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Entry version 119 (07 Apr 2021)
Sequence version 1 (01 Oct 1994)
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Protein

Bifunctional aspartokinase/homoserine dehydrogenase, chloroplastic

Gene
N/A
Organism
Daucus carota (Wild carrot)
Status
Reviewed-Annotation score:

Annotation score:4 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

<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 <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. 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. 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. 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi569 – 574NADPSequence analysis6

<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 functionKinase, Multifunctional enzyme, Oxidoreductase, Transferase
Biological processAmino-acid biosynthesis, Methionine biosynthesis
LigandATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P37142

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, chloroplastic
Short name:
AK-HD
Short name:
AK-HSDH
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 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>OrganismiDaucus carota (Wild carrot)
<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 identifieri4039 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsApialesApiaceaeApioideaeScandiceaeDaucinaeDaucusDaucus sect. Daucus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Chloroplast, Plastid

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei‹1 – 87ChloroplastAdd BLAST›87
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000239188 – 921Bifunctional aspartokinase/homoserine dehydrogenase, chloroplasticAdd BLAST834

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P37142

<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

3D structure databases

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

More...
SMRi
P37142

Database of comparative protein structure models

More...
ModBasei
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>Domaini417 – 489ACT 1PROSITE-ProRule annotationAdd BLAST73
Domaini498 – 575ACT 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>Regioni88 – 339AspartokinaseAdd BLAST252
Regioni340 – 567InterfaceAdd BLAST228
Regioni568 – 921Homoserine dehydrogenaseAdd BLAST354

<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, Transit peptide

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04257, AAK_AK-HSDH, 1 hit

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
IPR041743, AK-HSDH_N
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

The PANTHER Classification System

More...
PANTHERi
PTHR43070, PTHR43070, 1 hit

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

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>. The information is filed in different subsections. The current subsections and their content are listed below:<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: Fragment.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P37142-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
SLSSAISPSS YAAIAAAYSA RTPIFNKKKT AAVLSPLSLF HQSPSLSKTG
60 70 80 90 100
IFLHRGRKES SSKFYIAASV TTAVPSLDDS VEKVHLPRGA MWSIHKFGGT
110 120 130 140 150
CVGSSERIRN VAEIVVEDDS ERKLVVVSAM SKVTDMMYDL IYKAQSRDDS
160 170 180 190 200
YESALDAVME KHKLTAFDLL DEDDLARFLT RLQHDVITLK AMLRAIYIAG
210 220 230 240 250
HATESFSDFV VGHGELWSAQ LLSFVIRKNG GDCNWMDTRD VLVVNPAGSN
260 270 280 290 300
QVDPDYLESE KRLEKWFSSN QCQTIVATGF IASTPQNIPT TLKRDGSDFS
310 320 330 340 350
AAIMGALLRA GQVTIWTDVN GVYSADPRKV SEAVVLKTLS YQEAWEMSYF
360 370 380 390 400
GANVLHPRTI NPVMRYDIPI VIRNIFNLSA PGTMICRESV GETEDGLKLE
410 420 430 440 450
SHVKGFATID NLALINVEGT GMAGVPGTAT AIFGAVKDVG ANVIMISQAS
460 470 480 490 500
SEHSICFAVP ESEVKAVAKA LEARFRQALD AGRLSQVANN PNCSILATVG
510 520 530 540 550
QKMASTPGVS ATLFNALAKA NINVRAIAQG CTEYNITVVL SREDCVRALK
560 570 580 590 600
AVHSRFYLSR TTIAVGIVGP GLIGATLLDQ LRDQAAILKE NSKIDLRVMG
610 620 630 640 650
ITGSRTMLLS ETGIDLSRWR EVQKEKGQTA GLEKFVQHVR GNHFIPSTVI
660 670 680 690 700
VDCTADSEVA SHYHDWLCRG IHVITPNKKA NSGPLDQYLK LRALQRRSYT
710 720 730 740 750
HYFYEATVVA GLPIITTLQG LLETGDKILR IEGIFSGTLS YIFNNFKSTT
760 770 780 790 800
PFSEVVSEAK AAGYTEPDPR DDLAGTDVAR KVIILARGSG LKLELSDIPV
810 820 830 840 850
QSLVPEPLRG IASAEEFLLQ LPQFDSDMTR KREDAENAGE VLRYVGVVDA
860 870 880 890 900
VNQKGVVELK RYKKEHPFAQ LSGSDNINAF TTERYNKQPP IIRGPGAGAE
910 920
VTAGGVFSDI LRLASYLGAP S
Length:921
Mass (Da):100,226
Last modified:October 1, 1994 - v1
<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:i9C89C392DA76A996
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei11

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L11529 mRNA Translation: AAA16972.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S35160

<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
L11529 mRNA Translation: AAA16972.1
PIRiS35160

3D structure databases

SMRiP37142
ModBaseiSearch...

Proteomic databases

PRIDEiP37142

Enzyme and pathway databases

UniPathwayiUPA00034;UER00015
UPA00050;UER00063
UPA00050;UER00461
UPA00051;UER00462
UPA00051;UER00465
SABIO-RKiP37142

Family and domain databases

CDDicd04257, AAK_AK-HSDH, 1 hit
Gene3Di3.40.1160.10, 1 hit
InterProiView protein in InterPro
IPR036393, AceGlu_kinase-like_sf
IPR002912, ACT_dom
IPR041743, AK-HSDH_N
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
PANTHERiPTHR43070, PTHR43070, 1 hit
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
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

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 nameiAKH_DAUCA
<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: P37142
<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: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 7, 2021
This is version 119 of the entry and version 1 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 programPlant 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

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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