ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8K9V0

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name KHSE_BUCAP
Primary accession number Q8K9V0
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 47)
Name and origin of the protein
Protein name Homoserine kinase
Synonyms HSK
HK
EC 2.7.1.39
Gene name
Name: thrB
OrderedLocusNames: BUsg_187
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(2002).
Comments
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
AE013218; AAM67752.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660541.1; -.
3D structure databases
HSSP Q58504; 1H74. [HSSP ENTRY / PDB]
ModBase Q8K9V0.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG187-MON; -.
Ontologies
GO
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:0016310; Biological process: phosphorylation (inferred from electronic annotation from InterPro).
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.
ProtoNet Q8K9V0.
Genome annotation databases
GeneID 1005384; -.
GenomeReviews AE013218_GR; BUsg_187.
KEGG bas:BUsg187; -.
Phylogenomic databases
HOGENOM Q8K9V0; -.
Genome annotation databases
CMR Q8K9V0; BUsg_187.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Threonine biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   309  309     Homoserine kinase. PRO_0000156556
NP_BIND   91   101  11     ATP (Potential). 
Sequence information
Length: 309 AA [This is the length of the unprocessed precursor] Molecular weight: 34036 Da [This is the MW of the unprocessed precursor] CRC64: 76118A4C8CD1C3D3 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIKIYAPASV ANVGVGFDIL GAAIIPINGT LLGDCVTVKL SKKFELINKG IFSNKLPINK 

        70         80         90        100        110        120 
EQNIVWKCWF KFCKVIKKNI PVSIILEKNM PIGSGLGSSA CSVVATLVAI NQICNNPLNS 

       130        140        150        160        170        180 
KELLLLMGEI EGEISGSIHY DNVAPSYLGG LQLILEDSDI ISQKIPNFKH WFWIIAWPGI 

       190        200        210        220        230        240 
KVSTAEARKI LPKEYKKDIC IKNSRYLAGF IHASYTKQSH LAARCMQDFI AEPYRSKLLP 

       250        260        270        280        290        300 
NFLNAKEKIK KIGAISCGIS GSGPTIFAIS DKIKTAEKIS LWLKNNYLQN KTGFVHICAV 


DVKGVRKIG
Q8K9V0 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!