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Entry version 114 (16 Oct 2019)
Sequence version 2 (28 Nov 2012)
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Protein

2-oxoglutarate dehydrogenase E1/E2 component

Gene

odhA

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
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 E1 and E2 reactions as part of 2-oxoglutarate dehydrogenase (ODH) activity, to convert 2-oxoglutarate to succinyl-CoA and CO2. OdhA has reductase activity with 2-oxoglutarate but does not react with pyruvate, and also displays transsuccinylase but no transacetylase activity. Since OdhA is not lipoylated, the succinyltransferase activity of its E2 domain is dependent on lipoyl residues of the acetyltransferase AceF.1 Publication

Miscellaneous

Is non-lipoylated. In contrast, the E2 component AceF is the prominent lipoylated protein in C.glutamicum.

<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

Protein has several cofactor binding sites:

<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 unphosphorylated OdhI, but not by phosphorylated OdhI.1 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

  1. KM=0.014 mM for 2-oxoglutarate1 Publication

    <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: tricarboxylic acid cycle

    This protein is involved in step 1 of the subpathway that synthesizes succinyl-CoA from 2-oxoglutarate (dehydrogenase route).
    Proteins known to be involved in this subpathway in this organism are:
    1. 2-oxoglutarate dehydrogenase E1/E2 component (odhA), Dihydrolipoyl dehydrogenase (lpd)
    This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinyl-CoA from 2-oxoglutarate (dehydrogenase route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei316Proton acceptor; for succinyltransferase activity1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei5832-oxoglutarateBy similarity1
    Binding sitei6082-oxoglutarateBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi645MagnesiumBy similarity1
    Metal bindingi678MagnesiumBy similarity1
    Metal bindingi680Magnesium; via carbonyl oxygenBy similarity1
    Binding sitei949Thiamine pyrophosphateBy similarity1
    Binding sitei10172-oxoglutarateBy 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 functionAcyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase
    Biological processTricarboxylic acid cycle
    LigandMagnesium, Metal-binding, Thiamine pyrophosphate

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    CORYNE:G18NG-10701-MONOMER
    GCF_000196335:G1EEA-1138-MONOMER

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

    More...
    UniPathwayi
    UPA00223;UER00997

    <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/E2 component
    Short name:
    ODH E1/E2 component
    Including the following 2 domains:
    2-oxoglutarate dehydrogenase E1 component (EC:1.2.4.22 Publications)
    Short name:
    ODH E1 component
    Alternative name(s):
    Alpha-ketoglutarate dehydrogenase E1 component
    Short name:
    KDH E1 component
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC:2.3.1.611 Publication)
    Alternative name(s):
    2-oxoglutarate dehydrogenase complex E2 component
    Short name:
    ODH E2 component
    Short name:
    OGDC-E2
    Dihydrolipoamide succinyltransferase
    <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:odhAImported
    Ordered Locus Names:Cgl1129, cg1280
    <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>OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
    <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 identifieri196627 [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 lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
    <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
    • UP000000582 <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

    <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

    Strains lacking this gene completely lack 2-oxoglutarate dehydrogenase activity. Deletion of odhA also causes L-glutamate overproduction and accumulation during growth.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>Mutagenesisi258T → A: Loss of E2 succinyltransferase activity, but nearly no effect on E1 dehydrogenase activity. 1 Publication1
    Mutagenesisi316H → C: Loss of E2 succinyltransferase activity, and 2-fold reduction in E1 dehydrogenase activity. 1 Publication1
    Mutagenesisi320Q → D: Slight reduction in E2 succinyltransferase activity and in E1 dehydrogenase activity. 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <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_00002735212 – 12212-oxoglutarate dehydrogenase E1/E2 componentAdd BLAST1220

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q8NRC3

    <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 (By similarity).

    Part of an unusual ODH/PDH supercomplex, consisting of AceE (E1), AceF (E2), and Lpd (E3) together with OdhA (E1+E2).

    Interacts with the FHA domain of unphosphorylated OdhI via its C-terminal dehydrogenase domain.

    By similarity2 Publications

    <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

    WithEntry#Exp.IntActNotes
    odhIQ8NQJ32EBI-7868591,EBI-7868645

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    Q8NRC3, 1 interactor

    Molecular INTeraction database

    More...
    MINTi
    Q8NRC3

    STRING: functional protein association networks

    More...
    STRINGi
    196627.cg1280

    <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
    Q8NRC3

    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

    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>Regioni2 – 402-oxoglutarate dehydrogenase E1, N-terminal partAdd BLAST39
    Regioni41 – 89LinkerAdd BLAST49
    Regioni90 – 337Succinyltransferase E2Add BLAST248
    Regioni338 – 12212-oxoglutarate dehydrogenase E1, C-terminal partAdd BLAST884
    Regioni543 – 544Thiamine pyrophosphate bindingBy similarity2
    Regioni608 – 610Thiamine pyrophosphate bindingBy similarity3
    Regioni645 – 647Thiamine pyrophosphate bindingBy similarity3

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    OdhA is a fusion protein with two major domains exhibiting structural features of an E1 and E2 protein, and a short sequence stretch of E1 localized at the N-terminus, which is connected by a linker region to the rest of the protein. Deletion of individual parts of odhA show that all parts of odhA are required for a functional tricarboxylic acid cycle in C.glutamicum; the ODH activity is in fact completely abolished in each of these mutants, and the PDH activity is significantly reduced, which could indicate that the overall structure of the supercomplex is disturbed.2 Publications

    <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 alpha-ketoglutarate dehydrogenase family.Curated
    In the C-terminal section; belongs to the 2-oxoacid dehydrogenase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105C7P Bacteria
    COG0508 LUCA
    COG0567 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000259587

    KEGG Orthology (KO)

    More...
    KOi
    K00164

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.559.10, 1 hit
    3.40.50.11610, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001078 2-oxoacid_DH_actylTfrase
    IPR032106 2-oxogl_dehyd_N
    IPR011603 2oxoglutarate_DH_E1
    IPR023213 CAT-like_dom_sf
    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
    PF00198 2-oxoacid_dh, 1 hit
    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.

    <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.

    Q8NRC3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSSASTFGQN AWLVDEMFQQ FQKDPKSVDK EWRELFEAQG GPNTTPATTE
    60 70 80 90 100
    AQPSAPKESA KPAPKAAPAA KAAPRVETKP ADKTAPKAKE SSVPQQPKLP
    110 120 130 140 150
    EPGQTPIRGI FKSIAKNMDI SLEIPTATSV RDMPARLMFE NRAMVNDQLK
    160 170 180 190 200
    RTRGGKISFT HIIGYAMVKA VMAHPDMNNS YDVIDGKPTL IVPEHINLGL
    210 220 230 240 250
    AIDLPQKDGS RALVVAAIKE TEKMNFSEFL AAYEDIVARS RKGKLTMDDY
    260 270 280 290 300
    QGVTVSLTNP GGIGTRHSVP RLTKGQGTII GVGSMDYPAE FQGASEDRLA
    310 320 330 340 350
    ELGVGKLVTI TSTYDHRVIQ GAVSGEFLRT MSRLLTDDSF WDEIFDAMNV
    360 370 380 390 400
    PYTPMRWAQD VPNTGVDKNT RVMQLIEAYR SRGHLIADTN PLSWVQPGMP
    410 420 430 440 450
    VPDHRDLDIE THNLTIWDLD RTFNVGGFGG KETMTLREVL SRLRAAYTLK
    460 470 480 490 500
    VGSEYTHILD RDERTWLQDR LEAGMPKPTQ AEQKYILQKL NAAEAFENFL
    510 520 530 540 550
    QTKYVGQKRF SLEGAEALIP LMDSAIDTAA GQGLDEVVIG MPHRGRLNVL
    560 570 580 590 600
    FNIVGKPLAS IFNEFEGQME QGQIGGSGDV KYHLGSEGQH LQMFGDGEIK
    610 620 630 640 650
    VSLTANPSHL EAVNPVMEGI VRAKQDYLDK GVDGKTVVPL LLHGDAAFAG
    660 670 680 690 700
    LGIVPETINL AKLRGYDVGG TIHIVVNNQI GFTTTPDSSR SMHYATDYAK
    710 720 730 740 750
    AFGCPVFHVN GDDPEAVVWV GQLATEYRRR FGKDVFIDLV CYRLRGHNEA
    760 770 780 790 800
    DDPSMTQPKM YELITGRETV RAQYTEDLLG RGDLSNEDAE AVVRDFHDQM
    810 820 830 840 850
    ESVFNEVKEG GKKQAEAQTG ITGSQKLPHG LETNISREEL LELGQAFANT
    860 870 880 890 900
    PEGFNYHPRV APVAKKRVSS VTEGGIDWAW GELLAFGSLA NSGRLVRLAG
    910 920 930 940 950
    EDSRRGTFTQ RHAVAIDPAT AEEFNPLHEL AQSKGNNGKF LVYNSALTEY
    960 970 980 990 1000
    AGMGFEYGYS VGNEDSIVAW EAQFGDFANG AQTIIDEYVS SGEAKWGQTS
    1010 1020 1030 1040 1050
    KLILLLPHGY EGQGPDHSSA RIERFLQLCA EGSMTVAQPS TPANHFHLLR
    1060 1070 1080 1090 1100
    RHALSDLKRP LVIFTPKSML RNKAAASAPE DFTEVTKFQS VINDPNVADA
    1110 1120 1130 1140 1150
    AKVKKVMLVS GKLYYELAKR KEKDGRDDIA IVRIEMLHPI PFNRISEALA
    1160 1170 1180 1190 1200
    GYPNAEEVLF VQDEPANQGP WPFYQEHLPE LIPNMPKMRR VSRRAQSSTA
    1210 1220
    TGVAKVHQLE EKQLIDEAFE A
    Length:1,221
    Mass (Da):134,664
    Last modified:November 28, 2012 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBF0A1827EA1B0080
    GO

