LOCUS YP_031994 418 aa linear BCT 21-DEC-2012
DEFINITION aspartate kinase [Bartonella quintana str. Toulouse].
ACCESSION YP_031994
VERSION YP_031994.1 GI:49473952
DBLINK Project: 57635
BioProject: PRJNA57635
DBSOURCE REFSEQ: accession NC_005955.1
KEYWORDS .
SOURCE Bartonella quintana str. Toulouse
ORGANISM Bartonella quintana str. Toulouse
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Bartonellaceae; Bartonella.
REFERENCE 1 (residues 1 to 418)
AUTHORS Alsmark,C.M., Frank,A.C., Karlberg,E.O., Legault,B.A., Ardell,D.H.,
Canback,B., Eriksson,A.S., Naslund,A.K., Handley,S.A., Huvet,M., La
Scola,B., Holmberg,M. and Andersson,S.G.
TITLE The louse-borne human pathogen Bartonella quintana is a genomic
derivative of the zoonotic agent Bartonella henselae
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 101 (26), 9716-9721 (2004)
PUBMED 15210978
REFERENCE 2 (residues 1 to 418)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (11-SEP-2004) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
REFERENCE 3 (residues 1 to 418)
AUTHORS Frank,A.C.
TITLE Direct Submission
JOURNAL Submitted (08-JUN-2004) Dept. of Molecular Evolution, Evolutionary
Biology Centre, Uppsala University, Sweden
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from CAF25806.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..418
/organism="Bartonella quintana str. Toulouse"
/strain="Toulouse"
/db_xref="taxon:283165"
Protein 1..418
/product="aspartate kinase"
/EC_number="2.7.2.4"
/calculated_mol_wt=45132
Region 1..416
/region_name="PRK06635"
/note="aspartate kinase; Reviewed"
/db_xref="CDD:180641"
Region 3..253
/region_name="AAK_AKii-LysC-BS"
/note="AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily
(AAK), AKii; this CD includes the N-terminal catalytic
aspartokinase (AK) domain of the lysine-sensitive
aspartokinase isoenzyme AKII of Bacillus subtilis 168, and
the lysine plus threonine-sensitive...; cd04261"
/db_xref="CDD:58627"
Site order(7,9..11,175..176,179..180)
/site_type="other"
/note="putative nucleotide binding site [chemical
binding]"
/db_xref="CDD:58627"
Site order(7,47,75)
/site_type="active"
/note="putative catalytic residues [active]"
/db_xref="CDD:58627"
Site order(41,47,155,183)
/site_type="other"
/note="putative Mg ion binding site [ion binding]"
/db_xref="CDD:58627"
Site order(41..42,47,75)
/site_type="other"
/note="putative aspartate binding site [chemical binding]"
/db_xref="CDD:58627"
Region 273..344
/region_name="ACT_AKii-LysC-BS-like_1"
/note="ACT domains of the lysine-sensitive aspartokinase
isoenzyme AKII of Bacillus subtilis (BS) strain 168 and
related proteins; cd04913"
/db_xref="CDD:153185"
Site 310..311
/site_type="other"
/note="putative allosteric regulatory site"
/db_xref="CDD:153185"
Region 353..415
/region_name="ACT_AKii-LysC-BS-like_2"
/note="ACT domains of the lysine-sensitive, aspartokinase
(AK) isoenzyme AKII of Bacillus subtilis (BS) strain 168
and related domains; cd04936"
/db_xref="CDD:153208"
Site 353
/site_type="other"
/note="putative allosteric regulatory residue"
/db_xref="CDD:153208"
CDS 1..418
/gene="lysC"
/locus_tag="BQ03060"
/coded_by="NC_005955.1:379084..380340"
/inference="non-experimental evidence, no additional
details recorded"
/note="catalyzes the formation of 4-phospho-L-aspartate
from L-aspartate and ATP, in Bacillus, lysine sensitive;
regulated by response to starvation."
/transl_table=11
/db_xref="GeneID:2867224"
ORIGIN
1 marivmkfgg tsvanierih nvarhikrev dagnevavvv samagktnel vqwtrdaspm
61 hkdadeydvv vasgeqitag llalklqamg vnarswlgwq ipihtdnvhg saritdings
121 fliqrfqegq vaviagfqgl apdnristlg rggsdtsava iaaavqadrc diytdvdgvy
181 ttdpriepka rllpkvafee mlemaslgak vlqvrsvela mvhkvrtfvr ssfedpdalg
241 mddpinssgt licdedeile qqnvtgiafa kdeaqislrr ladrpgisaa ifgplaeeri
301 nvdmivqnis edgsktdmtf tvpsvdveka vtlleknrke igfdvlqfer nlakvsvigi
361 gmrshagvaa tafkalsekg iniqaittse ikisilidha ytelavrtlh alygldkg
//