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Entry version 108 (02 Jun 2021)
Sequence version 1 (09 Jan 2007)
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Protein

Multifunctional 2-oxoglutarate metabolism enzyme

Gene

kgd

Organism
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
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

Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle.

2 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

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Alpha-ketoglutarate dehydrogenase and decarboxylase activities are inhibited by unphosphorylated GarA, and allosterically activated by acetyl-CoA, the main substrate of the TCA cycle. Both the phosphoadenosine and acetyl moieties of acetyl-CoA are important for activation because neither CoA nor the synthetic compound S-(2-acetamidoethyl)-ethanethioate (which mimics the terminal acetyl-phosphopantetheine group of acetyl-CoA) has an activation effect.2 Publications

<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=0.54 mM for alpha-ketoglutarate1 Publication

    <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: tricarboxylic acid cycle

    This protein is involved in step 1 of the subpathway that synthesizes succinate from 2-oxoglutarate (transferase route).1 Publication 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 succinate from 2-oxoglutarate (transferase route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

    Pathwayi: tricarboxylic acid cycle

    This protein is involved in step 1 of the subpathway that synthesizes succinyl-CoA from 2-oxoglutarate (dehydrogenase route).1 Publication 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%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 sitei314Proton acceptor; for succinyltransferase activityBy similarity1
    <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 sitei5792-oxoglutarate1
    Binding sitei6042-oxoglutarate1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi645Magnesium1
    Metal bindingi678Magnesium1
    Metal bindingi680Magnesium; via carbonyl oxygen1
    Binding sitei952Thiamine pyrophosphate1
    Binding sitei10202-oxoglutarate1
    Binding sitei1038Allosteric activator1
    Binding sitei1054Allosteric activator1
    Binding sitei1142Allosteric activator1

    <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, Allosteric enzyme, Decarboxylase, Lyase, 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
    MSME246196:G1H7P-5022-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.1.1.71, 3512

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    A0R2B1

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

    More...
    UniPathwayi
    UPA00223;UER00997
    UPA00223;UER01001

    <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:
    Multifunctional 2-oxoglutarate metabolism enzyme
    Alternative name(s):
    2-hydroxy-3-oxoadipate synthase (EC:2.2.1.5)
    Short name:
    HOA synthase
    Short name:
    HOAS
    2-oxoglutarate carboxy-lyase
    2-oxoglutarate decarboxylase
    Alpha-ketoglutarate decarboxylase (EC:4.1.1.71)
    Short name:
    KG decarboxylase
    Short name:
    KGD
    Alpha-ketoglutarate-glyoxylate carboligase
    Including the following 2 domains:
    2-oxoglutarate dehydrogenase E1 component (EC:1.2.4.2)
    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:2.3.1.61)
    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%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:kgd
    Synonyms:sucA
    Ordered Locus Names:MSMEG_5049, MSMEI_4922
    <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>OrganismiMycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
    <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 identifieri246196 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycolicibacterium
    <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
    • UP000006158 <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
    • UP000000757 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

    Cells lacking this gene do not show any ODH activity, in contrast to wild-type, demonstrating that this protein is part of a functional ODH complex in mycobacteria.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi539H → A: Loss of KG decarboxylase activity. 1 Publication1
    Mutagenesisi579H → A: Loss of KG decarboxylase activity. 1 Publication1
    Mutagenesisi747H → A: 40-fold decrease in KG decarboxylase activity. 1 Publication1
    Mutagenesisi781R → A: Increase in KG decarboxylase activity. 1 Publication1
    Mutagenesisi1020H → A: Loss of KG decarboxylase activity. 1 Publication1
    Mutagenesisi1034E → A: Loss of activation by acetyl-CoA. 1 Publication1
    Mutagenesisi1062R → A: Loss of activation by acetyl-CoA. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003107181 – 1227Multifunctional 2-oxoglutarate metabolism enzymeAdd BLAST1227

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    A0R2B1

    <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.

