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Database: UniProt
Entry: A0A0D6ZA17_9BACI
LinkDB: A0A0D6ZA17_9BACI
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ID   A0A0D6ZA17_9BACI        Unreviewed;       410 AA.
AC   A0A0D6ZA17;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 22.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=UB32_09025 {ECO:0000313|EMBL:KIY22347.1};
OS   Bacillus subterraneus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=285983 {ECO:0000313|EMBL:KIY22347.1, ECO:0000313|Proteomes:UP000032512};
RN   [1] {ECO:0000313|EMBL:KIY22347.1, ECO:0000313|Proteomes:UP000032512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MITOT1 {ECO:0000313|EMBL:KIY22347.1,
RC   ECO:0000313|Proteomes:UP000032512};
RA   Peet K.C., Thompson J.R.;
RT   "Draft genome sequences of the supercritical CO2 tolerant bacteria
RT   Bacillus subterraneus MITOT1 and Bacillus cereus MIT0214.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KIY22347.1}.
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DR   EMBL; JXIQ01000072; KIY22347.1; -; Genomic_DNA.
DR   RefSeq; WP_044393065.1; NZ_JXIQ01000072.1.
DR   EnsemblBacteria; KIY22347; KIY22347; UB32_09025.
DR   PATRIC; fig|285983.3.peg.326; -.
DR   OrthoDB; 1067792at2; -.
DR   BioCyc; GCF_000934845:G1EKL-305-MONOMER; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000032512; Unassembled WGS sequence.
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:UP000032512};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:KIY22347.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032512};
KW   Transferase {ECO:0000256|RuleBase:RU003448,
KW   ECO:0000313|EMBL:KIY22347.1}.
FT   DOMAIN      264    338       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      344    410       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   BINDING      47     47       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING      74     74       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING     184    184       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
SQ   SEQUENCE   410 AA;  43837 MW;  09DECBC16A158968 CRC64;
     MGLIVQKFGG TSVGSVEKIR NAASRTAEEW KNGNQVVVVV SAMGKTTDHL VDMANEISEA
     PSKREMDMLL TTGEQITIAL YAMALAQNGI EAISFTGWQA GVKTEAIHGN ARIIDIETDR
     ISKELSAGKV VIVAGFQGVT ADGDITTLGR GGSDTTAVAL AAALKADKCD IYTDVTGVFT
     TDPRIVKSAR KLLNVSYDEM LELANLGAGV LHPRAVEFAK NYGLRLEVRS SMEKESGTII
     EEENEMEQNL IVRGVAFEDQ ITRVSVLGVS TSLKGLSTIF STLAQNHINV DIIVQSRTEA
     GAANISFSIK STNLPETLDV LESNKESLNY QSIESETGLA KVSIVGSGMV SNPGVAAKMF
     EVLEENGIQV KMVSTSEIKV STVVPEKQMV NAVESLHEAF ELFSGTVKTN
//
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