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Database: UniProt/TrEMBL
Entry: C0Q9T4_DESAH
LinkDB: C0Q9T4_DESAH
Original site: C0Q9T4_DESAH 
ID   C0Q9T4_DESAH            Unreviewed;       408 AA.
AC   C0Q9T4;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   22-JAN-2014, entry version 37.
DE   RecName: Full=Aspartokinase;
DE            EC=2.7.2.4;
GN   Name=lysC; OrderedLocusNames=HRM2_35870;
OS   Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfobacterium.
OX   NCBI_TaxID=177437;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / HRM2;
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J.,
RA   Andres S., Henne A., Fricke W.F., Martinez-Arias R., Bartels D.,
RA   Goesmann A., Krause L., Puehler A., Klenk H.P., Richter M.,
RA   Schuler M., Gloeckner F.O., Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine
RT   sulfate reducer oxidizing organic carbon completely to carbon
RT   dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-
CC       aspartate.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
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DR   EMBL; CP001087; ACN16652.1; -; Genomic_DNA.
DR   RefSeq; YP_002604816.1; NC_012108.1.
DR   ProteinModelPortal; C0Q9T4; -.
DR   STRING; 177437.HRM2_35870; -.
DR   EnsemblBacteria; ACN16652; ACN16652; HRM2_35870.
DR   GeneID; 7501877; -.
DR   KEGG; dat:HRM2_35870; -.
DR   PATRIC; 21686911; VBIDesAut25181_3691.
DR   eggNOG; COG0527; -.
DR   HOGENOM; HOG000293093; -.
DR   KO; K00928; -.
DR   OMA; INIMMIS; -.
DR   OrthoDB; EOG6NSGHC; -.
DR   ProtClustDB; CLSK2401972; -.
DR   BioCyc; DAUT177437:GHLR-3585-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; Kinase; Transferase.
SQ   SEQUENCE   408 AA;  43727 MW;  7AD973D3074502B1 CRC64;
     MALKVQKFGG TSVADIERIR NVAQRVARAY DKGDQLVVVL SAMSGMTDKL IALAEEASEI
     PDKRELDVLL ATGEQTTAAL LAMMLKSMGY KSKSLLGFQA GIKTDKSAGR ARILDIEAKR
     IKALLDNGHI VVVAGFQGSD TNGDITTLGR GGSDTSAVAI ASALKADVCE IYTDVDGVYT
     TDPRICAKAR KINIISYEEM LEMAVLGAKV LQIRSVEFAK KYNVPVHVRS SFSEEEGTMV
     VNESSDMESV VVSGITCDMN ETRITLKKVP DQPGISAKIF SPLAEAEIMV DMIIQNTRSG
     GETDVTFTVP TVDFKRAKEI SEQVGNKIGA KEVLTAEDIA KVSVIGLGMK SHSGVAATMF
     SALAAENINI RLIATSEIRI SCVIKAKYAE LAVRVLHTAF GLDNPTQS
//
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