    Interacts with the FHA domain of unphosphorylated GarA. The 2-oxoglutarate dehydrogenase (ODH) complex contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

    2 Publications

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    A0R2B1, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    246196.MSMEI_4922

    <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

    11227
    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
    A0R2B1

    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
    A0R2B1

    <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>Regioni1 – 412-oxoglutarate dehydrogenase E1, N-terminal partAdd BLAST41
    Regioni23 – 102DisorderedSequence analysisAdd BLAST80
    Regioni42 – 88LinkerAdd BLAST47
    Regioni89 – 335Succinyltransferase E2Add BLAST247
    Regioni336 – 12272-oxoglutarate dehydrogenase E1, C-terminal partAdd BLAST892
    Regioni539 – 540Thiamine pyrophosphate binding2
    Regioni604 – 606Thiamine pyrophosphate binding3
    Regioni645 – 647Thiamine pyrophosphate binding3
    Regioni1089 – 1092Allosteric activator4
    Regioni1149 – 1150Allosteric activator2

    Coiled coil

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili783 – 814Sequence analysisAdd BLAST32

    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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi43 – 59Polar residuesSequence analysisAdd BLAST17
    Compositional biasi60 – 76Pro residuesSequence analysisAdd BLAST17

    <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

    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.By similarity

    <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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0508, Bacteria
    COG0567, Bacteria

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    RDSYCRT

    Database of Orthologous Groups

    More...
    OrthoDBi
    29166at2

    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%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.

    A0R2B1-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSSSPSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY SPEPTTDSAS
    60 70 80 90 100
    NGRTTTAAPV TPPTPAPAPA PEPKAAPKPA AKTEAKPAKP AKSATPAKGD
    110 120 130 140 150
    ESQILRGAAA AVVKNMNASL EVPTATSVRA IPAKLMIDNR VVINNHLKRT
    160 170 180 190 200
    RGGKISFTHL LGYAIVQAVK KFPNMNRHFA VVDGKPTAIT PAHTNLGLAI
    210 220 230 240 250
    DLQGKDGNRS LVVAAIKRCE TMRFGQFIAA YEDIVRRARD GKLTAEDFSG
    260 270 280 290 300
    VTISLTNPGT LGTVHSVPRL MQGQGAIIGA GAMEYPAEFQ GASEERIADL
    310 320 330 340 350
    GIGKLITLTS TYDHRIIQGA ESGDFLRTIH QLLLDDDFFD EIFRELGIPY
    360 370 380 390 400
    EPVRWRTDNP DSIEDKNARV IELIAAYRNR GHLMADIDPL RLDNTRFRSH
    410 420 430 440 450
    PDLDVNSHGL TLWDLDREFK VDGFAGVQRK KLRDILSVLR DAYCRHVGVE
    460 470 480 490 500
    YTHILEPEQQ RWIQERVETK HDKPTVAEQK YILSKLNAAE AFETFLQTKY
    510 520 530 540 550
    VGQKRFSLEG AETVIPMMDA VIDQCAEHGL DEVVIAMPHR GRLNVLANIV
    560 570 580 590 600
    GKPYSQIFSE FEGNLNPSQA HGSGDVKYHL GATGTYIQMF GDNDIEVSLT
    610 620 630 640 650
    ANPSHLEAVD PVLEGLVRAK QDLLDTGEEG SDNRFSVVPL MLHGDAAFAG
    660 670 680 690 700
    QGVVAETLNL ALLRGYRTGG TIHIVVNNQI GFTTAPTDSR SSEYCTDVAK
    710 720 730 740 750
    MIGAPIFHVN GDDPEACAWV ARLAVDFRQA FKKDVVIDML CYRRRGHNEG
    760 770 780 790 800
    DDPSMTQPYM YDVIDTKRGS RKAYTEALIG RGDISMKEAE DALRDYQGQL
    810 820 830 840 850
    ERVFNEVREL EKHEIEPSES VEADQQIPSK LATAVDKAML QRIGDAHLAL
    860 870 880 890 900
    PEGFTVHPRV RPVLEKRREM AYEGRIDWAF AELLALGSLI AEGKLVRLSG
    910 920 930 940 950
    QDTQRGTFTQ RHAVIVDRKT GEEFTPLQLL ATNPDGTPTG GKFLVYNSAL
    960 970 980 990 1000
    SEFAAVGFEY GYSVGNPDAM VLWEAQFGDF VNGAQSIIDE FISSGEAKWG
    1010 1020 1030 1040 1050
    QLSDVVLLLP HGHEGQGPDH TSGRIERFLQ LWAEGSMTIA MPSTPANYFH
    1060 1070 1080 1090 1100
    LLRRHGKDGI QRPLIVFTPK SMLRNKAAVS DIRDFTESKF RSVLEEPMYT
    1110 1120 1130 1140 1150
    DGEGDRNKVT RLLLTSGKIY YELAARKAKE NREDVAIVRI EQLAPLPRRR
    1160 1170 1180 1190 1200
    LAETLDRYPN VKEKFWVQEE PANQGAWPSF GLTLPEILPD HFTGLKRISR
    1210 1220
    RAMSAPSSGS SKVHAVEQQE ILDTAFG
    Length:1,227
    Mass (Da):135,944
    Last modified:January 9, 2007 - 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:i76C5BFFD1638A391
    GO

