(data stored in SCRATCH zone)

SWISSPROT: Q3ILF2_PSEHT

ID   Q3ILF2_PSEHT            Unreviewed;       405 AA.
AC   Q3ILF2;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 87.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   Name=lysC {ECO:0000313|EMBL:CAI85622.1};
GN   OrderedLocusNames=PSHAa0533 {ECO:0000313|EMBL:CAI85622.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85622.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85622.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-
CC       aspartate. {ECO:0000256|RuleBase:RU003448}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC       {ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 1/3.
CC       {ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 1/5.
CC       {ECO:0000256|RuleBase:RU004249}.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC       {ECO:0000256|RuleBase:RU003448}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CR954246; CAI85622.1; -; Genomic_DNA.
DR   RefSeq; WP_011327235.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILF2; -.
DR   STRING; 326442.PSHAa0533; -.
DR   EnsemblBacteria; CAI85622; CAI85622; PSHAa0533.
DR   KEGG; pha:PSHAa0533; -.
DR   PATRIC; fig|326442.8.peg.502; -.
DR   eggNOG; ENOG4105CFH; Bacteria.
DR   eggNOG; COG0527; LUCA.
DR   HOGENOM; HOG000293093; -.
DR   KO; K00928; -.
DR   OMA; INIMMIS; -.
DR   OrthoDB; POG091H0223; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
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; PF13840; ACT_7; 1.
DR   PIRSF; PIRSF000726; Asp_kin; 2.
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;
DR   PRODOM; Q3ILF2.
DR   SWISS-2DPAGE; Q3ILF2.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:CAI85622.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Transferase {ECO:0000256|RuleBase:RU003448,
KW   ECO:0000313|EMBL:CAI85622.1}.
FT   DOMAIN      264    338       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      344    405       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   405 AA;  43783 MW;  CC057C6A704E9476 CRC64;
     MALIVQKFGG TSVGSIERIE AVADLVVKTK QQGHQVVVVL SAMSGETNRL INLAKQIDTR
     PSSRELDVLI STGEQVSVAL LAMAIIKRGH SAVSLLADQV NILTDNMFGK ARITDVAATR
     LKHELEHNRI AIIAGFQGRD IEGNVTTLGR GGTDTSAVEI AGAIKADECQ IYTDVNGVYT
     TDPRVEPNAR RMSQVTFAEM LELASLGAKV LHIRSVEAAG KHNVPLRVLS SFYPDAGTLI
     SFEESDMPGN VVSGIAFNRD ECLINVEGVL SGTQYLAKIL KLFADNGIEI DMINQVNHNV
     DKVDYAFTVH TNDYLHALDV LTEQQAQLTA QNIFGLTTVA KVSAVGMGMK SHSGVASLFF
     DALAAENINV ILVSTSEIKI SVLIDEKYLE LAVRALHKIF LTENE
//

If you have problems or comments...

PBIL Back to PBIL home page