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Entry version 35 (16 Oct 2019)
Sequence version 1 (16 Apr 2014)
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Protein

Multifunctional 2-oxoglutarate metabolism enzyme

Gene

kgd

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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, which can endow M.tuberculosis with the metabolic plasticity required for growth on diverse host-derived carbon sources. Appears to play a predominant role in growth on carbohydrates as the sole carbon source, and only a minimal role during growth on fatty acids.4 Publications

Caution

Was originally (PubMed:9634230 and PubMed:12218036) annotated as sucA because of sequence similarity, but this protein was shown (PubMed:16045627) not to be able to serve as the E1 component of 2-oxoglutarate dehydrogenase (ODH). However, it was later shown that this protein does in fact sustain ODH activity (PubMed:21867916), and requires specific activation by acetyl-CoA.2 Publications

<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

Alpha-ketoglutarate dehydrogenase and decarboxylase activities are inhibited by unphosphorylated GarA, and allosterically activated by acetyl-CoA, the main substrate of the TCA cycle.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=0.48 mM for 2-oxoglutarate1 Publication
  2. KM=0.196 mM for magnesium ions1 Publication
  3. KM=0.019 mM for thiamine pyrophosphate1 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 succinate from 2-oxoglutarate (transferase route).
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Multifunctional 2-oxoglutarate metabolism enzyme (kgd)
    2. no protein annotated in this organism
    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).
    Proteins known to be involved in this subpathway in this organism are:
    1. Multifunctional 2-oxoglutarate metabolism enzyme (kgd)
    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 activityBy similarity1
    <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 sitei5812-oxoglutarateBy similarity1
    Binding sitei6062-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 bindingi649MagnesiumBy similarity1
    Metal bindingi682MagnesiumBy similarity1
    Metal bindingi684Magnesium; via carbonyl oxygenBy similarity1
    Binding sitei956Thiamine pyrophosphateBy similarity1
    Binding sitei10242-oxoglutarateBy similarity1
    Binding sitei1042Allosteric activatorBy similarity1
    Binding sitei1058Allosteric activatorBy similarity1
    Binding sitei1146Allosteric activatorBy 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, 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
    MetaCyc:G185E-5419-MONOMER
    MTBH37RV:G185E-5419-MONOMER

    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_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:
    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_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:kgd
    Ordered Locus Names:Rv1248c
    <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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    <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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    <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
    • UP000001584 <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

    Organism-specific databases

    Mycobacterium tuberculosis strain H37Rv genome database

    More...
    TubercuListi
    Rv1248c

    <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

    <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

    Attempts to disrupt Rv1248c in M.tuberculosis H37Rv and Erdman strains by homologous recombination were unsuccessful, raising the possibility that Rv1248c may be essential (PubMed:20416504). However, deletion mutants were readily obtained in a strain derived from H37Rv in PubMed:19936047. The mutant strain grows as well as wild-type in medium containing both carbohydrates (dextrose and glycerol) and fatty acids, under a CO2 enriched atmosphere, but shows a marked growth defect when grown in medium containing carbohydrates as the sole carbon source in the presence of CO2. Simultaneous disruption of korAB and kgd results in strict dependence upon the glyoxylate shunt for growth. Growth of the kgd mutant strain on fatty acids as the sole carbon source is similar to that of the wild type strain regardless of the presence of CO2. But cells lacking both korAB and kgd is significantly more retarded for growth on fatty acids than is either korAB or kgd deleted mutant alone.2 Publications

    <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_00003107221 – 1231Multifunctional 2-oxoglutarate metabolism enzymeAdd BLAST1231

    Proteomic databases

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

    More...
    PaxDbi
    P9WIS5

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P9WIS5

    <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). The 2-oxoglutarate dehydrogenase (ODH) complex contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).

    Interacts with the FHA domain of unphosphorylated GarA.

    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
    P9WJA94EBI-6405560,EBI-6405522

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    P9WIS5, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    83332.Rv1248c

    <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
    P9WIS5

    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>Regioni1 – 412-oxoglutarate dehydrogenase E1, N-terminal partAdd BLAST41
    Regioni42 – 88LinkerAdd BLAST47
    Regioni89 – 337Succinyltransferase E2Add BLAST249
    Regioni338 – 12312-oxoglutarate dehydrogenase E1, C-terminal partAdd BLAST894
    Regioni541 – 542Thiamine pyrophosphate bindingBy similarity2
    Regioni606 – 608Thiamine pyrophosphate bindingBy similarity3
    Regioni649 – 651Thiamine pyrophosphate bindingBy similarity3
    Regioni1093 – 1096Allosteric activatorBy similarity4
    Regioni1153 – 1154Allosteric activatorBy similarity2

    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 coili787 – 817Sequence analysisAdd BLAST31

    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 biasi61 – 113Ala-richAdd BLAST53

    <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
    ENOG4105C7P Bacteria
    COG0508 LUCA
    COG0567 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K01616

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    RDSYCRT

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P9WIS5

    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.

