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Bifunctional aspartokinase/homoserine dehydrogenase 1 (Aspartokinase I/homoserine dehydrogenase I) (AKI-HDI) [Includes: Aspartokinase (EC 2.7.2.4); Homoserine dehydrogenase (EC 1.1.1.3)]

 AK1H_ECOLI              Reviewed;         820 AA.
P00561; Q47659; Q6LEL0;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
29-AUG-2003, sequence version 2.
12-SEP-2018, entry version 183.
RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase 1;
AltName: Full=Aspartokinase I/homoserine dehydrogenase I;
Short=AKI-HDI;
Includes:
RecName: Full=Aspartokinase;
EC=2.7.2.4;
Includes:
RecName: Full=Homoserine dehydrogenase;
EC=1.1.1.3;
Name=thrA; Synonyms=thrA1, thrA2; OrderedLocusNames=b0002, JW0001;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7003595; DOI=10.1073/pnas.77.10.5730;
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;
PubMed=1630901; DOI=10.1093/nar/20.13.3305;
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;
PubMed=7610040; DOI=10.1093/nar/23.12.2105;
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;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
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;
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.
PubMed=2410621; DOI=10.1016/0022-2836(85)90169-X;
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; DOI=10.1016/S0300-9084(79)80174-1;
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;
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.
PubMed=390305; DOI=10.1007/BF00267853;
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).
-!- CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4-
semialdehyde + NAD(P)H.
-!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-
aspartate.
-!- ACTIVITY REGULATION: The enzyme activities are regulated
allosterically by L-threonine.
-!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
-!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
novo pathway; L-homoserine from L-aspartate: step 1/3.
-!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
novo pathway; L-homoserine from L-aspartate: step 3/3.
-!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
threonine from L-aspartate: step 1/5.
-!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
threonine from L-aspartate: step 3/5.
-!- SUBUNIT: Homotetramer.
-!- MISCELLANEOUS: Aspartokinase II-homoserine dehydrogenase II and
aspartokinase III also catalyze the same reaction(s).
-!- SIMILARITY: In the N-terminal section; belongs to the
aspartokinase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the homoserine
dehydrogenase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; V00361; CAA23660.1; -; Genomic_DNA.
EMBL; J01706; AAA83914.1; -; Genomic_DNA.
EMBL; U14003; AAA97301.1; -; Genomic_DNA.
EMBL; U00096; AAC73113.1; -; Genomic_DNA.
EMBL; AP009048; BAB96579.2; -; Genomic_DNA.
EMBL; V00360; CAA23659.1; -; Genomic_DNA.
EMBL; X68872; CAA48734.1; -; Genomic_DNA.
EMBL; M28570; AAA24673.1; -; Genomic_DNA.
EMBL; M10644; AAA24671.1; -; Genomic_DNA.
PIR; B64720; DEECK.
RefSeq; NP_414543.1; NC_000913.3.
RefSeq; WP_001264707.1; NZ_LN832404.1.
ProteinModelPortal; P00561; -.
SMR; P00561; -.
BioGrid; 4261933; 242.
DIP; DIP-2907N; -.
IntAct; P00561; 7.
STRING; 316385.ECDH10B_0002; -.
BindingDB; P00561; -.
EPD; P00561; -.
PaxDb; P00561; -.
PRIDE; P00561; -.
EnsemblBacteria; AAC73113; AAC73113; b0002.
EnsemblBacteria; BAB96579; BAB96579; BAB96579.
GeneID; 945803; -.
KEGG; ecj:JW0001; -.
KEGG; eco:b0002; -.
PATRIC; fig|1411691.4.peg.2281; -.
EchoBASE; EB0991; -.
EcoGene; EG10998; thrA.
eggNOG; ENOG4105CFH; Bacteria.
eggNOG; COG0460; LUCA.
eggNOG; COG0527; LUCA.
HOGENOM; HOG000271593; -.
InParanoid; P00561; -.
KO; K12524; -.
OMA; CNKIACS; -.
PhylomeDB; P00561; -.
BioCyc; EcoCyc:ASPKINIHOMOSERDEHYDROGI-MONOMER; -.
BioCyc; MetaCyc:ASPKINIHOMOSERDEHYDROGI-MONOMER; -.
SABIO-RK; P00561; -.
UniPathway; UPA00034; UER00015.
UniPathway; UPA00050; UER00063.
UniPathway; UPA00050; UER00461.
UniPathway; UPA00051; UER00462.
UniPathway; UPA00051; UER00465.
PRO; PR:P00561; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0004072; F:aspartate kinase activity; IDA:EcoCyc.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004412; F:homoserine dehydrogenase activity; IDA:EcoCyc.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0009090; P:homoserine biosynthetic process; IDA:EcoCyc.
GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IDA:EcoCyc.
GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.1160.10; -; 2.
InterPro; IPR036393; AceGlu_kinase-like_sf.
InterPro; IPR002912; ACT_dom.
InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
InterPro; IPR001341; Asp_kinase.
InterPro; IPR018042; Aspartate_kinase_CS.
InterPro; IPR011147; Bifunc_aspartokin/hSer_DH.
InterPro; IPR027795; CASTOR_ACT_dom.
InterPro; IPR001342; HDH_cat.
InterPro; IPR019811; HDH_CS.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF00696; AA_kinase; 1.
Pfam; PF01842; ACT; 1.
Pfam; PF13840; ACT_7; 1.
Pfam; PF00742; Homoserine_dh; 1.
Pfam; PF03447; NAD_binding_3; 1.
PIRSF; PIRSF000727; ThrA; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF53633; SSF53633; 1.
TIGRFAMs; TIGR00657; asp_kinases; 1.
PROSITE; PS51671; ACT; 2.
PROSITE; PS00324; ASPARTOKINASE; 1.
PROSITE; PS01042; HOMOSER_DHGENASE; 1.
1: Evidence at protein level;
Allosteric enzyme; Amino-acid biosynthesis; ATP-binding;
Complete proteome; Direct protein sequencing; Kinase;
Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase;
Reference proteome; Repeat; Threonine biosynthesis; Transferase.
CHAIN 1 820 Bifunctional aspartokinase/homoserine
dehydrogenase 1.
/FTId=PRO_0000066681.
DOMAIN 320 394 ACT 1. {ECO:0000255|PROSITE-
ProRule:PRU01007}.
DOMAIN 401 478 ACT 2. {ECO:0000255|PROSITE-
ProRule:PRU01007}.
NP_BIND 471 478 NADP. {ECO:0000255}.
REGION 1 249 Aspartokinase.
REGION 250 470 Interface.
REGION 471 820 Homoserine dehydrogenase.
CONFLICT 11 11 V -> L (in Ref. 1; CAA23660/AAA83914).
{ECO:0000305}.
CONFLICT 113 113 Q -> E (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 230 230 D -> N (in Ref. 1; CAA23660/AAA83914).
{ECO:0000305}.
CONFLICT 375 375 Q -> L (in Ref. 1; CAA23660/AAA83914).
{ECO:0000305}.
CONFLICT 393 393 T -> A (in Ref. 1; CAA23660/AAA83914).
{ECO:0000305}.
CONFLICT 406 406 M -> L (in Ref. 1; CAA23660/AAA83914).
{ECO:0000305}.
CONFLICT 553 553 D -> N (in Ref. 1; CAA23660/AAA83914).
{ECO:0000305}.
CONFLICT 587 588 DY -> IT (in Ref. 10; AAA24671).
{ECO:0000305}.
CONFLICT 607 607 T -> I (in Ref. 1; CAA23660/AAA83914).
{ECO:0000305}.
CONFLICT 658 658 T -> R (in Ref. 1; CAA23660/AAA83914).
{ECO:0000305}.
SEQUENCE 820 AA; 89120 MW; 0BF28E9EECAB10ED CRC64;
MRVLKFGGTS VANAERFLRV ADILESNARQ GQVATVLSAP AKITNHLVAM IEKTISGQDA
LPNISDAERI FAELLTGLAA AQPGFPLAQL KTFVDQEFAQ IKHVLHGISL LGQCPDSINA
ALICRGEKMS IAIMAGVLEA RGHNVTVIDP VEKLLAVGHY LESTVDIAES TRRIAASRIP
ADHMVLMAGF TAGNEKGELV VLGRNGSDYS AAVLAACLRA DCCEIWTDVD GVYTCDPRQV
PDARLLKSMS YQEAMELSYF GAKVLHPRTI TPIAQFQIPC LIKNTGNPQA PGTLIGASRD
EDELPVKGIS NLNNMAMFSV SGPGMKGMVG MAARVFAAMS RARISVVLIT QSSSEYSISF
CVPQSDCVRA ERAMQEEFYL ELKEGLLEPL AVTERLAIIS VVGDGMRTLR GISAKFFAAL
ARANINIVAI AQGSSERSIS VVVNNDDATT GVRVTHQMLF NTDQVIEVFV IGVGGVGGAL
LEQLKRQQSW LKNKHIDLRV CGVANSKALL TNVHGLNLEN WQEELAQAKE PFNLGRLIRL
VKEYHLLNPV IVDCTSSQAV ADQYADFLRE GFHVVTPNKK ANTSSMDYYH QLRYAAEKSR
RKFLYDTNVG AGLPVIENLQ NLLNAGDELM KFSGILSGSL SYIFGKLDEG MSFSEATTLA
REMGYTEPDP RDDLSGMDVA RKLLILARET GRELELADIE IEPVLPAEFN AEGDVAAFMA
NLSQLDDLFA ARVAKARDEG KVLRYVGNID EDGVCRVKIA EVDGNDPLFK VKNGENALAF
YSHYYQPLPL VLRGYGAGND VTAAGVFADL LRTLSWKLGV


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