A0R220 (THRC_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Threonine synthase
Short name=TS
EC=4.2.3.1

Gene names

Name:	thrC
Ordered Locus Names:	MSMEG_4956, MSMEI_4829

Organism

Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]

Taxonomic identifier

246196 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium smegmatis

Protein attributes

Sequence length	360 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity.
Catalytic activity	O-phospho-L-homoserine + H2O = L-threonine + phosphate.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the threonine synthase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Threonine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Lyase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro threonine synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 360	360	Threonine synthase		PRO_0000396139
Regions
	Region	196 – 200	5	Pyridoxal phosphate binding By similarity
Sites
	Binding site	95	1	Pyridoxal phosphate By similarity
	Binding site	326	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	69	1	N6-(pyridoxal phosphate)lysine By similarity
	Cross-link	151		Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Sequences

	Sequence		Length	Mass (Da)
	A0R220 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: C40EF7EED839FE94	FASTA	360	37,443
	10 20 30 40 50 60 MSAAKAAVHQ PWPGLIEAYR DRLPIGDDWT TVTLLEGGTP LIHAKRISEL TGCTVHLKVE 70 80 90 100 110 120 GLNPTGSFKD RGMTVAVTES LARGQQAVLC ASTGNTSASA AAYAARAGIT CAVLIPQGKI 130 140 150 160 170 180 AMGKLAQAVM HGAKIIQVDG NFDDCLELAR KLTADFPTIA LVNSVNPYRI EGQKTAAFEI 190 200 210 220 230 240 VDALGTAPDV HALPVGNAGN ITAYWKGYSE YHRDGVSDRL PRMLGTQAAG AAPLVTGAPV 250 260 270 280 290 300 KDPETIATAI RIGSPASWNS AVEAQQQSDG RFLAATDEEI LAAYHLVART EGVFVEPASA 310 320 330 340 350 360 ASIAGLLKSV EDGWVKRGST VVCTVTGNGL KDPDTALKGM PQVTPVPVDP SAVVAELGLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Expansion of the mycobacterial 'PUPylome'." Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V., Barry C.E. III, Bark S., Dorrestein P.C. Mol. Biosyst. 6:376-385(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PUPYLATION AT LYS-151, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000480 Genomic DNA. Translation: ABK71073.1. CP001663 Genomic DNA. Translation: AFP41274.1.
RefSeq	YP_006569569.1. NC_018289.1. YP_889208.1. NC_008596.1.
3D structure databases
ProteinModelPortal	A0R220.
SMR	A0R220. Positions 10-340.
ModBase	Search...
Protein-protein interaction databases
STRING	246196.MSMEG_4956.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABK71073; ABK71073; MSMEG_4956.
GeneID	13430049. 4536683.
KEGG	msg:MSMEI_4829. msm:MSMEG_4956.
PATRIC	18082211. VBIMycSme59918_4835.
Phylogenomic databases
eggNOG	COG0498.
HOGENOM	HOG000076503.
KO	K01733.
OMA	AMGKLSQ.
ProtClustDB	PRK07409.
Enzyme and pathway databases
BioCyc	MSME246196:GJ4Y-4955-MONOMER.
UniPathway	UPA00050; UER00065.
Family and domain databases
InterPro	IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. IPR026260. Thr_Synthase. IPR004450. Thr_synthase_like. IPR001926. Trp_syn_b_sub_like_PLP_eny_SF. [Graphical view]
Pfam	PF00291. PALP. 1 hit. [Graphical view]
PIRSF	PIRSF038945. Thr_synthase. 1 hit.
SUPFAM	SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMs	TIGR00260. thrC. 1 hit.
PROSITE	PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

THRC_MYCS2

Accession

Primary (citable) accession number: A0R220
Secondary accession number(s): I7GEF5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 10, 2010
Last sequence update:	January 9, 2007
Last modified:	May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program