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UniProtKB - Q9FLQ4 (ODO2A_ARATH)

Entry version 128 (02 Dec 2020)
Sequence version 1 (01 Mar 2001)
Previous versions | rss
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Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial

Gene

At5g55070

Organism
Arabidopsis thaliana (Mouse-ear cress)
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

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).By similarity

<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

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

<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-lysine degradation via saccharopine pathway

This protein is involved in step 6 of the subpathway that synthesizes glutaryl-CoA from L-lysine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Lysine ketoglutarate reductase (C24_LOCUS20033), Lysine ketoglutarate reductase (LKR), Lysine ketoglutarate reductase (AXX17_At4g37980), Lysine ketoglutarate reductase (AN1_LOCUS20138), Alpha-aminoadipic semialdehyde synthase (LKR/SDH)
  2. Lysine ketoglutarate reductase (C24_LOCUS20033), Lysine ketoglutarate reductase (LKR), Lysine ketoglutarate reductase (AXX17_At4g37980), Lysine ketoglutarate reductase (AN1_LOCUS20138), Alpha-aminoadipic semialdehyde synthase (LKR/SDH)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. Dihydrolipoyllysine-residue succinyltransferase (C24_LOCUS25606), Dihydrolipoyllysine-residue succinyltransferase (AXX17_At4g31060), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial (At4g26910), Dihydrolipoyllysine-residue succinyltransferase (AXX17_At5g54170), Dihydrolipoyllysine-residue succinyltransferase (AN1_LOCUS25778), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial (At5g55070), Dihydrolipoyllysine-residue succinyltransferase (AXX17_At4g31060)
This subpathway is part of the pathway L-lysine degradation via saccharopine pathway, 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 glutaryl-CoA from L-lysine, the pathway L-lysine degradation via saccharopine pathway 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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei435By similarity1
Active sitei439By 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionAcyltransferase, Transferase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		ARA:AT5G55070-MONOMER

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

More...UniPathwayi		UPA00868;UER00840

<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:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial (EC:2.3.1.61)
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2-1
Short name:
OGDC-E2-1
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1
E2K-1
<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
Ordered Locus Names:At5g55070
ORF Names:MCO15.2
<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>OrganismiArabidopsis thaliana (Mouse-ear cress)
<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 identifieri3702 [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 lineageiEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis
<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
  • UP000006548 <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: Chromosome 5

Organism-specific databases

Arabidopsis Information Portal

More...Araporti		AT5G55070

The Arabidopsis Information Resource

More...TAIRi		locus:2161670, AT5G55070

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

<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 peptidei1 – 86Mitochondrion1 PublicationAdd BLAST86
<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_000039951287 – 464Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrialAdd BLAST378

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 residuei134N6-lipoyllysinePROSITE-ProRule annotation1

Proteomic databases

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

More...PaxDbi		Q9FLQ4

PRoteomics IDEntifications database

More...PRIDEi		Q9FLQ4

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		250874

PTM databases

MetOSite database of methionine sulfoxide sites

More...MetOSitei		Q9FLQ4

<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

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9FLQ4, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9FLQ4, AT

<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

Forms a 24-polypeptide structural core with octahedral symmetry.

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		20842, 11 interactors

Protein interaction database and analysis system

More...IntActi		Q9FLQ4, 1 interactor

STRING: functional protein association networks

More...STRINGi		3702.AT5G55070.1

<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		Q9FLQ4

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%5Fand%5Fdomains%5Fsection">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>Domaini93 – 168Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi179 – 231Pro-richAdd BLAST53

<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 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0559, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_016733_0_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9FLQ4

Identification of Orthologs from Complete Genome Data

More...OMAi		DMAGATF

Database of Orthologous Groups

More...OrthoDBi		850255at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9FLQ4

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.559.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003016, 2-oxoA_DH_lipoyl-BS
IPR001078, 2-oxoacid_DH_actylTfrase
IPR000089, Biotin_lipoyl
IPR023213, CAT-like_dom_sf
IPR011053, Single_hybrid_motif
IPR006255, SucB

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00198, 2-oxoacid_dh, 1 hit
PF00364, Biotin_lipoyl, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51230, SSF51230, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01347, sucB, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50968, BIOTINYL_LIPOYL, 1 hit
PS00189, LIPOYL, 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>Sequencei

<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.

<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 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.

