P23669 (THRC_CORGL) 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:	Cgl2220, cg2437

Organism

Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]

Taxonomic identifier

196627 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › Corynebacterium glutamicum

Protein attributes

Sequence length	481 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. 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	Monomer. 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 – 481	481	Threonine synthase		PRO_0000185630
Amino acid modifications
	Modified residue	118	1	N6-(pyridoxal phosphate)lysine Probable
Experimental info
	Sequence conflict	61	1	A → R in CAA39510. Ref.1
	Sequence conflict	159	1	R → A in CAA82670. Ref.2
	Sequence conflict	404	1	V → S in CAA82670. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P23669 [UniParc]. Last modified July 11, 2002. Version 2. Checksum: BB9155C3317EE220	FASTA	481	52,931
	10 20 30 40 50 60 MDYISTRDAS RTPARFSDIL LGGLAPDGGL YLPATYPQLD DAQLSKWREV LANEGYAALA 70 80 90 100 110 120 AEVISLFVDD IPVEDIKAIT ARAYTYPKFN SEDIVPVTEL EDNIYLGHLS EGPTAAFKDM 130 140 150 160 170 180 AMQLLGELFE YELRRRNETI NILGATSGDT GSSAEYAMRG REGIRVFMLT PAGRMTPFQQ 190 200 210 220 230 240 AQMFGLDDPN IFNIALDGVF DDCQDVVKAV SADAEFKKDN RIGAVNSINW ARLMAQVVYY 250 260 270 280 290 300 VSSWIRTTTS NDQKVSFSVP TGNFGDICAG HIARQMGLPI DRLIVATNEN DVLDEFFRTG 310 320 330 340 350 360 DYRVRSSADT HETSSPSMDI SRASNFERFI FDLLGRDATR VNDLFGTQVR QGGFSLADDA 370 380 390 400 410 420 NFEKAAAEYG FASGRSTHAD RVATIADVHS RLDVLIDPHT ADGVHVARQW RDEVNTPIIV 430 440 450 460 470 480 LETALPVKFA DTIVEAIGEA PQTPERFAAI MDAPFKVSDL PNDTDAVKQY IVDAIANTSV K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The molecular structure of the Corynebacterium glutamicum threonine synthase gene." Han K.S., Archer J.A.C., Sinskey A.J. Mol. Microbiol. 4:1693-1702(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis and expression of the thrC gene of Brevibacterium lactofermentum and characterization of the encoded threonine synthase." Malumbres M., Mateos L.M., Lumbreras M.A., Guerrero C., Martin J.F. Appl. Environ. Microbiol. 60:2209-2219(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT. Strain: ATCC 13869 / DSMZ 1412 / NCIMB 9567.
[3]	"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes." Ikeda M., Nakagawa S. Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X56037 Genomic DNA. Translation: CAA39510.1. Z29563 Genomic DNA. Translation: CAA82670.1. BA000036 Genomic DNA. Translation: BAB99613.1. BX927154 Genomic DNA. Translation: CAF20560.1.
PIR	S11979.
RefSeq	NP_601423.1. NC_003450.3. YP_226461.1. NC_006958.1.
3D structure databases
ProteinModelPortal	P23669.
ModBase	Search...
Protein-protein interaction databases
STRING	196627.cg2437.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB99613; BAB99613; BAB99613. CAF20560; CAF20560; cg2437.
GeneID	1020172. 3342939.
KEGG	cgb:cg2437. cgl:NCgl2139.
PATRIC	21496442. VBICorGlu203724_2157.
Phylogenomic databases
eggNOG	COG0498.
HOGENOM	HOG000230745.
KO	K01733.
OMA	FGRIAFQ.
ProtClustDB	PRK09225.
Enzyme and pathway databases
BioCyc	CGLU196627:GJDM-2193-MONOMER.
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...

Entry information

Entry name

THRC_CORGL

Accession

Primary (citable) accession number: P23669
Secondary accession number(s): Q59211

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	July 11, 2002
Last modified:	May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program