    P9WIS5-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MANISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY SPEPTSQPAA
    60 70 80 90 100
    EPTRVTSPLV AERAAAAAPQ APPKPADTAA AGNGVVAALA AKTAVPPPAE
    110 120 130 140 150
    GDEVAVLRGA AAAVVKNMSA SLEVPTATSV RAVPAKLLID NRIVINNQLK
    160 170 180 190 200
    RTRGGKISFT HLLGYALVQA VKKFPNMNRH YTEVDGKPTA VTPAHTNLGL
    210 220 230 240 250
    AIDLQGKDGK RSLVVAGIKR CETMRFAQFV TAYEDIVRRA RDGKLTTEDF
    260 270 280 290 300
    AGVTISLTNP GTIGTVHSVP RLMPGQGAII GVGAMEYPAE FQGASEERIA
    310 320 330 340 350
    ELGIGKLITL TSTYDHRIIQ GAESGDFLRT IHELLLSDGF WDEVFRELSI
    360 370 380 390 400
    PYLPVRWSTD NPDSIVDKNA RVMNLIAAYR NRGHLMADTD PLRLDKARFR
    410 420 430 440 450
    SHPDLEVLTH GLTLWDLDRV FKVDGFAGAQ YKKLRDVLGL LRDAYCRHIG
    460 470 480 490 500
    VEYAHILDPE QKEWLEQRVE TKHVKPTVAQ QKYILSKLNA AEAFETFLQT
    510 520 530 540 550
    KYVGQKRFSL EGAESVIPMM DAAIDQCAEH GLDEVVIGMP HRGRLNVLAN
    560 570 580 590 600
    IVGKPYSQIF TEFEGNLNPS QAHGSGDVKY HLGATGLYLQ MFGDNDIQVS
    610 620 630 640 650
    LTANPSHLEA VDPVLEGLVR AKQDLLDHGS IDSDGQRAFS VVPLMLHGDA
    660 670 680 690 700
    AFAGQGVVAE TLNLANLPGY RVGGTIHIIV NNQIGFTTAP EYSRSSEYCT
    710 720 730 740 750
    DVAKMIGAPI FHVNGDDPEA CVWVARLAVD FRQRFKKDVV IDMLCYRRRG
    760 770 780 790 800
    HNEGDDPSMT NPYVYDVVDT KRGARKSYTE ALIGRGDISM KEAEDALRDY
    810 820 830 840 850
    QGQLERVFNE VRELEKHGVQ PSESVESDQM IPAGLATAVD KSLLARIGDA
    860 870 880 890 900
    FLALPNGFTA HPRVQPVLEK RREMAYEGKI DWAFGELLAL GSLVAEGKLV
    910 920 930 940 950
    RLSGQDSRRG TFSQRHSVLI DRHTGEEFTP LQLLATNSDG SPTGGKFLVY
    960 970 980 990 1000
    DSPLSEYAAV GFEYGYTVGN PDAVVLWEAQ FGDFVNGAQS IIDEFISSGE
    1010 1020 1030 1040 1050
    AKWGQLSNVV LLLPHGHEGQ GPDHTSARIE RFLQLWAEGS MTIAMPSTPS
    1060 1070 1080 1090 1100
    NYFHLLRRHA LDGIQRPLIV FTPKSMLRHK AAVSEIKDFT EIKFRSVLEE
    1110 1120 1130 1140 1150
    PTYEDGIGDR NKVSRILLTS GKLYYELAAR KAKDNRNDLA IVRLEQLAPL
    1160 1170 1180 1190 1200
    PRRRLRETLD RYENVKEFFW VQEEPANQGA WPRFGLELPE LLPDKLAGIK
    1210 1220 1230
    RISRRAMSAP SSGSSKVHAV EQQEILDEAF G
    Length:1,231
    Mass (Da):135,902
    Last modified:April 16, 2014 - 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:i96C255612BA12889
    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
    AL123456 Genomic DNA Translation: CCP44004.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    G70953

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_215764.2, NC_000962.3
    WP_003898790.1, NZ_NVQJ01000049.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

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    EnsemblBacteriai
    CCP44004; CCP44004; Rv1248c

    Database of genes from NCBI RefSeq genomes

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    GeneIDi
    887084

    KEGG: Kyoto Encyclopedia of Genes and Genomes

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    KEGGi
    mtu:Rv1248c
    mtv:RVBD_1248c

    <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
    AL123456 Genomic DNA Translation: CCP44004.1
    PIRiG70953
    RefSeqiNP_215764.2, NC_000962.3
    WP_003898790.1, NZ_NVQJ01000049.1

    3D structure databases

    SMRiP9WIS5
    ModBaseiSearch...

    Protein-protein interaction databases

    IntActiP9WIS5, 1 interactor
    STRINGi83332.Rv1248c

    Proteomic databases

    PaxDbiP9WIS5
    PRIDEiP9WIS5

    Genome annotation databases

    EnsemblBacteriaiCCP44004; CCP44004; Rv1248c
    GeneIDi887084
    KEGGimtu:Rv1248c
    mtv:RVBD_1248c

    Organism-specific databases

    TubercuListiRv1248c

    Phylogenomic databases

    eggNOGiENOG4105C7P Bacteria
    COG0508 LUCA
    COG0567 LUCA
    KOiK01616
    OMAiRDSYCRT
    PhylomeDBiP9WIS5

    Enzyme and pathway databases

    UniPathwayiUPA00223;UER00997
    UPA00223;UER01001
    BioCyciMetaCyc:G185E-5419-MONOMER
    MTBH37RV:G185E-5419-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

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    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 nameiKGD_MYCTU
    <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: P9WIS5
    Secondary accession number(s): L0T8T9, O50463, Q7D8I9
    <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 16, 2014
    Last sequence update: April 16, 2014
    Last modified: October 16, 2019
    This is version 35 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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