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Database: UniProt/TrEMBL
Entry: Q6G0I0_BARQU
LinkDB: Q6G0I0_BARQU
Original site: Q6G0I0_BARQU 
ID   Q6G0I0_BARQU            Unreviewed;       418 AA.
AC   Q6G0I0;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   01-OCT-2014, entry version 76.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   Name=lysC {ECO:0000313|EMBL:CAF25806.1};
GN   OrderedLocusNames=BQ03060 {ECO:0000313|EMBL:CAF25806.1};
OS   Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283165 {ECO:0000313|EMBL:CAF25806.1, ECO:0000313|Proteomes:UP000000597};
RN   [1] {ECO:0000313|Proteomes:UP000000597}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse {ECO:0000313|Proteomes:UP000000597};
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-
CC       aspartate. {ECO:0000256|RuleBase:RU003448}.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC       {ECO:0000256|RuleBase:RU003448}.
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DR   EMBL; BX897700; CAF25806.1; -; Genomic_DNA.
DR   RefSeq; YP_031994.1; NC_005955.1.
DR   ProteinModelPortal; Q6G0I0; -.
DR   STRING; 283165.BQ03060; -.
DR   PRIDE; Q6G0I0; -.
DR   EnsemblBacteria; CAF25806; CAF25806; BQ03060.
DR   GeneID; 2867224; -.
DR   KEGG; bqu:BQ03060; -.
DR   PATRIC; 31951821; VBIBarQui58630_0347.
DR   HOGENOM; HOG000293093; -.
DR   KO; K00928; -.
DR   OMA; DEKYTEL; -.
DR   OrthoDB; EOG6NSGHC; -.
DR   BioCyc; BQUI283165:GHZA-306-MONOMER; -.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR005260; Asp_kin_monofn.
DR   InterPro; IPR001341; Asp_kinase_dom.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   InterPro; IPR027795; GATS-like_ACT_dom.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF13840; ACT_7; 1.
DR   PIRSF; PIRSF000726; Asp_kin; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00656; asp_kin_monofn; 1.
DR   TIGRFAMs; TIGR00657; asp_kinases; 1.
DR   PROSITE; PS51671; ACT; 2.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000597};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:CAF25806.1};
KW   Transferase {ECO:0000256|RuleBase:RU003416,
KW   ECO:0000256|RuleBase:RU003448}.
SQ   SEQUENCE   418 AA;  45263 MW;  12627DD76EDF2E03 CRC64;
     MARIVMKFGG TSVANIERIH NVARHIKREV DAGNEVAVVV SAMAGKTNEL VQWTRDASPM
     HKDADEYDVV VASGEQITAG LLALKLQAMG VNARSWLGWQ IPIHTDNVHG SARITDINGS
     FLIQRFQEGQ VAVIAGFQGL APDNRISTLG RGGSDTSAVA IAAAVQADRC DIYTDVDGVY
     TTDPRIEPKA RLLPKVAFEE MLEMASLGAK VLQVRSVELA MVHKVRTFVR SSFEDPDALG
     MDDPINSSGT LICDEDEILE QQNVTGIAFA KDEAQISLRR LADRPGISAA IFGPLAEERI
     NVDMIVQNIS EDGSKTDMTF TVPSVDVEKA VTLLEKNRKE IGFDVLQFER NLAKVSVIGI
     GMRSHAGVAA TAFKALSEKG INIQAITTSE IKISILIDHA YTELAVRTLH ALYGLDKG
//
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