Q42598 (THRC_SCHPO) 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
ORF Names:	SPAC9E9.06c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	514 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.
Sequence similarities	Belongs to the threonine synthase family.
Caution	Was originally (Ref.1) thought to originate from A.thaliana.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Threonine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	threonine biosynthetic process Inferred from sequence or structural similarity. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nucleus Inferred from direct assay PubMed 16823372. Source: PomBase
Molecular_function	pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro threonine synthase activity Inferred from sequence orthology. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 514	514	Threonine synthase		PRO_0000185644
Amino acid modifications
	Modified residue	117	1	N6-(pyridoxal phosphate)lysine By similarity
	Modified residue	319	1	Phosphoserine Ref.4
	Modified residue	321	1	Phosphoserine Ref.4
Experimental info
	Sequence conflict	253 – 254	2	SV → PA in BAA13852. Ref.3
	Sequence conflict	446	1	C → W in BAA13852. Ref.3
	Sequence conflict	456	1	D → G in BAA13852. Ref.3
	Sequence conflict	459	1	V → G in BAA13852. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q42598 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 1C61AEFBB5F961C4	FASTA	514	57,632
	10 20 30 40 50 60 MSSQVSYLST RGGSSNFSFE EAVLKGLAND GGLFIPSEIP QLPSGWIEAW KDKSFPEIAF 70 80 90 100 110 120 EVMSLYIPRS EISADELKKL VDRSYSTFRH PETTPLKSLK NGLNVLELFH GPTFAFKDVA 130 140 150 160 170 180 LQFLGNLFEF FLTRKNGNKP EDERDHLTVV GATSGDTGSA AIYGLRGKKD VSVFILFPNG 190 200 210 220 230 240 RVSPIQEAQM TTVTDPNVHC ITVNGVFDDC QDLVKQIFGD VEFNKKHHIG AVNSINWARI 250 260 270 280 290 300 LSQITYYLYS YLSVYKQGKA DDVRFIVPTG NFGDILAGYY AKRMGLPTKQ LVIATNENDI 310 320 330 340 350 360 LNRFFKTGRY EKADSTQVSP SGPISAKETY SPAMDILVSS NFERYLWYLA LATEAPNHTP 370 380 390 400 410 420 AEASEILSRW MNEFKRDGTV TVRPEVLEAA RRDFVSERVS NDETIDAIKK IYESDHYIID 430 440 450 460 470 480 PHTAVGVETG LRCLEKTKDQ DITYICLSTA HPAKFDKAVN LALSSYSDYN FNTQVLPIEF 490 500 510 DGLLDEERTC IFSGKPNIDI LKQIIEVTLS REKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of cDNA encoding threonine synthase from Schizosaccharomyces pombe by functional expression in Saccharomyces cerevisiae." Aas S.F., Rognes S.E. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 972 / ATCC 24843.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[3]	"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-514. Strain: PR745.
[4]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319 AND SER-321, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z46263 mRNA. Translation: CAA86405.1. CU329670 Genomic DNA. Translation: CAB16415.1. D89190 mRNA. Translation: BAA13852.1.
PIR	T39213. T42748.
RefSeq	NP_594579.1. NM_001020008.2.
3D structure databases
ProteinModelPortal	Q42598.
SMR	Q42598. Positions 2-511.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC9E9.06c-1.
Proteomic databases
PaxDb	Q42598.
PRIDE	Q42598.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC9E9.06c.1; SPAC9E9.06c.1:pep; SPAC9E9.06c.
GeneID	2542653.
KEGG	spo:SPAC9E9.06c.
Organism-specific databases
PomBase	SPAC9E9.06c.
Phylogenomic databases
eggNOG	COG0498.
HOGENOM	HOG000230745.
KO	K01733.
OMA	EEIASWA.
OrthoDB	EOG43V33W.
Enzyme and pathway databases
UniPathway	UPA00050; UER00065.
Family and domain databases
InterPro	IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. IPR004450. Thr_synthase_like. IPR001926. Trp_syn_b_sub_like_PLP_eny_SF. [Graphical view]
Pfam	PF00291. PALP. 1 hit. [Graphical view]
SUPFAM	SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMs	TIGR00260. thrC. 1 hit.
PROSITE	PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20803702.

Entry information

Entry name

THRC_SCHPO

Accession

Primary (citable) accession number: Q42598
Secondary accession number(s): P78841

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program