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Entry version 121 (02 Jun 2021)
Sequence version 1 (03 Oct 2006)
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Protein

3-hydroxykynurenine transaminase

Gene

HKT

Organism
Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
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

Catalyzes the pyridoxal 5'-phosphate-dependent transamination of both 3-hydroxykynurenine and L-kynurenine to xanthurenic acid and kynurenic acid, respectively, preferentially using the alpha-ketoacid pyruvate, glyoxylate or oxaloacetate as the amino group acceptor (PubMed:11880382, PubMed:12220660).

The affinity and catalytic efficiency for 3-hydroxykynurenine is higher than for L-kynurenine (PubMed:12220660).

Involved in the detoxification of cytotoxic metabolite 3-hydroxykynurenine generated by the hydroxylation of L-kynurenine, an intermediate in the tryptophan catabolism pathway (PubMed:11880382, PubMed:12220660).

Also catalyzes, although with a lesser efficiency, the transamination of alanine with glyoxylate as an amino group acceptor (PubMed:11880382).

May play a role in the detoxification of glyoxylate, a toxic plant metabolite from the diet (Probable).

2 Publications2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pyridoxal 5'-phosphateUniRule annotation1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 2424 min(-1) for 3-hydroxykynurenine (at 50 degrees Celsius and pH 7 (PubMed:11880382). kcat is 1640 min(-1) for L-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate) (PubMed:11880382). kcat is 1200 min(-1) for alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate) (PubMed:12220660). kcat is 1664 min(-1) for L,D-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate) (PubMed:11880382). kcat is 960 min(-1) for glyoxylate (at 50 degrees Celsius, pH 7.0 and with alanine as cosubstrate) (PubMed:12220660). kcat is 960 min(-1) for L-kynurenine (at 50 degrees Celsius and pH 7.0) (PubMed:11880382). kcat is 720 min(-1) for L,D-kynurenine (at 50 degrees Celsius and pH 7.0) (PubMed:11880382).2 Publications
  1. KM=3.7 mM for 3-hydroxykynurenine (at 50 degrees Celsius and pH 7.0)1 Publication
  2. KM=11.2 mM for L-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate)1 Publication
  3. KM=18 mM for alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate)1 Publication
  4. KM=22.8 mM for L,D-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate)1 Publication
  5. KM=1.6 mM for glyoxylate (at 50 degrees Celsius, pH 7.0 and with alanine as cosubstrate)1 Publication
  6. KM=6.2 mM for L-kynurenine (at 50 degrees Celsius and pH 7.0)1 Publication
  7. KM=10 mM for L,D-kynurenine (at 50 degrees Celsius and pH 7.0)1 Publication
  1. Vmax=60.6 µmol/min/mg enzyme toward 3-hydroxykynurenine (at 50 degrees Celsius and pH 7.0)1 Publication
  2. Vmax=41 µmol/min/mg enzyme toward L-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate)1 Publication
  3. Vmax=30 µmol/min/mg enzyme toward alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate)1 Publication
  4. Vmax=41.6 µmol/min/mg enzyme toward L,D-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate)1 Publication
  5. Vmax=24 µmol/min/mg enzyme toward glyoxylate (at 50 degrees Celsius, pH 7.0 and with alanine as cosubstrate)1 Publication
  6. Vmax=24 µmol/min/mg enzyme toward L-kynurenine (at 50 degrees Celsius and pH 7.0)1 Publication
  7. Vmax=18 µmol/min/mg enzyme toward L-kynurenine (at 50 degrees Celsius and pH 7.0)1 Publication

pH dependencei

Optimum pH is 9 with 3-hydroxykynurenine and pyruvate, or L-alanine and glyoxylate as substrates at 50 degrees Celsius.2 Publications

Temperature dependencei

Optimum temperature is 55 degrees Celsius with 3-hydroxykynurenine and pyruvate at pH 7 (PubMed:11880382, PubMed:12220660). Optimum temperature is 60 degrees Celsius with L-alanine and glyoxylate at pH 7 (PubMed:11880382, PubMed:12220660).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-kynurenine degradation

This protein is involved in step 1 of the subpathway that synthesizes kynurenate from L-kynurenine.2 Publications This subpathway is part of the pathway L-kynurenine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes kynurenate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei154Pyridoxal phosphateCombined sources1 Publication1
Binding sitei154SubstrateBy similarity1
Binding sitei204Pyridoxal phosphateCombined sources1 Publication1
Binding sitei256Pyridoxal phosphate; shared with dimeric partnerCombined sources1 Publication1
Binding sitei259Pyridoxal phosphate; shared with dimeric partnerCombined sources1 Publication1
Binding sitei356SubstrateBy similarity1

<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 functionAminotransferase, Transferase
LigandPyridoxal phosphate

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00334;UER00726

<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%5Fand%5Ftaxonomy%5Fsection">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:
3-hydroxykynurenine transaminase1 Publication (EC:2.6.1.632 Publications)
Alternative name(s):
3-hydroxykynurenine transaminase and alanine--glyoxylate aminotransferase1 Publication
Short name:
Ae-HKT/AGT1 Publication
Alanine--glyoxylate aminotransferaseUniRule annotation (EC:2.6.1.44UniRule annotation2 Publications)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:HKT1 Publication
ORF Names:AAEL003508Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiAedes aegypti (Yellowfever mosquito) (Culex aegypti)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri7159 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeCulicinaeAediniAedesStegomyia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000008820 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unplaced

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
VectorBase:AAEL003508

<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

Peroxisome

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004521851 – 4003-hydroxykynurenine transaminaseAdd BLAST400

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei205N6-(pyridoxal phosphate)lysineUniRule annotationCombined sources1 Publication1

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed in developing ovaries and larvae (PubMed:11880382). Expression increases from 1- to 4-day-old larvae, decreases in 5- and 6-day-old larvae and newly formed pupae, and becomes undetectable in 12 h pupae (PubMed:11880382).1 Publication

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (By similarity). May form homotetramer (PubMed:12220660).

