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A3Q3N5

- KGD_MYCSJ

UniProt

A3Q3N5 - KGD_MYCSJ

Protein

Multifunctional 2-oxoglutarate metabolism enzyme

Gene

kgd

Organism
Mycobacterium sp. (strain JLS)
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 (03 Apr 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 sitei352 – 3521Proton acceptor; for succinyltransferase activityBy similarity
    Binding sitei617 – 61712-oxoglutarateBy similarity
    Binding sitei642 – 64212-oxoglutarateBy similarity
    Metal bindingi681 – 6811MagnesiumBy similarity
    Metal bindingi714 – 7141MagnesiumBy similarity
    Metal bindingi716 – 7161Magnesium; via carbonyl oxygenBy similarity
    Binding sitei988 – 9881Thiamine pyrophosphateBy similarity
    Binding sitei1056 – 105612-oxoglutarateBy similarity
    Binding sitei1074 – 10741Allosteric activatorBy similarity
    Binding sitei1090 – 10901Allosteric activatorBy similarity
    Binding sitei1178 – 11781Allosteric 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

    BioCyciMSP164757:GHV3-4022-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:Mjls_3987
    OrganismiMycobacterium sp. (strain JLS)
    Taxonomic identifieri164757 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000002152: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12641264Multifunctional 2-oxoglutarate metabolism enzymePRO_0000310719Add
    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

    STRINGi164757.Mjls_3987.

    Structurei

    3D structure databases

    ProteinModelPortaliA3Q3N5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 41412-oxoglutarate dehydrogenase E1, N-terminal partAdd
    BLAST
    Regioni42 – 10261LinkerAdd
    BLAST
    Regioni103 – 373271Succinyltransferase E2Add
    BLAST
    Regioni374 – 12648912-oxoglutarate dehydrogenase E1, C-terminal partAdd
    BLAST
    Regioni577 – 5782Thiamine pyrophosphate bindingBy similarity
    Regioni642 – 6443Thiamine pyrophosphate bindingBy similarity
    Regioni681 – 6833Thiamine pyrophosphate bindingBy similarity
    Regioni1125 – 11284Allosteric activatorBy similarity
    Regioni1185 – 11862Allosteric activatorBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili819 – 85032Sequence 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.
    OMAiGHQNANL.
    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.

    A3Q3N5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSPSPFGQ NEWLVEEMYR KFREDPSSVD PSWHEFLVDY NPEPTTDSSA     50
    SENGQQTRTA APKAPPEPAP APAPKSQDSK SQAPKQDSKP QESKPQAKAK 100
    PAESKSSTKP ADAKSEKSGK SGTNGAAKPA AQPADDSDQN QVLRGAAAAV 150
    AKNMSASLDV PTATSVRAIP AKLMIDNRVV INNHLKRTRG GKISFTHLIG 200
    YAIVAAVKKF PNMNRHFAEV DGKPNAVTPA HTNLGLAIDL QGKDGNRQLV 250
    VAAIKKADTM RFGQFIAAYE DIVRRARDGK LTAEDFSGVT ISLTNPGTIG 300
    TVHSVPRLMR GQGAIIGVGA MEYPAEFQGA SEERIADLGI GKLITLTSTY 350
    DHRIIQGAES GDFLRTVHQL LLSDDFFDEI FRELGIPYEP VRWRTDNPDS 400
    IEDKNARVIE LIAAYRNRGH LMADIDPLRL DSNRFRSHPD LDVLTHGLTL 450
    WDLDREFKVN GFAGAERKKL RDVLAVLRDA YCRHIGVEYT HILEPEQQQW 500
    LQERIEGKHE KPTVAQQKYI LSRLNAAEAF ETFLQTKYVG QKRFSLEGAE 550
    TVIPAMDAVI DQCAEHALDE VVIGMPHRGR LNVLANIVGK PYSQIFSEFE 600
    GNLNPSQAHG SGDVKYHLGS SGTYLQMFGD NDITVSLTAN PSHLEAVDPV 650
    MEGLVRAKQD LLDKGDTEDG YTVVPLMLHG DAAFAGQGVV AETLNLALLR 700
    GYRTGGTIHL IVNNQIGFTT SPAAAKSSEY CTDVAKMIGA PIFHVNGDDP 750
    EAAVWVSRLA VDFRQKFKKD VVIDLLCYRR RGHNEGDDPS MTQPSMYDVI 800
    DTKRGVRKSY TEALIGRGDI SMKEAEDALR DYQGQLEQVF NEVRELEKHE 850
    IEPSESVEAD QQIPAKLATA VDKSLLARIG DAHLAVPEGF TVHPRVKPVL 900
    EKRREMAYEG KVDWAFAELL ALGTMISEGK LVRLSGQDTR RGTFTQRHSV 950
    VIDRKTGKEF TPLQLLATDS DGNPTGGKFL VYDSPLSEFA AVGFEYGYSV 1000
    GNPDAMVLWE AQFGDFINGA QSIIDEFISS GEAKWGQLSD VVLLLPHGHE 1050
    GQGPDHTSGR IERFLQLWAE GSMTIALPST PANYFHLLRR HSLDGIQRPL 1100
    IVFTPKSMLR NKAAVSDIRD FTEQKFRSVL EEPTYTDGDG DRNKVTRILL 1150
    TSGKIYYELV ARKNKESRDD VAIVRIEQLA PLPKRRLAET LDKYPNVDEK 1200
    FWVQEEPANQ GAWPTFGLTL PEMLPDHFTG IKRISRRAMS APSSGSSKVH 1250
    AVEQQEILDE AFAP 1264
    Length:1,264
    Mass (Da):139,593
    Last modified:April 3, 2007 - v1
    Checksum:iC5068956C2130DAC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000580 Genomic DNA. Translation: ABN99762.1.
    RefSeqiWP_011856407.1. NC_009077.1.
    YP_001072253.1. NC_009077.1.

    Genome annotation databases

    EnsemblBacteriaiABN99762; ABN99762; Mjls_3987.
    GeneIDi4879696.
    KEGGimjl:Mjls_3987.
    PATRICi18094212. VBIMycSp51234_4021.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000580 Genomic DNA. Translation: ABN99762.1 .
    RefSeqi WP_011856407.1. NC_009077.1.
    YP_001072253.1. NC_009077.1.

    3D structure databases

    ProteinModelPortali A3Q3N5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 164757.Mjls_3987.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABN99762 ; ABN99762 ; Mjls_3987 .
    GeneIDi 4879696.
    KEGGi mjl:Mjls_3987.
    PATRICi 18094212. VBIMycSp51234_4021.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00997 .
    UPA00223 ; UER01001 .
    BioCyci MSP164757:GHV3-4022-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: JLS.

    Entry informationi

    Entry nameiKGD_MYCSJ
    AccessioniPrimary (citable) accession number: A3Q3N5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: April 3, 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

    Documents

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

    External Data

    Dasty 3