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UniProtKB - P0AFG3 (ODO1_ECOLI)

Entry version 120 (11 Dec 2019)
Sequence version 1 (20 Dec 2005)
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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

sucA

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

E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO2.1 Publication

Miscellaneous

Binds AMP; however it is not clear if the binding is physiologically relevant.1 Publication

<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 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

thiamine diphosphate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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

Inhibited by oxaloacetate.1 Publication

<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 functionOxidoreductase
Biological processTricarboxylic acid cycle
LigandNucleotide-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:E1O-MONOMER
ECOL316407:JW0715-MONOMER
MetaCyc:E1O-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.2.4.2 2026

<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:
2-oxoglutarate dehydrogenase E1 component (EC:1.2.4.21 Publication)
Alternative name(s):
Alpha-ketoglutarate dehydrogenase
<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:sucA
Ordered Locus Names:b0726, JW0715
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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

<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

GO - Cellular componenti

Complete GO annotation on QuickGO ...

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Impaired growth in minimal medium containing acetate as the sole carbon source.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi260H → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi298H → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi313H → A: Mild reduction in growth in presence of acetate or glucose as sole source of carbon; when associated with A-337. 1 Publication1
Mutagenesisi313H → Q: No growth defect in presence of acetate or glucose as sole source of carbon. 1 Publication1
Mutagenesisi337R → A: Mild reduction in growth in presence of acetate or glucose as sole source of carbon; when associated with A-313. 1 Publication1
Mutagenesisi404S → A: No loss of AMPylation by YdiU. 1 Publication1
Mutagenesisi405T → A: Severe reduction in AMPylation by YdiU. 1 Publication1
Mutagenesisi533W → A: Mild reduction in growth in presence of acetate or glucose as sole source of carbon; when associated with A-710. 1 Publication1
Mutagenesisi533W → I: No growth defect in presence of acetate or glucose as sole source of carbon. 1 Publication1
Mutagenesisi710R → A: Mild reduction in growth in presence of acetate or glucose as sole source of carbon; when associated with A-533. 1 Publication1

<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_00001621911 – 9332-oxoglutarate dehydrogenase E1 componentAdd BLAST933

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 residuei405O-AMP-threonine; by ydiU1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0AFG3

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0AFG3

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

More...PaxDbi		P0AFG3

PRoteomics IDEntifications database

More...PRIDEi		P0AFG3

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P0AFG3

<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

Homodimer (PubMed:17367808). Part of the 2-oxoglutarate dehydrogenase (OGDH) complex composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the complex contains multiple copies of the three enzymatic components (E1, E2 and E3) (Probable).

Interacts (via N-terminus) with SucB, the E2 component of OGDH complex (PubMed:17367808).

1 Publication1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		849680, 3 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3921 2-oxoglutarate dehydrogenase complex

Database of interacting proteins

More...DIPi		DIP-36225N

Protein interaction database and analysis system

More...IntActi		P0AFG3, 13 interactors

Molecular INTeraction database

More...MINTi		P0AFG3

STRING: functional protein association networks

More...STRINGi		511145.b0726

<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

1933
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P0AFG3

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0AFG3

<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

<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 alpha-ketoglutarate dehydrogenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105C7P Bacteria
COG0567 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000259587

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0AFG3

KEGG Orthology (KO)

More...KOi		K00164

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.11610, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR032106 2-oxogl_dehyd_N
IPR011603 2oxoglutarate_DH_E1
IPR001017 DH_E1
IPR031717 KGD_C
IPR042179 KGD_C_sf
IPR029061 THDP-binding
IPR005475 Transketolase-like_Pyr-bd

The PANTHER Classification System

More...PANTHERi		PTHR23152 PTHR23152, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF16078 2-oxogl_dehyd_N, 1 hit
PF00676 E1_dh, 1 hit
PF16870 OxoGdeHyase_C, 1 hit
PF02779 Transket_pyr, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000157 Oxoglu_dh_E1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00861 Transket_pyr, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52518 SSF52518, 2 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00239 2oxo_dh_E1, 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: Complete.

