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Reviewed, UniProtKB/Swiss-Prot P00561 (AK1H_ECOLI)

Last modified June 16, 2009. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional aspartokinase/homoserine dehydrogenase 1
Alternative name(s):
    Aspartokinase I/homoserine dehydrogenase I
      Short name=AKI-HDI
Including the following 2 domains:
    1- Recommended name:
            Aspartokinase
              EC=2.7.2.4
    2- Recommended name:
            Homoserine dehydrogenase
              EC=1.1.1.3
Gene names
Name: thrA
Synonyms: thrA1, thrA2
Ordered Locus Names: b0002, JW0001
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length820 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Enzyme regulation

The enzyme activities are regulated allosterically by L-threonine.

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; 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 II-homoserine dehydrogenase II 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.

Contains 2 ACT domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 820820Bifunctional aspartokinase/homoserine dehydrogenase 1
PRO_0000066681

Regions

Domain316 – 38469ACT 1
Domain397 – 46872ACT 2
Nucleotide binding471 – 4788NADP Potential
Region1 – 249249Aspartokinase
Region250 – 470221Interface
Region471 – 820350Homoserine dehydrogenase

Experimental info

Sequence conflict111V → L Ref.1
Sequence conflict111V → L Ref.2
Sequence conflict1131Q → E AA sequence Ref.8
Sequence conflict2301D → N Ref.1
Sequence conflict2301D → N Ref.2
Sequence conflict3751Q → L Ref.1
Sequence conflict3751Q → L Ref.2
Sequence conflict3931T → A Ref.1
Sequence conflict3931T → A Ref.2
Sequence conflict4061M → L Ref.1
Sequence conflict4061M → L Ref.2
Sequence conflict5531D → N Ref.1
Sequence conflict5531D → N Ref.2
Sequence conflict587 – 5882DY → IT in AAA24671. Ref.10
Sequence conflict6071T → I Ref.1
Sequence conflict6071T → I Ref.2
Sequence conflict6581T → R Ref.1
Sequence conflict6581T → R Ref.2

Sequences

Sequence LengthMass (Da)Tools
P00561-1 [UniParc].

Last modified August 29, 2003. Version 2.
Checksum: 0BF28E9EECAB10ED

FASTA82089,120
        10         20         30         40         50         60 
MRVLKFGGTS VANAERFLRV ADILESNARQ GQVATVLSAP AKITNHLVAM IEKTISGQDA 

        70         80         90        100        110        120 
LPNISDAERI FAELLTGLAA AQPGFPLAQL KTFVDQEFAQ IKHVLHGISL LGQCPDSINA 

       130        140        150        160        170        180 
ALICRGEKMS IAIMAGVLEA RGHNVTVIDP VEKLLAVGHY LESTVDIAES TRRIAASRIP 

       190        200        210        220        230        240 
ADHMVLMAGF TAGNEKGELV VLGRNGSDYS AAVLAACLRA DCCEIWTDVD GVYTCDPRQV 

       250        260        270        280        290        300 
PDARLLKSMS YQEAMELSYF GAKVLHPRTI TPIAQFQIPC LIKNTGNPQA PGTLIGASRD 

       310        320        330        340        350        360 
EDELPVKGIS NLNNMAMFSV SGPGMKGMVG MAARVFAAMS RARISVVLIT QSSSEYSISF 

       370        380        390        400        410        420 
CVPQSDCVRA ERAMQEEFYL ELKEGLLEPL AVTERLAIIS VVGDGMRTLR GISAKFFAAL 

       430        440        450        460        470        480 
ARANINIVAI AQGSSERSIS VVVNNDDATT GVRVTHQMLF NTDQVIEVFV IGVGGVGGAL 

       490        500        510        520        530        540 
LEQLKRQQSW LKNKHIDLRV CGVANSKALL TNVHGLNLEN WQEELAQAKE PFNLGRLIRL 

       550        560        570        580        590        600 
VKEYHLLNPV IVDCTSSQAV ADQYADFLRE GFHVVTPNKK ANTSSMDYYH QLRYAAEKSR 

       610        620        630        640        650        660 
RKFLYDTNVG AGLPVIENLQ NLLNAGDELM KFSGILSGSL SYIFGKLDEG MSFSEATTLA 

       670        680        690        700        710        720 
REMGYTEPDP RDDLSGMDVA RKLLILARET GRELELADIE IEPVLPAEFN AEGDVAAFMA 

