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P00562 (AK2H_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional aspartokinase/homoserine dehydrogenase 2
Alternative name(s):
Aspartokinase II/homoserine dehydrogenase II
Short name=AKII-HDII

Including the following 2 domains:

  1. Aspartokinase
    EC=2.7.2.4
  2. Homoserine dehydrogenase
    EC=1.1.1.3
Gene names
Name:metL
Synonyms:metM
Ordered Locus Names:b3940, JW3911
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H.

ATP + L-aspartate = ADP + 4-phospho-L-aspartate.

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.

Subunit structure

Homotetramer.

Miscellaneous

Aspartokinase I-homoserine dehydrogenase I and aspartokinase III also catalyze the same reaction(s).

Sequence similarities

In the N-terminal section; belongs to the aspartokinase family.

In the C-terminal section; belongs to the homoserine dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 810809Bifunctional aspartokinase/homoserine dehydrogenase 2
PRO_0000066683

Regions

Nucleotide binding464 – 4718NADP Potential
Region2 – 252251Aspartokinase
Region253 – 463211Interface
Region464 – 810347Homoserine dehydrogenase

Experimental info

Sequence conflict561Q → R in CAA23585. Ref.1
Sequence conflict591N → S in CAA23585. Ref.1
Sequence conflict3331A → G in CAA23585. Ref.1
Sequence conflict6741M → S in CAA23585. Ref.1
Sequence conflict7621A → R in CAA23585. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P00562 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BD2515E3554F9B44

FASTA81088,888
        10         20         30         40         50         60 
MSVIAQAGAK GRQLHKFGGS SLADVKCYLR VAGIMAEYSQ PDDMMVVSAA GSTTNQLINW 

        70         80         90        100        110        120 
LKLSQTDRLS AHQVQQTLRR YQCDLISGLL PAEEADSLIS AFVSDLERLA ALLDSGINDA 

       130        140        150        160        170        180 
VYAEVVGHGE VWSARLMSAV LNQQGLPAAW LDAREFLRAE RAAQPQVDEG LSYPLLQQLL 

       190        200        210        220        230        240 
VQHPGKRLVV TGFISRNNAG ETVLLGRNGS DYSATQIGAL AGVSRVTIWS DVAGVYSADP 

       250        260        270        280        290        300 
RKVKDACLLP LLRLDEASEL ARLAAPVLHA RTLQPVSGSE IDLQLRCSYT PDQGSTRIER 

       310        320        330        340        350        360 
VLASGTGARI VTSHDDVCLI EFQVPASQDF KLAHKEIDQI LKRAQVRPLA VGVHNDRQLL 

       370        380        390        400        410        420 
QFCYTSEVAD SALKILDEAG LPGELRLRQG LALVAMVGAG VTRNPLHCHR FWQQLKGQPV 

       430        440        450        460        470        480 
EFTWQSDDGI SLVAVLRTGP TESLIQGLHQ SVFRAEKRIG LVLFGKGNIG SRWLELFARE 

       490        500        510        520        530        540 
QSTLSARTGF EFVLAGVVDS RRSLLSYDGL DASRALAFFN DEAVEQDEES LFLWMRAHPY 

       550        560        570        580        590        600 
DDLVVLDVTA SQQLADQYLD FASHGFHVIS ANKLAGASDS NKYRQIHDAF EKTGRHWLYN 

       610        620        630        640        650        660 
ATVGAGLPIN HTVRDLIDSG DTILSISGIF SGTLSWLFLQ FDGSVPFTEL VDQAWQQGLT 

       670        680        690        700        710        720 
EPDPRDDLSG KDVMRKLVIL AREAGYNIEP DQVRVESLVP AHCEGGSIDH FFENGDELNE 

       730        740        750        760        770        780 
QMVQRLEAAR EMGLVLRYVA RFDANGKARV GVEAVREDHP LASLLPCDNV FAIESRWYRD 

       790        800        810 
NPLVIRGPGA GRDVTAGAIQ SDINRLAQLL 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the metL gene of Escherichia coli. Its product, the bifunctional aspartokinase II-homoserine dehydrogenase II, and the bifunctional product of the thrA gene, aspartokinase I-homoserine dehydrogenase I, derive from a common ancestor."
Zakin M.M., Duchange N., Ferrara P., Cohen G.N.
J. Biol. Chem. 258:3028-3031(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-10.
[2]"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00305 Genomic DNA. Translation: CAA23585.1.
L19201 Genomic DNA. Translation: AAB03072.1.
U00096 Genomic DNA. Translation: AAC76922.1.
AP009048 Genomic DNA. Translation: BAE77370.1.
PIRDEECK2. S40883.
RefSeqNP_418375.1. NC_000913.3.
YP_491511.1. NC_007779.1.

3D structure databases

ProteinModelPortalP00562.
SMRP00562. Positions 16-810.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10197N.
IntActP00562. 3 interactions.
STRING511145.b3940.

Proteomic databases

PaxDbP00562.
PRIDEP00562.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76922; AAC76922; b3940.
BAE77370; BAE77370; BAE77370.
GeneID12932107.
948433.
KEGGecj:Y75_p3247.
eco:b3940.
PATRIC32123399. VBIEscCol129921_4060.

Organism-specific databases

EchoBASEEB0585.
EcoGeneEG10590. metL.

Phylogenomic databases

eggNOGCOG0527.
HOGENOMHOG000271594.
KOK12525.
OMATLQYPEF.
OrthoDBEOG6M0T34.
PhylomeDBP00562.
ProtClustDBPRK09466.

Enzyme and pathway databases

BioCycEcoCyc:ASPKINIIHOMOSERDEHYDROGII-MONOMER.
ECOL316407:JW3911-MONOMER.
MetaCyc:ASPKINIIHOMOSERDEHYDROGII-MONOMER.
UniPathwayUPA00034; UER00015.
UPA00050; UER00063.
UPA00050; UER00461.
UPA00051; UER00462.
UPA00051; UER00465.

Gene expression databases

GenevestigatorP00562.

Family and domain databases

Gene3D3.40.1160.10. 2 hits.
3.40.50.720. 1 hit.
InterProIPR001048. Asp/Glu/Uridylate_kinase.
IPR005106. Asp/hSer_DH_NAD-bd.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
IPR011147. Bifunc_aspartokin/hSer_DH.
IPR001342. HDH_cat.
IPR019811. HDH_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
PF00742. Homoserine_dh. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF000727. ThrA. 1 hit.
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR00657. asp_kinases. 1 hit.
PROSITEPS00324. ASPARTOKINASE. 1 hit.
PS01042. HOMOSER_DHGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP00562.

Entry information

Entry nameAK2H_ECOLI
AccessionPrimary (citable) accession number: P00562
Secondary accession number(s): P77856, Q2M8N6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene