[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11. STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613; PubMed=2835591 [NCBI, ExPASy, EBI, Israel, Japan] Peoples O.P., Liebl W., Bodis M., Maeng P.J., Follettie M.T., Archer J.A.C., Sinskey A.J.; "Nucleotide sequence and fine structural analysis of the Corynebacterium glutamicum hom-thrB operon."; Mol. Microbiol. 2:63-72(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567; DOI=10.1093/nar/15.9.3922; PubMed=3035505 [NCBI, ExPASy, EBI, Israel, Japan] Mateos L.M., del Real G., Aguilar A., Martin J.F.; "Nucleotide sequence of the homoserine kinase (thr B) gene of Brevibacterium lactofermentum."; Nucleic Acids Res. 15:3922-3922(1987).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; Nakagawa S.; "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; DOI=10.1016/S0168-1656(03)00154-8; PubMed=12948626 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."; J. Biotechnol. 104:5-25(2003).

Comments

CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L-homoserine.
PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5 .
SUBCELLULAR LOCATION: Cytoplasm (Potential).
SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y00546; CAA68615.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00140; CAA68332.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000036; BAB98577.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX927151; CAF19888.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S00866; KIFKMG.

RefSeq

NP_600410.1; -.
YP_225474.1; -.

3D structure databases

ModBase

P07128.

Enzyme and pathway databases

BioCyc

CGLU196627-1:CG1338-MON; -.

2D gel databases

World-2DPAGE

0001:P07128; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004413;	Molecular function: homoserine kinase activity (inferred from electronic annotation from HAMAP).
GO:0009088;	Biological process: threonine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00384; -; 1.
PBIL [Tree]

InterPro

IPR006204; GHMP_kinase.
IPR013750; GHMP_kinase_C.
IPR006203; GHMP_knse_ATP_bd_CS.
IPR000870; Homoser_kin.
IPR014721; Ribosomal_S5_D2-type_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1.

Pfam

PF08544; GHMP_kinases_C; 1.
PF00288; GHMP_kinases_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000676; Homoser_kin; 1.

PRINTS

PR00958; HOMSERKINASE.

TIGRFAMs

TIGR00191; thrB; 1.

PROSITE

PS00627; GHMP_KINASES_ATP; 1.

Genome annotation databases

GeneID

1019167; -.
3345034; -.

GenomeReviews

BX927147_GR; cg1338.
BA000036_GR; Cgl1184.

KEGG

cgb:cg1338; -.
cgl:NCgl1137; -.

Phylogenomic databases

HOGENOM

P07128; -.

Genome annotation databases

CMR

P07128; Cgl1184.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding; Threonine biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 309`	`308`	`Homoserine kinase.`	`PRO_0000156565`
`NP_BIND`	`95 105`	`11`	`ATP (Potential).`
`CONFLICT`	`246 246`		`I -> V (in Ref. 2; CAA68332).`

Sequence information

Length: 309 AA [This is the length of the unprocessed precursor]

Molecular weight: 32620 Da [This is the MW of the unprocessed precursor]

CRC64: 89C807BC983A60E7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAIELNVGRK VTVTVPGSSA NLGPGFDTLG LALSVYDTVE VEIIPSGLEV EVFGEGQGEV 

        70         80         90        100        110        120 
PLDGSHLVVK AIRAGLKAAD AEVPGLRVVC HNNIPQSRGL GSSAAAAVAG VAAANGLADF 

       130        140        150        160        170        180 
PLTQEQIVQL SSAFEGHPDN AAASVLGGAV VSWTNLSIDG KSQPQYAAVP LEVQDNIRAT 

       190        200        210        220        230        240 
ALVPNFHAST EAVRRVLPTE VTHIDARFNV SRVAVMIVAL QQRPDLLWEG TRDRLHQPYR 

       250        260        270        280        290        300 
AEVLPITSEW VNRLRNRGYA AYLSGAGPTA MVLSTEPIPD KVLEDARESG IKVLELEVAG 


PVKVEVNQP

P07128 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools