Q8TQD4 (THRC_METAC) 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:	MA_1610

Organism

Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) [Reference proteome] [HAMAP]

Taxonomic identifier

188937 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina › Methanosarcina acetivorans

Protein attributes

Sequence length	405 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. Does not catalyze the conversion of O-acetyl-L-homoserine into 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	Homotrimer. Ref.2
Domain	The N-terminal 41 amino acids are required for activity. Ref.2
Sequence similarities	Belongs to the threonine synthase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Threonine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Lyase
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 – 405	405	Threonine synthase		PRO_0000392651
Regions
	Region	231 – 235	5	Pyridoxal phosphate binding By similarity
Sites
	Binding site	130	1	Pyridoxal phosphate By similarity
	Binding site	369	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	104	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8TQD4 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 3D2A303B42A4D942	FASTA	405	43,285
	10 20 30 40 50 60 MYHLKCIECG AEYSRDEVIY TCSKCDGLLD VIYDYSSIKI DMEKLKTECP SVWKYAKLLP 70 80 90 100 110 120 VEREPVTIQE GGTPLYKCDR LAEKIGIKKL YVKHEGMNPT GSFKDRGMTV GVTKALELGM 130 140 150 160 170 180 NTVACASTGN TSAALAIYGA KAGIPVVVLL PAGKVALGKV AQALMHGAKV LSIRGNFDDA 190 200 210 220 230 240 LALVRTLCSQ EKIYLLNSIN PYRLEGQKTI GFEIADQLDF KVPDRIVLPV GNAGNITAIY 250 260 270 280 290 300 KGFREFKILG ITDSLPKMTG IQAEGSCPIV KAIKSGAPAI TPEENPETVA TAIRIGNPVN 310 320 330 340 350 360 ATKALSAIRE SGGTAESVTD EEILAAQKDL ARLEGIGVEP ASAASVAGLR KLVDMGVIGR 370 380 390 400 DETVVCITTG HLLKDPQTVI DVCEEPTVVD ANIDAIREAI FGKAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE010299 Genomic DNA. Translation: AAM05023.1.
RefSeq	NP_616543.1. NC_003552.1.
3D structure databases
HSSP	HSSP built from PDB template 1E5X based on UniProtKB Q9S7B5.
ProteinModelPortal	Q8TQD4.
SMR	Q8TQD4. Positions 51-384.
ModBase	Search...
Protein-protein interaction databases
STRING	188937.MA1610.
Proteomic databases
PRIDE	Q8TQD4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM05023; AAM05023; MA_1610.
GeneID	1473498.
KEGG	mac:MA1610.
Phylogenomic databases
eggNOG	COG0498.
KO	K01733.
OMA	KCIVLLP.
ProtClustDB	PRK06260.
Enzyme and pathway databases
BioCyc	MACE188937:GI2O-1672-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_METAC

Accession

Primary (citable) accession number: Q8TQD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 23, 2010
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program