Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bifunctional aspartokinase/homoserine dehydrogenase 1

Gene

thrA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Miscellaneous

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

Catalytic activityi

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

Enzyme regulationi

The enzyme activities are regulated allosterically by L-threonine.

Pathwayi: L-lysine biosynthesis via DAP pathway

This protein is involved in step 1 of the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Lysine-sensitive aspartokinase 3 (lysC), Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. 4-hydroxy-tetrahydrodipicolinate synthase (dapA)
  4. 4-hydroxy-tetrahydrodipicolinate reductase (dapB)
This subpathway is part of the pathway L-lysine biosynthesis via DAP pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate, the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

Pathwayi: L-methionine biosynthesis via de novo pathway

This protein is involved in step 1 and 3 of the subpathway that synthesizes L-homoserine from L-aspartate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homoserine from L-aspartate, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Pathwayi: L-threonine biosynthesis

This protein is involved in step 1 and 3 of the subpathway that synthesizes L-threonine from L-aspartate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
  4. Homoserine kinase (thrB)
  5. Threonine synthase (thrC)
This subpathway is part of the pathway L-threonine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-threonine from L-aspartate, the pathway L-threonine biosynthesis and in Amino-acid biosynthesis.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi471 – 478NADPSequence analysis8

GO - Molecular functioni

  • aspartate kinase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-KW
  • homoserine dehydrogenase activity Source: EcoCyc
  • NADP binding Source: InterPro

GO - Biological processi

  • homoserine biosynthetic process Source: EcoCyc
  • lysine biosynthetic process via diaminopimelate Source: EcoCyc
  • threonine biosynthetic process Source: UniProtKB-UniPathway

Keywordsi

Molecular functionAllosteric enzyme, Kinase, Multifunctional enzyme, Oxidoreductase, Transferase
Biological processAmino-acid biosynthesis, Threonine biosynthesis
LigandATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ASPKINIHOMOSERDEHYDROGI-MONOMER
MetaCyc:ASPKINIHOMOSERDEHYDROGI-MONOMER
SABIO-RKiP00561
UniPathwayiUPA00034; UER00015
UPA00050; UER00063
UPA00050; UER00461
UPA00051; UER00462
UPA00051; UER00465

Names & Taxonomyi

Protein namesi
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 namesi
Name:thrA
Synonyms:thrA1, thrA2
Ordered Locus Names:b0002, JW0001
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10998 thrA

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000666811 – 820Bifunctional aspartokinase/homoserine dehydrogenase 1Add BLAST820

Proteomic databases

EPDiP00561
PaxDbiP00561
PRIDEiP00561

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi4261933, 242 interactors
DIPiDIP-2907N
IntActiP00561, 7 interactors
STRINGi316385.ECDH10B_0002

Chemistry databases

BindingDBiP00561

Structurei

3D structure databases

ProteinModelPortaliP00561
SMRiP00561
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini320 – 394ACT 1PROSITE-ProRule annotationAdd BLAST75
Domaini401 – 478ACT 2PROSITE-ProRule annotationAdd BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 249AspartokinaseAdd BLAST249
Regioni250 – 470InterfaceAdd BLAST221
Regioni471 – 820Homoserine dehydrogenaseAdd BLAST350

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CFH Bacteria
COG0460 LUCA
COG0527 LUCA
HOGENOMiHOG000271593
InParanoidiP00561
KOiK12524
OMAiCNKIACS
PhylomeDBiP00561

Family and domain databases

Gene3Di3.40.1160.10, 2 hits
InterProiView protein in InterPro
IPR036393 AceGlu_kinase-like_sf
IPR002912 ACT_dom
IPR001048 Asp/Glu/Uridylate_kinase
IPR005106 Asp/hSer_DH_NAD-bd
IPR001341 Asp_kinase
IPR018042 Aspartate_kinase_CS
IPR011147 Bifunc_aspartokin/hSer_DH
IPR027795 CASTOR_ACT_dom
IPR001342 HDH_cat
IPR019811 HDH_CS
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF00696 AA_kinase, 1 hit
PF01842 ACT, 1 hit
PF13840 ACT_7, 1 hit
PF00742 Homoserine_dh, 1 hit
PF03447 NAD_binding_3, 1 hit
PIRSFiPIRSF000727 ThrA, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
SSF53633 SSF53633, 1 hit
TIGRFAMsiTIGR00657 asp_kinases, 1 hit
PROSITEiView protein in PROSITE
PS51671 ACT, 2 hits
PS00324 ASPARTOKINASE, 1 hit
PS01042 HOMOSER_DHGENASE, 1 hit

Sequencei

Sequence statusi: Complete.