P0AFG3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQNSALKAWL DSSYLSGANQ SWIEQLYEDF LTDPDSVDAN WRSTFQQLPG 
        60         70         80         90        100
TGVKPDQFHS QTREYFRRLA KDASRYSSTI SDPDTNVKQV KVLQLINAYR 
       110        120        130        140        150
FRGHQHANLD PLGLWQQDKV ADLDPSFHDL TEADFQETFN VGSFASGKET 
       160        170        180        190        200
MKLGELLEAL KQTYCGPIGA EYMHITSTEE KRWIQQRIES GRATFNSEEK 
       210        220        230        240        250
KRFLSELTAA EGLERYLGAK FPGAKRFSLE GGDALIPMLK EMIRHAGNSG 
       260        270        280        290        300
TREVVLGMAH RGRLNVLVNV LGKKPQDLFD EFAGKHKEHL GTGDVKYHMG 
       310        320        330        340        350
FSSDFQTDGG LVHLALAFNP SHLEIVSPVV IGSVRARLDR LDEPSSNKVL 
       360        370        380        390        400
PITIHGDAAV TGQGVVQETL NMSKARGYEV GGTVRIVINN QVGFTTSNPL 
       410        420        430        440        450
DARSTPYCTD IGKMVQAPIF HVNADDPEAV AFVTRLALDF RNTFKRDVFI 
       460        470        480        490        500
DLVCYRRHGH NEADEPSATQ PLMYQKIKKH PTPRKIYADK LEQEKVATLE 
       510        520        530        540        550
DATEMVNLYR DALDAGDCVV AEWRPMNMHS FTWSPYLNHE WDEEYPNKVE 
       560        570        580        590        600
MKRLQELAKR ISTVPEAVEM QSRVAKIYGD RQAMAAGEKL FDWGGAENLA 
       610        620        630        640        650
YATLVDEGIP VRLSGEDSGR GTFFHRHAVI HNQSNGSTYT PLQHIHNGQG 
       660        670        680        690        700
AFRVWDSVLS EEAVLAFEYG YATAEPRTLT IWEAQFGDFA NGAQVVIDQF 
       710        720        730        740        750
ISSGEQKWGR MCGLVMLLPH GYEGQGPEHS SARLERYLQL CAEQNMQVCV 
       760        770        780        790        800
PSTPAQVYHM LRRQALRGMR RPLVVMSPKS LLRHPLAVSS LEELANGTFL 
       810        820        830        840        850
PAIGEIDELD PKGVKRVVMC SGKVYYDLLE QRRKNNQHDV AIVRIEQLYP 
       860        870        880        890        900
FPHKAMQEVL QQFAHVKDFV WCQEEPLNQG AWYCSQHHFR EVIPFGASLR 
       910        920        930 
YAGRPASASP AVGYMSVHQK QQQDLVNDAL NVE
Length:933
Mass (Da):105,062
Last modified:December 20, 2005 - 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:iEAEF8429EC31E749
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 conflicti454C → S in AAA23897 (PubMed:6376123).Curated1
Sequence conflicti454C → S in CAA25280 (PubMed:6376123).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
J01619 Genomic DNA Translation: AAA23897.1
X00661 Genomic DNA Translation: CAA25280.1
U00096 Genomic DNA Translation: AAC73820.1
AP009048 Genomic DNA Translation: BAA35392.1

Protein sequence database of the Protein Information Resource

More...PIRi		E64808 DEECOG

NCBI Reference Sequences

More...RefSeqi		NP_415254.1, NC_000913.3
WP_001181473.1, NZ_STEB01000035.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73820; AAC73820; b0726
BAA35392; BAA35392; BAA35392

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945303

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0715
eco:b0726

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1547

<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
J01619 Genomic DNA Translation: AAA23897.1
X00661 Genomic DNA Translation: CAA25280.1
U00096 Genomic DNA Translation: AAC73820.1
AP009048 Genomic DNA Translation: BAA35392.1
PIRiE64808 DEECOG
RefSeqiNP_415254.1, NC_000913.3
WP_001181473.1, NZ_STEB01000035.1

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
2JGDX-ray2.60A/B1-933[»]
SMRiP0AFG3
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi849680, 3 interactors
ComplexPortaliCPX-3921 2-oxoglutarate dehydrogenase complex
DIPiDIP-36225N
IntActiP0AFG3, 13 interactors
MINTiP0AFG3
STRINGi511145.b0726

2D gel databases

SWISS-2DPAGEiP0AFG3

Proteomic databases

EPDiP0AFG3
jPOSTiP0AFG3
PaxDbiP0AFG3
PRIDEiP0AFG3

Genome annotation databases

EnsemblBacteriaiAAC73820; AAC73820; b0726
BAA35392; BAA35392; BAA35392
GeneIDi945303
KEGGiecj:JW0715
eco:b0726
PATRICifig|1411691.4.peg.1547

Organism-specific databases

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

More...EchoBASEi		EB0972

Phylogenomic databases

eggNOGiENOG4105C7P Bacteria
COG0567 LUCA
HOGENOMiHOG000259587
InParanoidiP0AFG3
KOiK00164

Enzyme and pathway databases

BioCyciEcoCyc:E1O-MONOMER
ECOL316407:JW0715-MONOMER
MetaCyc:E1O-MONOMER
BRENDAi1.2.4.2 2026

Miscellaneous databases

EvolutionaryTraceiP0AFG3

Protein Ontology

More...PROi		PR:P0AFG3

Family and domain databases

Gene3Di3.40.50.11610, 1 hit
InterProiView protein in InterPro
IPR032106 2-oxogl_dehyd_N
IPR011603 2oxoglutarate_DH_E1
IPR001017 DH_E1
IPR031717 KGD_C
IPR042179 KGD_C_sf
IPR029061 THDP-binding
IPR005475 Transketolase-like_Pyr-bd
PANTHERiPTHR23152 PTHR23152, 1 hit
PfamiView protein in Pfam
PF16078 2-oxogl_dehyd_N, 1 hit
PF00676 E1_dh, 1 hit
PF16870 OxoGdeHyase_C, 1 hit
PF02779 Transket_pyr, 1 hit
PIRSFiPIRSF000157 Oxoglu_dh_E1, 1 hit
SMARTiView protein in SMART
SM00861 Transket_pyr, 1 hit
SUPFAMiSSF52518 SSF52518, 2 hits
TIGRFAMsiTIGR00239 2oxo_dh_E1, 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 nameiODO1_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: P0AFG3
Secondary accession number(s): P07015, P78225
<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: April 1, 1988
Last sequence update: December 20, 2005
Last modified: December 11, 2019
This is version 120 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 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, Reference proteome

Documents

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