008596.1.

3D structure databases

ProteinModelPortali A0R220.
SMRi A0R220. Positions 10-340.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 246196.MSMEG_4956.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK71073 ; ABK71073 ; MSMEG_4956 .
AFP41274 ; AFP41274 ; MSMEI_4829 .
GeneIDi 4536683.
KEGGi msm:MSMEG_4956.
PATRICi 18082211. VBIMycSme59918_4835.

Phylogenomic databases

eggNOGi COG0498.
HOGENOMi HOG000076503.
KOi K01733.
OMAi DPDWAVA.
OrthoDBi EOG6HMX9M.

Enzyme and pathway databases

UniPathwayi UPA00050 ; UER00065 .
BioCyci MSME246196:GJ4Y-4955-MONOMER.

Family and domain databases

InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR026260. Thr_Synthase_bac/arc.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[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

« Hide 'large scale' publications
  1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
    Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
    Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
    Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
    Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  4. Cited for: PUPYLATION AT LYS-151, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTHRC_MYCS2
AccessioniPrimary (citable) accession number: A0R220
Secondary accession number(s): I7GEF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: January 9, 2007
Last modified: November 26, 2014
This is version 59 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