P00561-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVLKFGGTS VANAERFLRV ADILESNARQ GQVATVLSAP AKITNHLVAM
60 70 80 90 100
IEKTISGQDA LPNISDAERI FAELLTGLAA AQPGFPLAQL KTFVDQEFAQ
110 120 130 140 150
IKHVLHGISL LGQCPDSINA ALICRGEKMS IAIMAGVLEA RGHNVTVIDP
160 170 180 190 200
VEKLLAVGHY LESTVDIAES TRRIAASRIP ADHMVLMAGF TAGNEKGELV
210 220 230 240 250
VLGRNGSDYS AAVLAACLRA DCCEIWTDVD GVYTCDPRQV PDARLLKSMS
260 270 280 290 300
YQEAMELSYF GAKVLHPRTI TPIAQFQIPC LIKNTGNPQA PGTLIGASRD
310 320 330 340 350
EDELPVKGIS NLNNMAMFSV SGPGMKGMVG MAARVFAAMS RARISVVLIT
360 370 380 390 400
QSSSEYSISF CVPQSDCVRA ERAMQEEFYL ELKEGLLEPL AVTERLAIIS
410 420 430 440 450
VVGDGMRTLR GISAKFFAAL ARANINIVAI AQGSSERSIS VVVNNDDATT
460 470 480 490 500
GVRVTHQMLF NTDQVIEVFV IGVGGVGGAL LEQLKRQQSW LKNKHIDLRV
510 520 530 540 550
CGVANSKALL TNVHGLNLEN WQEELAQAKE PFNLGRLIRL VKEYHLLNPV
560 570 580 590 600
IVDCTSSQAV ADQYADFLRE GFHVVTPNKK ANTSSMDYYH QLRYAAEKSR
610 620 630 640 650
RKFLYDTNVG AGLPVIENLQ NLLNAGDELM KFSGILSGSL SYIFGKLDEG
660 670 680 690 700
MSFSEATTLA REMGYTEPDP RDDLSGMDVA RKLLILARET GRELELADIE
710 720 730 740 750
IEPVLPAEFN AEGDVAAFMA NLSQLDDLFA ARVAKARDEG KVLRYVGNID
760 770 780 790 800
EDGVCRVKIA EVDGNDPLFK VKNGENALAF YSHYYQPLPL VLRGYGAGND
810 820
VTAAGVFADL LRTLSWKLGV
Length:820
Mass (Da):89,120
Last modified:August 29, 2003 - v2
Checksum:i0BF28E9EECAB10ED
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti11V → L in CAA23660 (PubMed:7003595).Curated1
Sequence conflicti11V → L in AAA83914 (PubMed:7003595).Curated1
Sequence conflicti113Q → E AA sequence (PubMed:387092).Curated1
Sequence conflicti230D → N in CAA23660 (PubMed:7003595).Curated1
Sequence conflicti230D → N in AAA83914 (PubMed:7003595).Curated1
Sequence conflicti375Q → L in CAA23660 (PubMed:7003595).Curated1
Sequence conflicti375Q → L in AAA83914 (PubMed:7003595).Curated1
Sequence conflicti393T → A in CAA23660 (PubMed:7003595).Curated1
Sequence conflicti393T → A in AAA83914 (PubMed:7003595).Curated1
Sequence conflicti406M → L in CAA23660 (PubMed:7003595).Curated1
Sequence conflicti406M → L in AAA83914 (PubMed:7003595).Curated1
Sequence conflicti553D → N in CAA23660 (PubMed:7003595).Curated1
Sequence conflicti553D → N in AAA83914 (PubMed:7003595).Curated1
Sequence conflicti587 – 588DY → IT in AAA24671 (PubMed:390305).Curated2
Sequence conflicti607T → I in CAA23660 (PubMed:7003595).Curated1
Sequence conflicti607T → I in AAA83914 (PubMed:7003595).Curated1
Sequence conflicti658T → R in CAA23660 (PubMed:7003595).Curated1
Sequence conflicti658T → R in AAA83914 (PubMed:7003595).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiB64720 DEECK
RefSeqiNP_414543.1, NC_000913.3
WP_001264707.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73113; AAC73113; b0002
BAB96579; BAB96579; BAB96579
GeneIDi945803
KEGGiecj:JW0001
eco:b0002
PATRICifig|1411691.4.peg.2281

Similar proteinsi

Entry informationi

Entry nameiAK1H_ECOLI
AccessioniPrimary (citable) accession number: P00561
Secondary accession number(s): Q47659, Q6LEL0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 29, 2003
Last modified: March 28, 2018
This is version 182 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health