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A1UK81

- KGD_MYCSK

UniProt

A1UK81 - KGD_MYCSK

Protein

Multifunctional 2-oxoglutarate metabolism enzyme

Gene

kgd

Organism
Mycobacterium sp. (strain KMS)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      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 sitei357 – 3571Proton acceptor; for succinyltransferase activityBy similarity
    Binding sitei622 – 62212-oxoglutarateBy similarity
    Binding sitei647 – 64712-oxoglutarateBy similarity
    Metal bindingi686 – 6861MagnesiumBy similarity
    Metal bindingi719 – 7191MagnesiumBy similarity
    Metal bindingi721 – 7211Magnesium; via carbonyl oxygenBy similarity
    Binding sitei993 – 9931Thiamine pyrophosphateBy similarity
    Binding sitei1061 – 106112-oxoglutarateBy similarity
    Binding sitei1079 – 10791Allosteric activatorBy similarity
    Binding sitei1095 – 10951Allosteric activatorBy similarity
    Binding sitei1183 – 11831Allosteric 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

    BioCyciMSP189918:GH4X-4086-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:Mkms_4047
    OrganismiMycobacterium sp. (strain KMS)
    Taxonomic identifieri189918 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000638: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12691269Multifunctional 2-oxoglutarate metabolism enzymePRO_0000310720Add
    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

    STRINGi189918.Mkms_4047.

    Structurei

    3D structure databases

    ProteinModelPortaliA1UK81.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 41412-oxoglutarate dehydrogenase E1, N-terminal partAdd
    BLAST
    Regioni42 – 10766LinkerAdd
    BLAST
    Regioni108 – 378271Succinyltransferase E2Add
    BLAST
    Regioni379 – 12698912-oxoglutarate dehydrogenase E1, C-terminal partAdd
    BLAST
    Regioni582 – 5832Thiamine pyrophosphate bindingBy similarity
    Regioni647 – 6493Thiamine pyrophosphate bindingBy similarity
    Regioni686 – 6883Thiamine pyrophosphate bindingBy similarity
    Regioni1130 – 11334Allosteric activatorBy similarity
    Regioni1190 – 11912Allosteric activatorBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili824 – 85532Sequence 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.
    OMAiDPLEYKQ.
    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.

    A1UK81-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSPSPFGQ NEWLVEEMYR KFREDPSSVD PSWHEFLVDY NPEPTTDSSA     50
    SENGQQTRTA APKAPPEPAP APAPKTPDSK TPDSKSQAPK QDSKPQESKP 100
    QAKAKPAESK SSTKPADAKS EKSGKSGTNG AAKPAAQPAD DSDQNQVLRG 150
    AAAAVAKNMS ASLDVPTATS VRAIPAKLMI DNRVVINNHL KRTRGGKISF 200
    THLIGYAIVA AVKKFPNMNR HFAEVDGKPN AVTPAHTNLG LAIDLQGKDG 250
    NRQLVVAAIK KADTMRFGQF IAAYEDIVRR ARDGKLTAED FSGVTISLTN 300
    PGTIGTVHSV PRLMRGQGAI IGVGAMEYPA EFQGASEERI ADLGIGKLIT 350
    LTSTYDHRII QGAESGDFLR TVHQLLLSDD FFDEIFRELG IPYEPVRWRT 400
    DNPDSIEDKN ARVIELIAAY RNRGHLMADI DPLRLDSNRF RSHPDLDVLT 450
    HGLTLWDLDR EFKVNGFAGA ERKKLRDVLA VLRDAYCRHI GVEYTHILEP 500
    EQQQWLQERI EGKHEKPTVA QQKYILSRLN AAEAFETFLQ TKYVGQKRFS 550
    LEGAETVIPA MDAVIDQCAE HALDEVVIGM PHRGRLNVLA NIVGKPYSQI 600
    FSEFEGNLNP SQAHGSGDVK YHLGSSGTYL QMFGDNDITV SLTANPSHLE 650
    AVDPVMEGLV RAKQDLLDKG DTEDGYTVVP LMLHGDAAFA GQGVVAETLN 700
    LALLRGYRTG GTIHLIVNNQ IGFTTSPAAA KSSEYCTDVA KMIGAPIFHV 750
    NGDDPEAAVW VSRLAVDFRQ KFKKDVVIDL LCYRRRGHNE GDDPSMTQPS 800
    MYDVIDTKRG VRKSYTEALI GRGDISMKEA EDALRDYQGQ LEQVFNEVRE 850
    LEKHEIEPSE SVEADQQIPA KLATAVDKSL LARIGDAHLA VPEGFTVHPR 900
    VKPVLEKRRE MAYEGKVDWA FAELLALGTM ISEGKLVRLS GQDTRRGTFT 950
    QRHSVVIDRK TGKEFTPLQL LATDSDGNPT GGKFLVYDSP LSEFAAVGFE 1000
    YGYSVGNPDA MVLWEAQFGD FINGAQSIID EFISSGEAKW GQLSDVVLLL 1050
    PHGHEGQGPD HTSGRIERFL QLWAEGSMTI ALPSTPANYF HLLRRHSLDG 1100
    IQRPLIVFTP KSMLRNKAAV SDIRDFTEQK FRSVLEEPTY TDGDGDRNKV 1150
    TRILLTSGKI YYELVARKNK ESRDDVAIVR IEQLAPLPKR RLAETLDKYP 1200
    NVEEKFWVQE EPANQGAWPT FGLTLPEMLP DHFTGIKRIS RRAMSAPSSG 1250
    SSKVHAVEQQ EILDEAFAP 1269
    Length:1,269
    Mass (Da):140,119
    Last modified:February 6, 2007 - v1
    Checksum:iF6F4221B80E76B83
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000518 Genomic DNA. Translation: ABL93239.1.
    RefSeqiYP_940029.1. NC_008705.1.

    Genome annotation databases

    EnsemblBacteriaiABL93239; ABL93239; Mkms_4047.
    GeneIDi4611987.
    KEGGimkm:Mkms_4047.
    PATRICi18107106. VBIMycSp70743_4570.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000518 Genomic DNA. Translation: ABL93239.1 .
    RefSeqi YP_940029.1. NC_008705.1.

    3D structure databases

    ProteinModelPortali A1UK81.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 189918.Mkms_4047.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABL93239 ; ABL93239 ; Mkms_4047 .
    GeneIDi 4611987.
    KEGGi mkm:Mkms_4047.
    PATRICi 18107106. VBIMycSp70743_4570.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00997 .
    UPA00223 ; UER01001 .
    BioCyci MSP189918:GH4X-4086-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: KMS.

    Entry informationi

    Entry nameiKGD_MYCSK
    AccessioniPrimary (citable) accession number: A1UK81
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 57 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