ID   AK2_BACST               Reviewed;         407 AA.
AC   P53553;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Aspartokinase 2;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartokinase II;
DE   AltName: Full=Aspartate kinase 2;
GN   Name=lysC;
OS   Bacillus stearothermophilus (Geobacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NUB3621;
RX   MEDLINE=96186919; PubMed=8635739; DOI=10.1016/0378-1119(95)00834-9;
RA   Cantoni R., Labo M., de Rossi E., Riccardi G.;
RT   "Sequence of the Bacillus stearothermophilus gene encoding
RT   aspartokinase II.";
RL   Gene 169:135-136(1996).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-
CC       aspartate.
CC   -!- ENZYME REGULATION: Lysine-sensitive (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; tetrahydrodipicolinate from L-aspartate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 1/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 1/5.
CC   -!- SUBUNIT: Tetramer consisting of 2 isoforms Alpha (catalytic) and 2
CC       isoforms Beta (function not known).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Alpha; Synonyms=Aspartokinase 2 subunit alpha;
CC         IsoId=P53553-1; Sequence=Displayed;
CC       Name=Beta; Synonyms=Aspartokinase 2 subunit beta;
CC         IsoId=P53553-2; Sequence=VSP_018654;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC   -!- SIMILARITY: Contains 2 ACT domains.
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DR   EMBL; L46351; AAB06216.1; -; Genomic_DNA.
DR   PIR; JC4640; JC4640.
DR   BRENDA; 2.7.2.4; 266715.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002912; ACT_bd.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR005260; Asp_kin_monofn.
DR   InterPro; IPR001341; Asp_kin_reg.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01842; ACT; 2.
DR   TIGRFAMs; TIGR00656; asp_kin_monofn; 1.
DR   TIGRFAMs; TIGR00657; asp_kinases; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   3: Inferred from homology;
KW   Alternative initiation; Amino-acid biosynthesis; ATP-binding;
KW   Diaminopimelate biosynthesis; Kinase; Lysine biosynthesis;
KW   Nucleotide-binding; Repeat; Transferase.
FT   CHAIN         1    407       Aspartokinase 2.
FT                                /FTId=PRO_0000002371.
FT   DOMAIN      262    335       ACT 1.
FT   DOMAIN      339    404       ACT 2.
FT   VAR_SEQ       1    245       Missing (in isoform Beta).
FT                                /FTId=VSP_018654.
SQ   SEQUENCE   407 AA;  44002 MW;  2A848E6A7037B172 CRC64;
     MGIIVQKFGG TSVGSIERIQ HVANRVIEEV QKGNDVVVVV SAMGKTTDEL VNLAKQISNH
     PSKREMDMLL STGEQVSIAL LAMSLHEKGY KAVSLTGWQA GITTEEMHGN ARIMNIDTTR
     IRRCLDEGAI VIVAGFQGVT ETGEITTLGR GGSDTTAVAL AAALKAEKCD IYTDVTGVFT
     TDPRYVKTAR KIKEISYDEM LELANLGAGV LHPRAVEFAK NYEVPLEVRS SMENERGTMV
     KEEVSMEQHL IVRGIAFEDQ VTRVTVVGIE KYLQSVATIF TALANRGINV DIIIQNATNS
     ETASVSFSIR TEDLPETLQV LQALEGADVH YESGLAKVSI VGSGMISNPG VAARVFEVLA
     DQGIEIKMVS ISEIKISTVI DEKYMVSAVE ELHEAFGLAE EAAAVRS
//