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Q73WX4

- KGD_MYCPA

UniProt

Q73WX4 - KGD_MYCPA

Protein

Multifunctional 2-oxoglutarate metabolism enzyme

Gene

kgd

Organism
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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 By similarity.By similarity

    Catalytic activityi

    2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2.
    2-oxoglutarate = succinate semialdehyde + CO2.
    2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.
    Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

    Cofactori

    Magnesium.By similarity
    Thiamine pyrophosphate.By similarity

    Enzyme 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.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei332 – 3321Proton acceptor; for succinyltransferase activityBy similarity
    Binding sitei597 – 59712-oxoglutarateBy similarity
    Binding sitei622 – 62212-oxoglutarateBy similarity
    Metal bindingi665 – 6651MagnesiumBy similarity
    Metal bindingi698 – 6981MagnesiumBy similarity
    Metal bindingi700 – 7001Magnesium; via carbonyl oxygenBy similarity
    Binding sitei972 – 9721Thiamine pyrophosphateBy similarity
    Binding sitei1040 – 104012-oxoglutarateBy similarity
    Binding sitei1058 – 10581Allosteric activatorBy similarity
    Binding sitei1074 – 10741Allosteric activatorBy similarity
    Binding sitei1162 – 11621Allosteric activatorBy similarity

    GO - Molecular functioni

    1. 2-hydroxy-3-oxoadipate synthase activity Source: UniProtKB-EC
    2. 2-oxoglutarate decarboxylase activity Source: UniProtKB-EC
    3. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC
    4. metal ion binding Source: UniProtKB-KW
    5. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB-EC
    6. thiamine pyrophosphate binding Source: InterPro

    GO - Biological processi

    1. tricarboxylic acid cycle Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Acyltransferase, Decarboxylase, Lyase, Oxidoreductase, Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    Magnesium, Metal-binding, Thiamine pyrophosphate

    Enzyme and pathway databases

    BioCyciMAVI262316:GCQR-2572-MONOMER.
    UniPathwayiUPA00223; UER00997.
    UPA00223; UER01001.

    Names & Taxonomyi

    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
    Gene namesi
    Name:kgd
    Ordered Locus Names:MAP_2536
    OrganismiMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
    Taxonomic identifieri262316 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)
    ProteomesiUP000000580: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12471247Multifunctional 2-oxoglutarate metabolism enzymePRO_0000310717Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer. 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.By similarity

    Protein-protein interaction databases

    STRINGi262316.MAP2536.

    Structurei

    3D structure databases

    ProteinModelPortaliQ73WX4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 41412-oxoglutarate dehydrogenase E1, N-terminal partAdd
    BLAST
    Regioni42 – 10463LinkerAdd
    BLAST
    Regioni105 – 353249Succinyltransferase E2Add
    BLAST
    Regioni354 – 12478942-oxoglutarate dehydrogenase E1, C-terminal partAdd
    BLAST
    Regioni557 – 5582Thiamine pyrophosphate bindingBy similarity
    Regioni622 – 6243Thiamine pyrophosphate bindingBy similarity
    Regioni665 – 6673Thiamine pyrophosphate bindingBy similarity
    Regioni1109 – 11124Allosteric activatorBy similarity
    Regioni1169 – 11702Allosteric activatorBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili803 – 83331Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi51 – 12979Ala-richAdd
    BLAST

    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

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0508.
    KOiK01616.
    OMAiQIDKEAR.
    OrthoDBiEOG6V1M1F.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    3.40.50.970. 2 hits.
    InterProiIPR001078. 2-oxoacid_DH_actylTfrase.
    IPR011603. 2oxoglutarate_DH_E1.
    IPR023213. CAT-like_dom.
    IPR001017. DH_E1.
    IPR029061. THDP-binding.
    IPR005475. Transketolase-like_Pyr-bd.
    [Graphical view]
    PANTHERiPTHR23152. PTHR23152. 1 hit.
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00676. E1_dh. 1 hit.
    PF02779. Transket_pyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
    SMARTiSM00861. Transket_pyr. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 2 hits.
    TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q73WX4-1 [UniParc]FASTAAdd to Basket