    <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 BAB98522 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
    The sequence CAF19835 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.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 conflicti44T → A in BAA12222 (PubMed:9004499).Curated1
    Sequence conflicti82D → A in BAA12222 (PubMed:9004499).Curated1
    Sequence conflicti238A → T in BAA12222 (PubMed:9004499).Curated1
    Sequence conflicti413N → S in BAA12222 (PubMed:9004499).Curated1
    Sequence conflicti424N → S in BAA12222 (PubMed:9004499).Curated1
    Sequence conflicti967I → V in BAA12222 (PubMed:9004499).Curated1
    Sequence conflicti1093N → D in BAA12222 (PubMed:9004499).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
    D84102 Genomic DNA Translation: BAA12222.2
    BA000036 Genomic DNA Translation: BAB98522.1 Different initiation.
    BX927151 Genomic DNA Translation: CAF19835.1 Different initiation.

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_600357.3, NC_003450.3
    WP_011014138.1, NC_006958.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    BAB98522; BAB98522; BAB98522
    CAF19835; CAF19835; cg1280

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    1019114

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    cgb:cg1280
    cgl:NCgl1084

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|196627.13.peg.1108

    <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
    D84102 Genomic DNA Translation: BAA12222.2
    BA000036 Genomic DNA Translation: BAB98522.1 Different initiation.
    BX927151 Genomic DNA Translation: CAF19835.1 Different initiation.
    RefSeqiNP_600357.3, NC_003450.3
    WP_011014138.1, NC_006958.1

    3D structure databases

    SMRiQ8NRC3
    ModBaseiSearch...

    Protein-protein interaction databases

    IntActiQ8NRC3, 1 interactor
    MINTiQ8NRC3
    STRINGi196627.cg1280

    Proteomic databases

    PRIDEiQ8NRC3

    Genome annotation databases

    EnsemblBacteriaiBAB98522; BAB98522; BAB98522
    CAF19835; CAF19835; cg1280
    GeneIDi1019114
    KEGGicgb:cg1280
    cgl:NCgl1084
    PATRICifig|196627.13.peg.1108

    Phylogenomic databases

    eggNOGiENOG4105C7P Bacteria
    COG0508 LUCA
    COG0567 LUCA
    HOGENOMiHOG000259587
    KOiK00164

    Enzyme and pathway databases

    UniPathwayiUPA00223;UER00997
    BioCyciCORYNE:G18NG-10701-MONOMER
    GCF_000196335:G1EEA-1138-MONOMER

    Family and domain databases

    Gene3Di3.30.559.10, 1 hit
    3.40.50.11610, 1 hit
    InterProiView protein in InterPro
    IPR001078 2-oxoacid_DH_actylTfrase
    IPR032106 2-oxogl_dehyd_N
    IPR011603 2oxoglutarate_DH_E1
    IPR023213 CAT-like_dom_sf
    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
    PF00198 2-oxoacid_dh, 1 hit
    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 nameiODO12_CORGL
    <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: Q8NRC3
    Secondary accession number(s): P96746, Q6M641
    <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: January 23, 2007
    Last sequence update: November 28, 2012
    Last modified: October 16, 2019
    This is version 114 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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