    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
    CP000480 Genomic DNA Translation: ABK74238.1
    CP001663 Genomic DNA Translation: AFP41366.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_011730279.1, NZ_SIJM01000019.1
    YP_889299.1, NC_008596.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    ABK74238; ABK74238; MSMEG_5049
    AFP41366; AFP41366; MSMEI_4922

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    msg:MSMEI_4922
    msm:MSMEG_5049

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|246196.19.peg.4927

    <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
    CP000480 Genomic DNA Translation: ABK74238.1
    CP001663 Genomic DNA Translation: AFP41366.1
    RefSeqiWP_011730279.1, NZ_SIJM01000019.1
    YP_889299.1, NC_008596.1

    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
    2XT6X-ray2.74A/B116-1227[»]
    2XTAX-ray2.20A/B/C/D361-1227[»]
    2Y0PX-ray2.40A/B/C/D361-1227[»]
    2YICX-ray1.96A/B/C/D361-1227[»]
    2YIDX-ray2.25A/B/C/D361-1227[»]
    3ZHQX-ray2.50A/B/C/D361-1227[»]
    3ZHRX-ray2.10A/B/C/D361-1227[»]
    3ZHSX-ray2.10A/B/C/D361-1227[»]
    3ZHTX-ray2.15A/B/C/D361-1227[»]
    3ZHUX-ray2.30A/B/C/D361-1227[»]
    3ZHVX-ray2.30A/B/C/D361-1227[»]
    6I2QX-ray2.15A361-1227[»]
    6I2RX-ray2.20A/C361-1227[»]
    6I2SX-ray2.40A361-1227[»]
    6R29X-ray1.67A/B361-1227[»]
    6R2AX-ray1.70A/B361-1227[»]
    6R2BX-ray1.96A/B/C/D361-1227[»]
    6R2CX-ray2.09A/B/C/D361-1227[»]
    6R2DX-ray2.30A/B/C/D361-1227[»]
    SMRiA0R2B1
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    IntActiA0R2B1, 1 interactor
    STRINGi246196.MSMEI_4922

    Proteomic databases

    PRIDEiA0R2B1

    Genome annotation databases

    EnsemblBacteriaiABK74238; ABK74238; MSMEG_5049
    AFP41366; AFP41366; MSMEI_4922
    KEGGimsg:MSMEI_4922
    msm:MSMEG_5049
    PATRICifig|246196.19.peg.4927

    Phylogenomic databases

    eggNOGiCOG0508, Bacteria
    COG0567, Bacteria
    OMAiRDSYCRT
    OrthoDBi29166at2

    Enzyme and pathway databases

    UniPathwayiUPA00223;UER00997
    UPA00223;UER01001
    BioCyciMSME246196:G1H7P-5022-MONOMER
    BRENDAi4.1.1.71, 3512
    SABIO-RKiA0R2B1

    Miscellaneous databases

    EvolutionaryTraceiA0R2B1

    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

    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 nameiKGD_MYCS2
    <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: A0R2B1
    Secondary accession number(s): I7GDF5
    <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: November 13, 2007
    Last sequence update: January 9, 2007
    Last modified: June 2, 2021
    This is version 108 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. 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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