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Database: UniProt
Entry: A0A0C4YDD1_9BURK
LinkDB: A0A0C4YDD1_9BURK
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ID   A0A0C4YDD1_9BURK        Unreviewed;       416 AA.
AC   A0A0C4YDD1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   08-MAY-2019, entry version 20.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=RR42_m1315 {ECO:0000313|EMBL:AJG18721.1};
OS   Cupriavidus basilensis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG18721.1, ECO:0000313|Proteomes:UP000031843};
RN   [1] {ECO:0000313|EMBL:AJG18721.1, ECO:0000313|Proteomes:UP000031843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4G11 {ECO:0000313|EMBL:AJG18721.1};
RX   PubMed=25977418;
RA   Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA   Chakraborty R., Arkin A.P., Deutschbauer A.;
RT   "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated
RT   from the Oak Ridge Field Research Center Site.";
RL   Genome Announc. 3:0-0(2015).
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; CP010536; AJG18721.1; -; Genomic_DNA.
DR   RefSeq; WP_043344971.1; NZ_CP010536.1.
DR   EnsemblBacteria; AJG18721; AJG18721; RR42_m1315.
DR   KEGG; cbw:RR42_m1315; -.
DR   KO; K00928; -.
DR   OrthoDB; 1067792at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000031843; Chromosome main.
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; cd04261; AAK_AKii-LysC-BS; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR041740; AKii-LysC-BS.
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   InterPro; IPR027795; CASTOR_ACT_dom.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01842; ACT; 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;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031843};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:AJG18721.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031843};
KW   Transferase {ECO:0000256|RuleBase:RU003448,
KW   ECO:0000313|EMBL:AJG18721.1}.
FT   DOMAIN      274    349       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      355    416       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       7     10       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   NP_BIND     173    174       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   NP_BIND     209    210       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   BINDING      47     47       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING      74     74       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING     179    179       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000726-
FT                                1}.
FT   BINDING     184    184       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
SQ   SEQUENCE   416 AA;  44784 MW;  878F4A471E230005 CRC64;
     MALIVHKYGG TSMGSPERIK NVAKRVAKWH RAGHRVVVVP SAMSGETNRL LGLAKEISAQ
     PSPRELDMLA ATGEQASSAL LAIALQSEGV DAISYTGWQV PVKTDSSHTK ARIESIDDER
     ILADLDAGRV VVVTGFQGID DNGNITTLGR GGSDTSAVAI AAAIEAEECL IYTDVDGVYT
     TDPRVVEDAR RLDQITFEEM LEMASLGSKV LQIRSVEFAG KYRVKTRVLS SLTDPLMPLE
     QEMHSGTLIT FEENSEMEAA VISGIAFARD EAKITVLGVP DKPGIAYQIL GPVADANIDV
     DMIIQNQSVD GKTDFTFTVP RGEYQRALAI LNDSVKAHIG AASVSGDPKV SKVSVVGVGM
     RSHVGIASKM FRTLSEEGIN IQMISTSEIK ISVLIDEKYM ELAVRALHKV FELDQA
//
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