Bifunctional aspartokinase/homoserine dehydrogenase 1

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P00561 (AK1H_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 131. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Bifunctional aspartokinase/homoserine dehydrogenase 1

Alternative name(s):
Aspartokinase I/homoserine dehydrogenase I
Short name=AKI-HDI

Including the following 2 domains:

Aspartokinase
EC=2.7.2.4
Homoserine dehydrogenase
EC=1.1.1.3

Gene names

Name:	thrA
Synonyms:	thrA1, thrA2
Ordered Locus Names:	b0002, JW0001

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	820 AA.
Sequence status	Complete.
Protein existence	Evidence 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; (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 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Threonine biosynthesis
Domain	Repeat
Ligand	ATP-binding NADP Nucleotide-binding
Molecular function	Kinase Oxidoreductase Transferase
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	homoserine biosynthetic process Inferred from direct assay. Source: EcoCyc lysine biosynthetic process via diaminopimelate Inferred from direct assay. Source: EcoCyc threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NADP binding Inferred from electronic annotation. Source: InterPro amino acid binding Inferred from electronic annotation. Source: InterPro aspartate kinase activity Inferred from electronic annotation. Source: EC homoserine dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 820

820

Bifunctional aspartokinase/homoserine dehydrogenase 1

PRO_0000066681

Regions

Domain

316 – 384

ACT 1

Domain

397 – 468

ACT 2

Nucleotide binding

471 – 478

NADP Potential

Region

1 – 249

249

Aspartokinase

Region

250 – 470

221

Interface

Region

471 – 820

350

Homoserine dehydrogenase

Experimental info

Sequence conflict

V → L in CAA23660. Ref.1

Sequence conflict

V → L in AAA83914. Ref.1

Sequence conflict

113

Q → E AA sequence Ref.8

Sequence conflict

230

D → N in CAA23660. Ref.1

Sequence conflict

230

D → N in AAA83914. Ref.1

Sequence conflict

375

Q → L in CAA23660. Ref.1

Sequence conflict

375

Q → L in AAA83914. Ref.1

Sequence conflict

393

T → A in CAA23660. Ref.1

Sequence conflict

393

T → A in AAA83914. Ref.1

Sequence conflict

406

M → L in CAA23660. Ref.1

Sequence conflict

406

M → L in AAA83914. Ref.1

Sequence conflict

553

D → N in CAA23660. Ref.1

Sequence conflict

553

D → N in AAA83914. Ref.1

Sequence conflict

587 – 588

DY → IT in AAA24671. Ref.10

Sequence conflict

607

T → I in CAA23660. Ref.1

Sequence conflict

607

T → I in AAA83914. Ref.1

Sequence conflict

658

T → R in CAA23660. Ref.1

Sequence conflict

658

T → R in AAA83914. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P00561 [UniParc].

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

FASTA

820

89,120

        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' referencesShow '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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	DEECK. B64720.
RefSeq	NP_414543.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P00561.
SMR	P00561. Positions 1-816.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2907N.
IntAct	P00561. 7 interactions.
MINT	MINT-1288804.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000004324; EBESCP00000004324; EBESCG00000003521. EBESCT00000016021; EBESCP00000015312; EBESCG00000015081.
GeneID	945803.
GenomeReviews	Gene locus JW0001 in contig AP009048_GR. Gene locus b0002 in contig U00096_GR.
KEGG	ecj:JW0001. eco:b0002.
PATRIC	32115099. VBIEscCol129921_0001.
Organism-specific databases
EchoBASE	EB0991.
EcoGene	EG10998. thrA.
Phylogenomic databases
eggNOG	COG0527.
GeneTree	EBGT00050000009086.
HOGENOM	HBG298754.
OMA	GANEMNI.
PhylomeDB	P00561.
ProtClustDB	PRK09436.
Enzyme and pathway databases
BioCyc	EcoCyc:ASPKINIHOMOSERDEHYDROGI-MONOMER. MetaCyc:ASPKINIHOMOSERDEHYDROGI-MONOMER.
Gene expression databases
Genevestigator	P00561.
Family and domain databases
InterPro	IPR002912. ACT-bd. IPR001048. 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]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 2 hits. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K12524.
Pfam	PF00696. AA_kinase. 1 hit. PF01842. ACT. 2 hits. PF00742. Homoserine_dh. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view]
PIRSF	PIRSF000727. ThrA. 1 hit.
SUPFAM	SSF53633. Aa_kinase. 1 hit.
TIGRFAMs	TIGR00657. Asp_kinases. 1 hit.
PROSITE	PS00324. ASPARTOKINASE. 1 hit. PS01042. HOMOSER_DHGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AK1H_ECOLI

Accession

Primary (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:	January 25, 2012
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents