Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A1TDK2

- KGD_MYCVP

UniProt

A1TDK2 - KGD_MYCVP

Protein

Multifunctional 2-oxoglutarate metabolism enzyme

Gene

kgd

Organism
Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 bindingi661 – 6611MagnesiumBy similarity
    Metal bindingi694 – 6941MagnesiumBy similarity
    Metal bindingi696 – 6961Magnesium; via carbonyl oxygenBy similarity
    Binding sitei968 – 9681Thiamine pyrophosphateBy similarity
    Binding sitei1036 – 103612-oxoglutarateBy similarity
    Binding sitei1054 – 10541Allosteric activatorBy similarity
    Binding sitei1070 – 10701Allosteric activatorBy similarity
    Binding sitei1158 – 11581Allosteric 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

    BioCyciMVAN350058:GIWR-4517-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:Mvan_4477
    OrganismiMycobacterium vanbaalenii (strain DSM 7251 / PYR-1)
    Taxonomic identifieri350058 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000009159: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12431243Multifunctional 2-oxoglutarate metabolism enzymePRO_0000310725Add
    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

    STRINGi350058.Mvan_4477.

    Structurei

    3D structure databases

    ProteinModelPortaliA1TDK2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 40402-oxoglutarate dehydrogenase E1, N-terminal partAdd
    BLAST
    Regioni41 – 10363LinkerAdd
    BLAST
    Regioni104 – 353250Succinyltransferase E2Add
    BLAST
    Regioni354 – 12438902-oxoglutarate dehydrogenase E1, C-terminal partAdd
    BLAST
    Regioni557 – 5582Thiamine pyrophosphate bindingBy similarity
    Regioni622 – 6243Thiamine pyrophosphate bindingBy similarity
    Regioni661 – 6633Thiamine pyrophosphate bindingBy similarity
    Regioni1105 – 11084Allosteric activatorBy similarity
    Regioni1165 – 11662Allosteric activatorBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili799 – 83133Sequence AnalysisAdd
    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.
    HOGENOMiHOG000259587.
    KOiK01616.
    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.

    A1TDK2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNSPSPFGQN EWLVEEMYRK FREDPSSVDP SWHEFLVDYS PEPTNDAPAG     50
    NGKPAAAPTA PPEPASAPAP KPASTNGGAP PAKADTSTTR APEKKPEEKT 100
    SPAPKAKTAA PAGVSDDDET QVLRGAAAAV VKNMSASLDV PTATSVRAIP 150
    AKAMIDNRIV INNHLKRTRG GKISFTHLLG YAIVQAVKKF PNMNRHFAEI 200
    DGKPVAVTPA HTNLGLAIDL PGKDGKRSLV VAAIKNCETM HFGQFIAAYE 250
    DIVRRARDGK LTAEDFAGVT ISLTNPGTIG TVHSVPRLMK GQGAIVGAGA 300
    MEYPAEFQGA SEERIAELGV GKLMTLTSTY DHRIIQGAES GDFLRTIHTL 350
    LLDDEFYDEI FRELGIPHEP VRWRIDNPDS IEDKNARVIE LIAAYRNRGH 400
    LMADIDPLRL DKTRFRSHPD LDVNTHGLTL WDLDREFKVN GFAGKTHKKL 450
    RDILGLLRDA YCRHIGVEYT HILEPEQQQW LQERIEVKHE KPTVAEQKYI 500
    LSKLNAAEAF ETFLQTKYVG QKRFSLEGAE TVIPMMDAAI DQCAEHGLDE 550
    VVIGMPHRGR LNVLANIVGK PYSQIFTEFE GNLNPSQAHG SGDVKYHLGA 600
    NGTYIQMFGD NDIDVSLVAN PSHLEAVDPV LEGLVRAKQD ILDKGNGPDG 650
    FTVVPMMLHG DAAFAGQGVV AETLNLALLR GYRTGGTIHI IVNNQIGFTT 700
    SPYDSRSSEY CTDVAKMIGA PIFHVNGDDP EACVWVAKLA VDFRQKFKKD 750
    VVIDMLCYRR RGHNEGDDPS MTQPTMYDVI DTKRGVRKSY TEALIGRGDI 800
    SMKEAEDALR DYQGQLERVF NEVRELEKHA IAPSSSVESD QMVPAGMSTA 850
    VDKSLLARIG DAHLGYPDDF NVHPRVKPVL EKRREMAYEG KVDWAFAELL 900
    ALGTFLAEGK TIRFTGQDTR RGTFTQRHSV IIDRQTGREF TPLDLLTVDS 950
    DGNPTGGKFM AYDSALSEFA AVGFEYGYSV GNPNALVLWE AQFGDFVNGA 1000
    QSIIDEFISS GEAKWGQLSD VVLLLPHGHE GQGPDHTSGR IERFLLLWAE 1050
    GSMTIAMPST PANYFHLLRR HGLDGIHRPL IVFTPKSMLR NKAAVSDLKD 1100
    FTEMKFRSVL EEPTYTEGTG DRSKAKRILL TSGKLYYELA ARKSKEGRDD 1150
    VAILRLEQLA PLPKRRLAAT LDEYPNAEQY FWVQEEPANQ GAWPTLGLTL 1200
    PEVLPEKLAG IKRISRRAMS APSSGSSKVH AVEQQEIIDE AFG 1243
    Length:1,243
    Mass (Da):136,980
    Last modified:November 13, 2007 - v2
    Checksum:i88066C7C78C4835D
    GO

    Sequence cautioni

    The sequence ABM15252.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000511 Genomic DNA. Translation: ABM15252.1. Different initiation.
    RefSeqiYP_955258.1. NC_008726.1.

    Genome annotation databases

    EnsemblBacteriaiABM15252; ABM15252; Mvan_4477.
    GeneIDi4649093.
    KEGGimva:Mvan_4477.
    PATRICi18187301. VBIMycVan31953_4554.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000511 Genomic DNA. Translation: ABM15252.1 . Different initiation.
    RefSeqi YP_955258.1. NC_008726.1.

    3D structure databases

    ProteinModelPortali A1TDK2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 350058.Mvan_4477.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABM15252 ; ABM15252 ; Mvan_4477 .
    GeneIDi 4649093.
    KEGGi mva:Mvan_4477.
    PATRICi 18187301. VBIMycVan31953_4554.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000259587.
    KOi K01616.
    OrthoDBi EOG6V1M1F.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00997 .
    UPA00223 ; UER01001 .
    BioCyci MVAN350058:GIWR-4517-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 7251 / PYR-1.

    Entry informationi

    Entry nameiKGD_MYCVP
    AccessioniPrimary (citable) accession number: A1TDK2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 56 of the entry and version 2 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