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Entry version 187 (13 Feb 2019)
Sequence version 2 (29 Aug 2003)
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Protein

Bifunctional aspartokinase/homoserine dehydrogenase 1

Gene

thrA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The enzyme activities are regulated allosterically by L-threonine.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi471 – 478NADPSequence analysis8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:ASPKINIHOMOSERDEHYDROGI-MONOMER
ECOL316407:JW0001-MONOMER
MetaCyc:ASPKINIHOMOSERDEHYDROGI-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00561

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00034;UER00015

UPA00050;UER00063

UPA00050;UER00461

UPA00051;UER00462

UPA00051;UER00465

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:thrA
Synonyms:thrA1, thrA2
Ordered Locus Names:b0002, JW0001
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10998 thrA

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000666811 – 820Bifunctional aspartokinase/homoserine dehydrogenase 1Add BLAST820

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P00561

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P00561

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P00561

PRoteomics IDEntifications database

More...
PRIDEi
P00561

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261933, 242 interactors

Database of interacting proteins

More...
DIPi
DIP-2907N

Protein interaction database and analysis system

More...
IntActi
P00561, 7 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_0002

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P00561

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1820
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6MX1X-ray1.67A/B301-460[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P00561

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P00561

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini320 – 394ACT 1PROSITE-ProRule annotationAdd BLAST75
Domaini401 – 478ACT 2PROSITE-ProRule annotationAdd BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 249AspartokinaseAdd BLAST249
Regioni250 – 470InterfaceAdd BLAST221
Regioni471 – 820Homoserine dehydrogenaseAdd BLAST350

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CFH Bacteria
COG0460 LUCA
COG0527 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000271593

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00561

KEGG Orthology (KO)

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KOi
K12524

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P00561

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1160.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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

Pfam protein domain database

More...
Pfami
View 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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000727 ThrA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit
SSF53633 SSF53633, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00657 asp_kinases, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51671 ACT, 2 hits
PS00324 ASPARTOKINASE, 1 hit
PS01042 HOMOSER_DHGENASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0BF28E9EECAB10ED
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
B64720 DEECK

NCBI Reference Sequences

More...
RefSeqi
NP_414543.1, NC_000913.3
WP_001264707.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73113; AAC73113; b0002
BAB96579; BAB96579; BAB96579

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945803

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0001
eco:b0002

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2281

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6MX1X-ray1.67A/B301-460[»]
ProteinModelPortaliP00561
SMRiP00561
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP00561

Proteomic databases

EPDiP00561
jPOSTiP00561
PaxDbiP00561
PRIDEiP00561

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0991
EcoGeneiEG10998 thrA

Phylogenomic databases

eggNOGiENOG4105CFH Bacteria
COG0460 LUCA
COG0527 LUCA
HOGENOMiHOG000271593
InParanoidiP00561
KOiK12524
PhylomeDBiP00561

Enzyme and pathway databases

UniPathwayi
UPA00034;UER00015

UPA00050;UER00063

UPA00050;UER00461

UPA00051;UER00462

UPA00051;UER00465

BioCyciEcoCyc:ASPKINIHOMOSERDEHYDROGI-MONOMER
ECOL316407:JW0001-MONOMER
MetaCyc:ASPKINIHOMOSERDEHYDROGI-MONOMER
SABIO-RKiP00561

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P00561

Family and domain databases

Gene3Di3.40.1160.10, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAK1H_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00561
Secondary accession number(s): Q47659, Q6LEL0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 29, 2003
Last modified: February 13, 2019
This is version 187 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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