LOCUS YP_970286 324 aa linear BCT 22-DEC-2012
DEFINITION homoserine kinase [Acidovorax citrulli AAC00-1].
ACCESSION YP_970286
VERSION YP_970286.1 GI:120610608
DBLINK Project: 58429
BioProject: PRJNA58429
DBSOURCE REFSEQ: accession NC_008752.1
KEYWORDS .
SOURCE Acidovorax citrulli AAC00-1
ORGANISM Acidovorax citrulli AAC00-1
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Comamonadaceae; Acidovorax.
REFERENCE 1 (residues 1 to 324)
AUTHORS Copeland,A., Lucas,S., Lapidus,A., Barry,K., Detter,J.C., Glavina
del Rio,T., Dalin,E., Tice,H., Pitluck,S., Kiss,H., Brettin,T.,
Bruce,D., Han,C., Tapia,R., Gilna,P., Schmutz,J., Larimer,F.,
Land,M., Hauser,L., Kyrpides,N., Kim,E., Stahl,D. and Richardson,P.
CONSRTM US DOE Joint Genome Institute
TITLE Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1
JOURNAL Unpublished
REFERENCE 2 (residues 1 to 324)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (04-JAN-2007) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
REFERENCE 3 (residues 1 to 324)
AUTHORS Copeland,A., Lucas,S., Lapidus,A., Barry,K., Detter,J.C., Glavina
del Rio,T., Dalin,E., Tice,H., Pitluck,S., Kiss,H., Brettin,T.,
Bruce,D., Han,C., Tapia,R., Gilna,P., Schmutz,J., Larimer,F.,
Land,M., Hauser,L., Kyrpides,N., Kim,E., Stahl,D. and Richardson,P.
CONSRTM US DOE Joint Genome Institute
TITLE Direct Submission
JOURNAL Submitted (13-DEC-2006) US DOE Joint Genome Institute, 2800
Mitchell Drive B100, Walnut Creek, CA 94598-1698, USA
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from ABM32512.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..324
/organism="Acidovorax citrulli AAC00-1"
/strain="AAC00-1"
/db_xref="taxon:397945"
Protein 1..324
/product="homoserine kinase"
/EC_number="2.7.1.39"
/calculated_mol_wt=35905
Region 9..309
/region_name="HomoserineK_II"
/note="Homoserine Kinase, type II. Homoserine kinase is
part of a larger superfamily that includes the catalytic
domains of other kinases, such as the typical
serine/threonine/tyrosine protein kinases (PKs), RIO
kinases, actin-fragmin kinase (AFK), and...; cd05153"
/db_xref="CDD:88616"
Region 26..258
/region_name="APH"
/note="Phosphotransferase enzyme family; pfam01636"
/db_xref="CDD:201896"
Site order(34,38,49,51,79,101..104,193,197..198,200,210..211,
230)
/site_type="active"
/note="putative active site [active]"
/db_xref="CDD:88616"
Site order(34,193,230)
/site_type="other"
/note="putative substrate binding site [chemical binding]"
/db_xref="CDD:88616"
Site order(38,49,51,79,101..104,193,197..198,200,210..211)
/site_type="other"
/note="ATP binding site [chemical binding]"
/db_xref="CDD:88616"
CDS 1..324
/locus_tag="Aave_1928"
/coded_by="complement(NC_008752.1:2090040..2091014)"
/note="catalyzes the formation of O-phospho-L-homoserine
from L-homoserine"
/transl_table=11
/db_xref="InterPro:IPR002575"
/db_xref="InterPro:IPR005280"
/db_xref="GeneID:4666306"
ORIGIN
1 mavftevskk eardllrrlq lgtleslrgi eggientnyf ltsdqgeyvl tlferltaeq
61 lpfylhlmkh laqagipvpd prgdrhgnil hsvagkpaav vnklpgrsql apgpvhcaav
121 ggmlarmhla grdyerrqpn lrglawwnet vpvvlphige aqrtllrsel ayqnhvaasa
181 gyaalprgpv hadlfrdnam fdgealtgff dfyfagvdtw lfdlavclnd wcidwptglh
241 esgraaamld ayqavrplsa derallpaml ragalrfwis rlwdfhlpre aslltphdpa
301 hfervlrgri arplharagg gfee
//
