AK2H_ECOLI
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 03-AUG-2022, entry version 184.
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; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-10.
RX PubMed=6298218; DOI=10.1016/s0021-9258(18)32824-2;
RA Zakin M.M., Duchange N., Ferrara P., Cohen G.N.;
RT "Nucleotide sequence of the metL gene of Escherichia coli. Its product, the
RT bifunctional aspartokinase II-homoserine dehydrogenase II, and the
RT bifunctional product of the thrA gene, aspartokinase I-homoserine
RT 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 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 region
RT 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 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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3;
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 -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 1/3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC 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 aspartokinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine
CC dehydrogenase family. {ECO:0000305}.
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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; NP_418375.1; NC_000913.3.
DR RefSeq; WP_000110772.1; NZ_STEB01000037.1.
DR AlphaFoldDB; P00562; -.
DR SMR; P00562; -.
DR BioGRID; 4261101; 419.
DR DIP; DIP-10197N; -.
DR IntAct; P00562; 3.
DR STRING; 511145.b3940; -.
DR jPOST; P00562; -.
DR PaxDb; P00562; -.
DR PRIDE; P00562; -.
DR EnsemblBacteria; AAC76922; AAC76922; b3940.
DR EnsemblBacteria; BAE77370; BAE77370; BAE77370.
DR GeneID; 67417542; -.
DR GeneID; 948433; -.
DR KEGG; ecj:JW3911; -.
DR KEGG; eco:b3940; -.
DR PATRIC; fig|1411691.4.peg.2765; -.
DR EchoBASE; EB0585; -.
DR eggNOG; COG0460; Bacteria.
DR eggNOG; COG0527; Bacteria.
DR HOGENOM; CLU_009116_7_2_6; -.
DR InParanoid; P00562; -.
DR OMA; GAGVCKN; -.
DR PhylomeDB; P00562; -.
DR BioCyc; EcoCyc:ASPKINIIHOMOSERDEHYDROGII-MON; -.
DR BioCyc; MetaCyc:ASPKINIIHOMOSERDEHYDROGII-MON; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR UniPathway; UPA00051; UER00465.
DR PRO; PR:P00562; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004072; F:aspartate kinase activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009090; P:homoserine biosynthetic process; IDA:EcoCyc.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IDA:EcoCyc.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04257; AAK_AK-HSDH; 1.
DR Gene3D; 1.20.120.1320; -; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR041743; AK-HSDH_N.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR042199; AsparK_Bifunc_asparK/hSer_DH.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR InterPro; IPR011147; Bifunc_aspartokin/hSer_DH.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR019811; HDH_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53633; SSF53633; 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; ATP-binding; Direct protein sequencing; Kinase;
KW Methionine biosynthesis; Multifunctional enzyme; NADP; Nucleotide-binding;
KW Oxidoreductase; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6298218"
FT CHAIN 2..810
FT /note="Bifunctional aspartokinase/homoserine dehydrogenase
FT 2"
FT /id="PRO_0000066683"
FT REGION 2..252
FT /note="Aspartokinase"
FT REGION 253..463
FT /note="Interface"
FT REGION 464..810
FT /note="Homoserine dehydrogenase"
FT BINDING 464..471
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT CONFLICT 56
FT /note="Q -> R (in Ref. 1; CAA23585)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="N -> S (in Ref. 1; CAA23585)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="A -> G (in Ref. 1; CAA23585)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="M -> S (in Ref. 1; CAA23585)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="A -> R (in Ref. 1; CAA23585)"
FT /evidence="ECO:0000305"
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