Q9FLQ4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMLRAVFRRA SIRGSSSASG LGKSLQSSRV AVSAQFHSVS ATETLVPRGN 
        60         70         80         90        100
HAHSFHHRSC PGCPDCSRTI INGYQGTALQ RWVRPFSSDS GDVVEAVVPH 
       110        120        130        140        150
MGESITDGTL AAFLKKPGDR VEADEAIAQI ETDKVTIDIA SPASGVIQEF 
       160        170        180        190        200
LVKEGDTVEP GNKVARISTS ADAVSHVAPS EKAPEKPAPK PSPPAEKPKV 
       210        220        230        240        250
ESTKVAEKPK APSPPPPPPS KQSAKEPQLP PKDRERRVPM TRLRKRVATR 
       260        270        280        290        300
LKDSQNTFAL LTTFNEVDMT NLMKLRSQYK DAFLEKHGVK LGLMSGFIKA 
       310        320        330        340        350
AVSALQHQPV VNAVIDGDDI IYRDYVDISI AVGTSKGLVV PVIRDADKMN 
       360        370        380        390        400
FADIEKTING LAKKATEGTI SIDEMAGGSF TVSNGGVYGS LISTPIINPP 
       410        420        430        440        450
QSAILGMHSI VQRPMVVGGS VVPRPMMYVA LTYDHRLIDG REAVYFLRRI 
       460 
KDVVEDPQRL LLDI
Length:464
Mass (Da):50,134
Last modified:March 1, 2001 - 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:iD5BD3083ACA39879
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 conflicti30 – 34VAVSA → LVASS in CAA11553 (Ref. 1) Curated5
Sequence conflicti70I → V in CAA11553 (Ref. 1) Curated1
Sequence conflicti74Y → F in CAA11553 (Ref. 1) Curated1
Sequence conflicti218 – 219Missing in CAA11553 (Ref. 1) Curated2

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
AJ223803 mRNA Translation: CAA11553.1
AB010071 Genomic DNA Translation: BAB08576.1
CP002688 Genomic DNA Translation: AED96577.1
CP002688 Genomic DNA Translation: ANM68999.1
AY042897 mRNA Translation: AAK68837.1
AY128726 mRNA Translation: AAM91126.1

NCBI Reference Sequences

More...RefSeqi		NP_001330709.1, NM_001345105.1
NP_200318.1, NM_124889.5

Genome annotation databases

Ensembl plant genome annotation project

More...EnsemblPlantsi		AT5G55070.1; AT5G55070.1; AT5G55070
AT5G55070.2; AT5G55070.2; AT5G55070

Database of genes from NCBI RefSeq genomes

More...GeneIDi		835598

Gramene; a comparative resource for plants

More...Gramenei		AT5G55070.1; AT5G55070.1; AT5G55070
AT5G55070.2; AT5G55070.2; AT5G55070

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ath:AT5G55070

<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
AJ223803 mRNA Translation: CAA11553.1
AB010071 Genomic DNA Translation: BAB08576.1
CP002688 Genomic DNA Translation: AED96577.1
CP002688 Genomic DNA Translation: ANM68999.1
AY042897 mRNA Translation: AAK68837.1
AY128726 mRNA Translation: AAM91126.1
RefSeqiNP_001330709.1, NM_001345105.1
NP_200318.1, NM_124889.5

3D structure databases

SMRiQ9FLQ4
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi20842, 11 interactors
IntActiQ9FLQ4, 1 interactor
STRINGi3702.AT5G55070.1

PTM databases

MetOSiteiQ9FLQ4

Proteomic databases

PaxDbiQ9FLQ4
PRIDEiQ9FLQ4
ProteomicsDBi250874

Genome annotation databases

EnsemblPlantsiAT5G55070.1; AT5G55070.1; AT5G55070
AT5G55070.2; AT5G55070.2; AT5G55070
GeneIDi835598
GrameneiAT5G55070.1; AT5G55070.1; AT5G55070
AT5G55070.2; AT5G55070.2; AT5G55070
KEGGiath:AT5G55070

Organism-specific databases

AraportiAT5G55070
TAIRilocus:2161670, AT5G55070

Phylogenomic databases

eggNOGiKOG0559, Eukaryota
HOGENOMiCLU_016733_0_2_1
InParanoidiQ9FLQ4
OMAiDMAGATF
OrthoDBi850255at2759
PhylomeDBiQ9FLQ4

Enzyme and pathway databases

UniPathwayiUPA00868;UER00840
BioCyciARA:AT5G55070-MONOMER

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q9FLQ4

Gene expression databases

ExpressionAtlasiQ9FLQ4, baseline and differential
GenevisibleiQ9FLQ4, AT

Family and domain databases

Gene3Di3.30.559.10, 1 hit
InterProiView protein in InterPro
IPR003016, 2-oxoA_DH_lipoyl-BS
IPR001078, 2-oxoacid_DH_actylTfrase
IPR000089, Biotin_lipoyl
IPR023213, CAT-like_dom_sf
IPR011053, Single_hybrid_motif
IPR006255, SucB
PfamiView protein in Pfam
PF00198, 2-oxoacid_dh, 1 hit
PF00364, Biotin_lipoyl, 1 hit
SUPFAMiSSF51230, SSF51230, 1 hit
TIGRFAMsiTIGR01347, sucB, 1 hit
PROSITEiView protein in PROSITE
PS50968, BIOTINYL_LIPOYL, 1 hit
PS00189, LIPOYL, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiODO2A_ARATH
<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: Q9FLQ4
Secondary accession number(s): Q9ZRQ1
<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: October 5, 2010
Last sequence update: March 1, 2001
Last modified: December 2, 2020
This is version 128 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

Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
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