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UniProtKB/Swiss-Prot entry P00561


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AK1H_ECOLI
Primary accession number P00561
Secondary accession numbers Q47659 Q6LEL0
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on August 29, 2003 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 98)
Name and origin of the protein
Protein name Bifunctional aspartokinase/homoserine dehydrogenase 1
Synonyms Aspartokinase I/homoserine dehydrogenase I
AKI-HDI
Includes Aspartokinase
     (EC 2.7.2.4)
Homoserine dehydrogenase
     (EC 1.1.1.3)
Gene name
Name: thrA
Synonyms: thrA1, thrA2
OrderedLocusNames: b0002, JW0001
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7003595 [NCBI, ExPASy, EBI, Israel, Japan]
Katinka M., Cossart P., Sibilli L., Saint-Girons I., Chalvignac M.A., le Bras G., Cohen G.N., Yaniv M.;
"Nucleotide sequence of the thrA gene of Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 77:5730-5733(1980).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12;
DOI=10.1093/nar/20.13.3305; PubMed=1630901 [NCBI, ExPASy, EBI, Israel, Japan]
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region.";
Nucleic Acids Res. 20:3305-3308(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/23.12.2105; PubMed=7610040 [NCBI, ExPASy, EBI, Israel, Japan]
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes.";
Nucleic Acids Res. 23:2105-2119(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
PubMed=6277952 [NCBI, ExPASy, EBI, Israel, Japan]
Gardner J.F.;
"Initiation, pausing, and termination of transcription in the threonine operon regulatory region of Escherichia coli.";
J. Biol. Chem. 257:3896-3904(1982).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
DOI=10.1016/0022-2836(85)90169-X; PubMed=2410621 [NCBI, ExPASy, EBI, Israel, Japan]
Lynn S.P., Bauer C.E., Chapman K.A., Gardner J.F.;
"Identification and characterization of mutants affecting transcription termination at the threonine operon attenuator.";
J. Mol. Biol. 183:529-541(1985).
[8]
PROTEIN SEQUENCE OF 51-129.
PubMed=387092 [NCBI, ExPASy, EBI, Israel, Japan]
Sibilli L., le Bras G., Cossart P., Chalvignac M.A., le Bras G., Briley P.A., Cohen G.N.;
"The primary structure of Escherichia coli K 12 aspartokinase I-homoserine dehydrogenase I: sequence of cyanogen bromide peptide CB 3.";
Biochimie 61:733-739(1979).
[9]
SEQUENCE REVISION TO 11.
PubMed=6298218 [NCBI, ExPASy, EBI, Israel, Japan]
Zakin M.M., Duchange N., Ferrara P., Cohen G.N.;
"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.";
J. Biol. Chem. 258:3028-3031(1983).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 553-588.
DOI=10.1007/BF00267853; PubMed=390305 [NCBI, ExPASy, EBI, Israel, Japan]
Cossart P., Katinka M., Yaniv M.;
"Construction and expression of a hybrid plasmid containing the Escherichia coli thrA and thrB genes.";
Mol. Gen. Genet. 175:39-44(1979).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
V00361; CAA23660.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J01706; AAA83914.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14003; AAA97301.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73113.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAB96579.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V00360; CAA23659.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X68872; CAA48734.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M28570; AAA24673.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M10644; AAA24671.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B64720; DEECK.
RefSeq AP_000666.1; -.
NP_414543.1; -.
3D structure databases
HSSP P31116; 1EBF. [HSSP ENTRY / PDB]
ModBase P00561.
Protein-protein interaction databases
DIP DIP:2907N; -.
IntAct P00561; -.
Enzyme and pathway databases
BioCyc EcoCyc:ASPKINIHOMOSERDEHYDROGI-MON; -.
Organism-specific databases
EchoBASE EB0991; -.
EcoGene EG10998; thrA.
Family and domain databases
InterPro IPR002912; ACT_bd.
IPR001048; Asp/Glu/Uridylate_kinase.
IPR005106; Asp/hSer_DHase_NAD-bd.
IPR001341; Asp_kin_reg.
IPR011147; bifunc_aspartokin/hSer_DHase.
IPR001342; hSer_DHase_cat.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.1160.10; Aa_kinase; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00696; AA_kinase; 1.
PF01842; ACT; 2.
PF00742; Homoserine_dh; 1.
PF03447; NAD_binding_3; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000727; ThrA; 1.
TIGRFAMs TIGR00657; asp_kinases; 1.
PROSITE PS00324; ASPARTOKINASE; 1.
PS01042; HOMOSER_DHGENASE; 1.
BLOCKS P00561.
Genome annotation databases
GeneID 945803; -.
GenomeReviews U00096_GR; b0002.
AP009048_GR; JW0001.
KEGG ecj:JW0001; -.
eco:b0002; -.
Phylogenomic databases
HOGENOM P00561; -.
Genome annotation databases
CMR P00561; b0002.
Other
ProtoNet P00561.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Allosteric enzyme; Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; Kinase; Multifunctional enzyme; NADP; Oxidoreductase; Repeat; Threonine biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   820  820     Bifunctional aspartokinase/homoserine dehydrogenase 1. PRO_0000066681
DOMAIN   316   384  69     ACT 1. 
DOMAIN   397   468  72     ACT 2. 
NP_BIND   471   478  8     NADP (Potential). 
REGION   1   249  249     Aspartokinase. 
REGION   250   470  221     Interface. 
REGION   471   820  350     Homoserine dehydrogenase. 
CONFLICT   11    11        V -> L (in Ref. 1 and 2). 
CONFLICT   113   113        Q -> E (in Ref. 8; AA sequence). 
CONFLICT   230   230        D -> N (in Ref. 1 and 2). 
CONFLICT   375   375        Q -> L (in Ref. 1 and 2). 
CONFLICT   393   393        T -> A (in Ref. 1 and 2). 
CONFLICT   406   406        M -> L (in Ref. 1 and 2). 
CONFLICT   553   553        D -> N (in Ref. 1 and 2). 
CONFLICT   587   588        DY -> IT (in Ref. 10; AAA24671). 
CONFLICT   607   607        T -> I (in Ref. 1 and 2). 
CONFLICT   658   658        T -> R (in Ref. 1 and 2). 
Sequence information
Length: 820 AA [This is the length of the unprocessed precursor] Molecular weight: 89120 Da [This is the MW of the unprocessed precursor] CRC64: 0BF28E9EECAB10ED [This is a checksum on the sequence]
        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 

P00561 in FASTA format

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