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    MSNISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY NPEPTGDSVL     50
    AAPASTDGPS APAPAAPQTA QPALPAQTAP PAQTAQPARP APQPAAAPGN 100
    GASTRPAKPA TPPPAEGDEL QTLRGAAAAV VKNMSASLEV PTATSVRAIP 150
    AKLLIDNRIV INNQLKRTRG GKISFTHLLG YALVQAIKKF PNMNRHYAEI 200
    DGKPTAITPA HTNLGLAIDL QGKDGKRSLV VAGIKNCETM RFAQFVTAYE 250
    DIVRRARDGK LTAEDFAGVT ISLTNPGTIG TVHSVPRLMN GQGAIIGVGA 300
    MEYPAEFQGA SEERIAELGI GKLITLTSTY DHRIIQGAES GDFLRTIHEM 350
    LLSDGFWDDI FRELSIPYLP IRWSTDNPDS IVDKNARVME LIAAYRNRGH 400
    LMADIDPLRL DGSRFRSHPD LEILNHGLTL WDLDRVFKVN GFAGAEYKKL 450
    RDILGLLRDA YCRHIGVEYT HILDPEQQEW LQQRVETKHV KPTVAEQKFI 500
    LSKLNAAEAF ETFLQTKYVG QKRFSLEGAE SVIPMMDAAI DQCAEHGLDE 550
    VVIGMPHRGR LNVLANIVGK PYSQIFSEFE GNLNPAQAHG SGDVKYHLGA 600
    TGVYLQMFGD NDIQVSLTAN PSHLEAVDPV LEGLVRAKQD LLDHGADDQG 650
    DEKAFSVVPM MLHGDAAFAG QGVVAETLNL THLPGYRVGG TIHIIVNNQI 700
    GFTTAPEHSR SSEYCTDVAK MIGAPIFHVN GDDPEACAWV AKLAVDFRQK 750
    FKKDVVIDML CYRKRGHNEG DDPSMTNPAM YDVVDIKRGV RKSYTEALIG 800
    RGDISMKEAE DALRDYQGQL ERVFNEVREL EKHGVGPSES VEADQMLPAG 850
    LATAVDKALL ARIGDAFLAL PEGFTAHPRV QPVLEKRREM AYEGKIDWAF 900
    AELLALGSLV AGGKLVRLSG QDTRRGTFSQ RHSVIIDRNT GEEFTPLQLL 950
    ATNPDGTPTG GKFLVYDSPL SEYAAVGFEY GYTVGNPDAL VLWEAQFGDF 1000
    VNGAQSIIDE FISSGEAKWG QLSNVVLLLP HGHEGQGPDH TSARIERFLQ 1050
    LWAEGSMTIA MPSTPSNYFH LLRRHALDGI KRPLIVFTPK SMLRNKAAVS 1100
    DIKDFTEIKF RSVLEEPTYE DGIGDRGKVS RVLLTSGKLY YELVARKNKD 1150
    NRDDVAIVRI EQLAPLPKRR LGETLDRYPN VREYFWVQEE PANQGAWPRF 1200
    GLELPELLPD KLTGLKRISR RAMSAPSSGS SKVHAVEQQE IIDTAFA 1247
    Length:1,247
    Mass (Da):137,073
    Last modified:July 5, 2004 - v1
    Checksum:iD31E9876D146519A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016958 Genomic DNA. Translation: AAS04853.1.
    RefSeqiNP_961470.1. NC_002944.2.

    Genome annotation databases

    EnsemblBacteriaiAAS04853; AAS04853; MAP_2536.
    GeneIDi2719042.
    KEGGimpa:MAP2536.
    PATRICi17997756. VBIMycAvi108102_2692.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016958 Genomic DNA. Translation: AAS04853.1 .
    RefSeqi NP_961470.1. NC_002944.2.

    3D structure databases

    ProteinModelPortali Q73WX4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 262316.MAP2536.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS04853 ; AAS04853 ; MAP_2536 .
    GeneIDi 2719042.
    KEGGi mpa:MAP2536.
    PATRICi 17997756. VBIMycAvi108102_2692.

    Phylogenomic databases

    eggNOGi COG0508.
    KOi K01616.
    OMAi QIDKEAR.
    OrthoDBi EOG6V1M1F.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00997 .
    UPA00223 ; UER01001 .
    BioCyci MAVI262316:GCQR-2572-MONOMER.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    3.40.50.970. 2 hits.
    InterProi IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR011603. 2oxoglutarate_DH_E1.
    IPR023213. CAT-like_dom.
    IPR001017. DH_E1.
    IPR029061. THDP-binding.
    IPR005475. Transketolase-like_Pyr-bd.
    [Graphical view ]
    PANTHERi PTHR23152. PTHR23152. 1 hit.
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00676. E1_dh. 1 hit.
    PF02779. Transket_pyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
    SMARTi SM00861. Transket_pyr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 2 hits.
    TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
      Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
      Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-968 / K-10.

    Entry informationi

    Entry nameiKGD_MYCPA
    AccessioniPrimary (citable) accession number: Q73WX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

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

    External Data

    Dasty 3