ID AK2H_ECOLI Reviewed; 810 AA. AC P00562; P77856; Q2M8N6; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 04-NOV-2008, entry version 90. DE RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase 2; DE AltName: Full=Aspartokinase II/homoserine dehydrogenase II; DE Short=AKII-HDII; DE Includes: DE RecName: Full=Aspartokinase; DE EC=2.7.2.4; DE Includes: DE RecName: Full=Homoserine dehydrogenase; DE EC=1.1.1.3; GN Name=metL; Synonyms=metM; OrderedLocusNames=b3940, JW3911; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-10. RX MEDLINE=83135751; PubMed=6298218; RA Zakin M.M., Duchange N., Ferrara P., Cohen G.N.; RT "Nucleotide sequence of the metL gene of Escherichia coli. Its RT product, the bifunctional aspartokinase II-homoserine dehydrogenase RT II, and the bifunctional product of the thrA gene, aspartokinase I- RT homoserine dehydrogenase I, derive from a common ancestor."; RL J. Biol. Chem. 258:3028-3031(1983). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=93347969; PubMed=8346018; DOI=10.1093/nar/21.15.3391; RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.; RT "Analysis of the Escherichia coli genome. III. DNA sequence of the RT region from 87.2 to 89.2 minutes."; RL Nucleic Acids Res. 21:3391-3398(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). CC -!- CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4- CC semialdehyde + NAD(P)H. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L- CC aspartate. 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-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 3/3. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 1/5. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 3/5. CC -!- SUBUNIT: Homotetramer. CC -!- MISCELLANEOUS: Aspartokinase I-homoserine dehydrogenase I and CC aspartokinase III also catalyze the same reaction(s). CC -!- SIMILARITY: In the N-terminal section; belongs to the CC aspartokinase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine CC dehydrogenase family. 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; V00305; CAA23585.1; -; Genomic_DNA. DR EMBL; L19201; AAB03072.1; -; Genomic_DNA. DR EMBL; U00096; AAC76922.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77370.1; -; Genomic_DNA. DR PIR; S40883; DEECK2. DR RefSeq; AP_003869.1; -. DR RefSeq; NP_418375.1; -. DR HSSP; P31116; 1EBF. DR GeneID; 948433; -. DR GenomeReviews; U00096_GR; b3940. DR GenomeReviews; AP009048_GR; JW3911. DR KEGG; ecj:JW3911; -. DR KEGG; eco:b3940; -. DR EchoBASE; EB0585; -. DR EcoGene; EG10590; metL. DR HOGENOM; P00562; -. DR BioCyc; EcoCyc:ASPKINIIHOMOSERDEHYDROGII-MON; -. DR BioCyc; MetaCyc:ASPKINIIHOMOSERDEHYDROGII-MON; -. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005106; Asp/hSer_DHase_NAD-bd. DR InterPro; IPR001341; Asp_kin_reg. DR InterPro; IPR011147; bifunc_aspartokin/hSer_DHase. DR InterPro; IPR001342; hSer_DHase_cat. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF00742; Homoserine_dh; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR PIRSF; PIRSF000727; ThrA; 1. DR TIGRFAMs; TIGR00657; asp_kinases; 1. DR PROSITE; PS00324; ASPARTOKINASE; 1. DR PROSITE; PS01042; HOMOSER_DHGENASE; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; KW Kinase; Methionine biosynthesis; Multifunctional enzyme; NADP; KW Oxidoreductase; Transferase. FT INIT_MET 1 1 Removed. FT CHAIN 2 810 Bifunctional aspartokinase/homoserine FT dehydrogenase 2. FT /FTId=PRO_0000066683. FT NP_BIND 464 471 NADP (Potential). FT REGION 2 252 Aspartokinase. FT REGION 253 463 Interface. FT REGION 464 810 Homoserine dehydrogenase. FT CONFLICT 56 56 Q -> R (in Ref. 1; CAA23585). FT CONFLICT 59 59 N -> S (in Ref. 1; CAA23585). FT CONFLICT 333 333 A -> G (in Ref. 1; CAA23585). FT CONFLICT 674 674 M -> S (in Ref. 1; CAA23585). FT CONFLICT 762 762 A -> R (in Ref. 1; CAA23585). SQ SEQUENCE 810 AA; 88888 MW; BD2515E3554F9B44 CRC64; MSVIAQAGAK GRQLHKFGGS SLADVKCYLR VAGIMAEYSQ PDDMMVVSAA GSTTNQLINW LKLSQTDRLS AHQVQQTLRR YQCDLISGLL PAEEADSLIS AFVSDLERLA ALLDSGINDA VYAEVVGHGE VWSARLMSAV LNQQGLPAAW LDAREFLRAE RAAQPQVDEG LSYPLLQQLL VQHPGKRLVV TGFISRNNAG ETVLLGRNGS DYSATQIGAL AGVSRVTIWS DVAGVYSADP RKVKDACLLP LLRLDEASEL ARLAAPVLHA RTLQPVSGSE IDLQLRCSYT PDQGSTRIER VLASGTGARI VTSHDDVCLI EFQVPASQDF KLAHKEIDQI LKRAQVRPLA VGVHNDRQLL QFCYTSEVAD SALKILDEAG LPGELRLRQG LALVAMVGAG VTRNPLHCHR FWQQLKGQPV EFTWQSDDGI SLVAVLRTGP TESLIQGLHQ SVFRAEKRIG LVLFGKGNIG SRWLELFARE QSTLSARTGF EFVLAGVVDS RRSLLSYDGL DASRALAFFN DEAVEQDEES LFLWMRAHPY DDLVVLDVTA SQQLADQYLD FASHGFHVIS ANKLAGASDS NKYRQIHDAF EKTGRHWLYN ATVGAGLPIN HTVRDLIDSG DTILSISGIF SGTLSWLFLQ FDGSVPFTEL VDQAWQQGLT EPDPRDDLSG KDVMRKLVIL AREAGYNIEP DQVRVESLVP AHCEGGSIDH FFENGDELNE QMVQRLEAAR EMGLVLRYVA RFDANGKARV GVEAVREDHP LASLLPCDNV FAIESRWYRD NPLVIRGPGA GRDVTAGAIQ SDINRLAQLL //