       730        740        750        760        770        780 
NLSQLDDLFA ARVAKARDEG KVLRYVGNID EDGVCRVKIA EVDGNDPLFK VKNGENALAF 

       790        800        810        820 
YSHYYQPLPL VLRGYGAGND VTAAGVFADL LRTLSWKLGV 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the thrA gene of Escherichia coli."
Katinka M., Cossart P., Sibilli L., Saint-Girons I., Chalvignac M.A., le Bras G., Cohen G.N., Yaniv M.
Proc. Natl. Acad. Sci. U.S.A. 77:5730-5733(1980) [PubMed: 7003595] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
Nucleic Acids Res. 20:3305-3308(1992) [PubMed: 1630901] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.
[3]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Initiation, pausing, and termination of transcription in the threonine operon regulatory region of Escherichia coli."
Gardner J.F.
J. Biol. Chem. 257:3896-3904(1982) [PubMed: 6277952] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
[7]"Identification and characterization of mutants affecting transcription termination at the threonine operon attenuator."
Lynn S.P., Bauer C.E., Chapman K.A., Gardner J.F.
J. Mol. Biol. 183:529-541(1985) [PubMed: 2410621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
[8]"The primary structure of Escherichia coli K 12 aspartokinase I-homoserine dehydrogenase I: sequence of cyanogen bromide peptide CB 3."
Sibilli L., le Bras G., Cossart P., Chalvignac M.A., le Bras G., Briley P.A., Cohen G.N.
Biochimie 61:733-739(1979) [PubMed: 387092] [Abstract]
Cited for: PROTEIN SEQUENCE OF 51-129.
[9]"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: 6298218] [Abstract]
Cited for: SEQUENCE REVISION TO 11.
[10]"Construction and expression of a hybrid plasmid containing the Escherichia coli thrA and thrB genes."
Cossart P., Katinka M., Yaniv M.
Mol. Gen. Genet. 175:39-44(1979) [PubMed: 390305] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 553-588.

Cross-references

Sequence databases

V00361 Genomic DNA. Translation: CAA23660.1.
J01706 Genomic DNA. Translation: AAA83914.1.
U14003 Genomic DNA. Translation: AAA97301.1.
U00096 Genomic DNA. Translation: AAC73113.1.
AP009048 Genomic DNA. Translation: BAB96579.2.
V00360 Genomic DNA. Translation: CAA23659.1.
X68872 Genomic DNA. Translation: CAA48734.1.
M28570 Genomic DNA. Translation: AAA24673.1.
M10644 Genomic DNA. Translation: AAA24671.1.
PIRDEECK. B64720.
RefSeqAP_000666.1.
NP_414543.1.

3D structure databases

HSSPHSSP built from PDB template 1EBF based on UniProtKB P31116.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2907N.

Genome annotation databases

GeneID945803.
GenomeReviewsGene locus JW0001 in contig AP009048_GR.
Gene locus b0002 in contig U00096_GR.
KEGGecj:JW0001.
eco:b0002.

Organism-specific databases

EchoBASEEB0991.
EcoGeneEG10998. thrA.
CMRSearch...

Phylogenomic databases

HOGENOMP00561.
OMAP00561. MFNVSGP.

Enzyme and pathway databases

BioCycEcoCyc:ASPKINIHOMOSERDEHYDROGI-MON.
MetaCyc:ASPKINIHOMOSERDEHYDROGI-MON.

Family and domain databases

InterProIPR002912. ACT_bd.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR005106. Asp/hSer_DH_NAD-bd.
IPR001341. Asp_kin_reg.
IPR018042. Aspartate_kinase_CS.
IPR011147. bifunc_aspartokin/hSer_DH.
IPR001342. Homoserine_dehydrogenase_cat.
IPR019811. Homoserine_dehydrogenase_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.1160.10. Aa_kinase. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00696. AA_kinase. 1 hit.
PF01842. ACT. 2 hits.
PF00742. Homoserine_dh. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF000727. ThrA. 1 hit.
TIGRFAMsTIGR00657. asp_kinases. 1 hit.
PROSITEPS00324. ASPARTOKINASE. 1 hit.
PS01042. HOMOSER_DHGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAK1H_ECOLI
AccessionPrimary (citable) accession number: P00561
Secondary accession number(s): Q47659, Q6LEL0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 29, 2003
Last modified: June 16, 2009
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents