(data stored in SCRATCH zone)

SWISSPROT: A0A0E1NTB7_YERPA

ID   A0A0E1NTB7_YERPA        Unreviewed;       461 AA.
AC   A0A0E1NTB7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 25.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   OrderedLocusNames=YPA_0025 {ECO:0000313|EMBL:ABG11994.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG11994.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG11994.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG11994.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP;
CC         Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
CC         Evidence={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}.
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DR   EMBL; CP000308; ABG11994.1; -; Genomic_DNA.
DR   RefSeq; WP_002212084.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG11994; ABG11994; YPA_0025.
DR   EnsemblBacteria; AJJ79487; AJJ79487; CH58_2859.
DR   KEGG; ypa:YPA_0025; -.
DR   PATRIC; fig|360102.15.peg.3014; -.
DR   KO; K00928; -.
DR   OMA; DFNLRMI; -.
DR   BioCyc; YPES360102:GHZU-31-MONOMER; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   CDD; cd04258; AAK_AKiii-LysC-EC; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR041745; AKiii-LysC-EC.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR005260; Asp_kin_monofn.
DR   InterPro; IPR001341; Asp_kinase.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   Pfam; PF00696; AA_kinase; 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; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1NTB7.
DR   SWISS-2DPAGE; A0A0E1NTB7.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:ABG11994.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Transferase {ECO:0000256|RuleBase:RU003448,
KW   ECO:0000313|EMBL:ABG11994.1}.
FT   NP_BIND      20     23       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   NP_BIND     233    234       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   BINDING      57     57       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING     131    131       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING     239    239       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000726-
FT                                1}.
FT   BINDING     244    244       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
SQ   SEQUENCE   461 AA;  49691 MW;  AE58239B6B05D0E0 CRC64;
     MIQVAPQQTR DAPSATVVAK FGGTSVASFD AMSRSADVVL SNPDVRLVIL SASAGITNLL
     VALADGSEPE KRADHLEDIR HIQYDIIARL TDSTVIREEI DRMLENIAML SEAASLATSP
     ALTDELVSHG ELMSTLLFVE LLRQRQVAVE WFDVRKVMRT NDRFGRAEPD TSALAELAQT
     LLAPRIEDAI VVTQGFIGSE GKGRTTTLGR GGSDYTAALL GEALNVSRID IWTDVPGIYT
     TDPRVVPAAK RIDKIAFEEA AEMATFGAKI LHPATLLPAV RSDIPMFVGS SKDPAAGGTL
     VCNETYNPPL FRALALRRKQ TLLTLHSLNM LHARGFLAEV FNILARHSIS VDLITTSEVS
     VALTLDTTGS TSTGDSLLTT SLLTELSSLC RVEVEEDLAL VAIIGNNLSQ ACGVGKEVFG
     VLDPFNIRMI CYGASSHNLC FLVPGNDADK VVQTLHYNLF E
//

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