By similarity1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
7159.AAEL003508-PB

<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
Q0IG34

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

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>Regioni43 – 44Binds to and confers specificity for 3-hydroxykynurenine; shared with dimeric partnerBy similarity2
Regioni77 – 79Pyridoxal phosphate bindingCombined sources1 Publication3

<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

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2862, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_027686_0_0_1

Identification of Orthologs from Complete Genome Data

More...
OMAi
NGIWAER

Database of Orthologous Groups

More...
OrthoDBi
984738at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.640.10, 1 hit
3.90.1150.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000192, Aminotrans_V_dom
IPR015424, PyrdxlP-dep_Trfase
IPR015422, PyrdxlP-dep_Trfase_dom1
IPR015421, PyrdxlP-dep_Trfase_major
IPR024169, SP_NH2Trfase/AEP_transaminase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00266, Aminotran_5, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000524, SPT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53383, SSF53383, 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%5Flength">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q0IG34-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKFTPPPSSL RGPLVIPDKI MMGPGPSNCS KRVLAALNNT CLSNFHDELF
60 70 80 90 100
QVIDEVKDGL RYIFQTENRT TMCITGSAHT GMEALLCNLL EEGDIVLIAN
110 120 130 140 150
NGIWAERAIN MATRYGADVR VLGGPADKPF SMTDFKKAIE QHRPKCLFVV
160 170 180 190 200
HGDSSSGLLQ PLEGLGKICH DYDCLLLVDA VASLCGVPFY MDKWEIDGVY
210 220 230 240 250
TGSQKVLGAP PGITPISISP KALEVIRSRK TPSKVFYWDL LILGNYWGCY
260 270 280 290 300
DEQKRYHHTV PSNLIFALRE AIAQIAEEGL EPVIRRRQEC AEQMYRGLQA
310 320 330 340 350
MGLEIFVKDP EYRLPTVTCI MIPKGVNWWK VSEYAMNNFS LEIQGGFGPT
360 370 380 390 400
MGIAWRAGIM GESSTLQRVN FYLYAFKESL KATHPDYVFE KKNGQTNGTK
Length:400
Mass (Da):44,691
Last modified:October 3, 2006 - 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:i770F59D680DB7D8A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A6I8T814A0A6I8T814_AEDAE
Alanine--glyoxylate aminotransferas...
5578354
400Annotation score:

Annotation score:2 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>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAL29468 differs from that shown. Reason: Frameshift.Curated

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 conflicti123G → E in AAL29468 (PubMed:11880382).Curated1

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
CH477274 Genomic DNA Translation: EAT45177.1
CH477274 Genomic DNA Translation: EAT45178.1
AF435806 mRNA Translation: AAL29468.1 Frameshift.

NCBI Reference Sequences

More...
RefSeqi
XP_001656923.1, XM_001656873.1
XP_001656924.1, XM_001656874.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5578354

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
aag:5578354

<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
CH477274 Genomic DNA Translation: EAT45177.1
CH477274 Genomic DNA Translation: EAT45178.1
AF435806 mRNA Translation: AAL29468.1 Frameshift.
RefSeqiXP_001656923.1, XM_001656873.1
XP_001656924.1, XM_001656874.1

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
6MFBX-ray2.50A/B/C/D1-386[»]
SMRiQ0IG34
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi7159.AAEL003508-PB

Genome annotation databases

GeneIDi5578354
KEGGiaag:5578354

Organism-specific databases

VEuPathDBiVectorBase:AAEL003508

Phylogenomic databases

eggNOGiKOG2862, Eukaryota
HOGENOMiCLU_027686_0_0_1
OMAiNGIWAER
OrthoDBi984738at2759

Enzyme and pathway databases

UniPathwayiUPA00334;UER00726

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 1 hit
InterProiView protein in InterPro
IPR000192, Aminotrans_V_dom
IPR015424, PyrdxlP-dep_Trfase
IPR015422, PyrdxlP-dep_Trfase_dom1
IPR015421, PyrdxlP-dep_Trfase_major
IPR024169, SP_NH2Trfase/AEP_transaminase
PfamiView protein in Pfam
PF00266, Aminotran_5, 1 hit
PIRSFiPIRSF000524, SPT, 1 hit
SUPFAMiSSF53383, SSF53383, 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 nameiHKT_AEDAE
<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: Q0IG34
Secondary accession number(s): Q95V15
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 7, 2021
Last sequence update: October 3, 2006
Last modified: June 2, 2021
This is version 121 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)

<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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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