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Q9CC97

- KGD_MYCLE

UniProt

Q9CC97 - KGD_MYCLE

Protein

Multifunctional 2-oxoglutarate metabolism enzyme

Gene

kgd

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 2 (13 Nov 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 sitei325 – 3251Proton acceptor; for succinyltransferase activityBy similarity
    Binding sitei590 – 59012-oxoglutarateBy similarity
    Binding sitei615 – 61512-oxoglutarateBy similarity
    Metal bindingi657 – 6571MagnesiumBy similarity
    Metal bindingi690 – 6901MagnesiumBy similarity
    Metal bindingi692 – 6921Magnesium; via carbonyl oxygenBy similarity
    Binding sitei964 – 9641Thiamine pyrophosphateBy similarity
    Binding sitei1032 – 103212-oxoglutarateBy similarity
    Binding sitei1050 – 10501Allosteric activatorBy similarity
    Binding sitei1066 – 10661Allosteric activatorBy similarity
    Binding sitei1154 – 11541Allosteric 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

    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:ML1095
    OrganismiMycobacterium leprae (strain TN)
    Taxonomic identifieri272631 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000806: Chromosome

    Organism-specific databases

    LepromaiML1095.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12381238Multifunctional 2-oxoglutarate metabolism enzymePRO_0000310716Add
    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

    STRINGi272631.ML1095.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CC97.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 41412-oxoglutarate dehydrogenase E1, N-terminal partAdd
    BLAST
    Regioni42 – 9756LinkerAdd
    BLAST
    Regioni98 – 346249Succinyltransferase E2Add
    BLAST
    Regioni347 – 12388922-oxoglutarate dehydrogenase E1, C-terminal partAdd
    BLAST
    Regioni550 – 5512Thiamine pyrophosphate bindingBy similarity
    Regioni615 – 6173Thiamine pyrophosphate bindingBy similarity
    Regioni657 – 6593Thiamine pyrophosphate bindingBy similarity
    Regioni1101 – 11044Allosteric activatorBy similarity
    Regioni1161 – 11622Allosteric activatorBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili795 – 82531Sequence 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.

    Q9CC97-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY NPESTAEPVL     50
    TDPTSTDKQP SATPQAKPAA AADPVASRAK PATTPTVANG TAAGSAAAPA 100
    KTTTTPPIEG DELQVLRGAA AVVVKNMSAS LDVPTATSVR AVPAKLMIDN 150
    RTVINNQLKR NRGGKISFTH LLGYALVQAV KKFPNINRHY AEIDGKPIAV 200
    TPAHTNLGLA IDLQGKDGKR SLVVAGIKRC EELRFAQFVT AYEDIVRRAR 250
    DGKLTAEDFA GVTISLTNPG TIGTVHSVPR LMTGQGAIIG VGAMEYPAEF 300
    QGASAERIAE LGIGKLITLT STYDHRIIQG AESGDFLRTI HEMVLSDSFW 350
    DEIFRELSIP YLPVRWRTDN PDSIVDKNAR VMELIAAYRN RGHLMADIDP 400
    LRLDNTRFRS HPDLDLLTHG LTLWDLDRVF KVNGFGGWKY KKLRDVLGLL 450
    RDAYCRHIGV EYTHILDPEQ QEWLQQRVET KNVKPTVAEQ KYILSKLNAA 500
    EAFETFLHTK YVGQKRFSLE GAESVIPMMD AAIDQCAKHG LDEVVIGMPH 550
    RGRLNVLANI VGKPYSQIFT EFEGNLNPTL AHSSGDVKYH LGATGLYLQM 600
    FGDNDIQVSL TANPSHLEAV DPVLEGLVRA KQDLLNKDTN GNQDEAFSVV 650
    PMMLHGDAAF AGQGVVAETL NLANLPGYRV GGTIHIIVNN QIGFTTAPEY 700
    SRSSEYCTDV AKMIGAPIFH VNGDDPEACV WVAKLAVDFR QRFKKDVVID 750
    MLCYRRRGHN EGDDPSMTNP YMYDVVDTKR GARKSYTEAL IGRGDISLKE 800
    AEDALRDYQG QLERVFNEVR DLEKHGVQPS ESVESDQMIP AGLSTAVDKA 850
    LLARIGDAFL AVPEGFTVHP RVQPVLEKRR EMAYEGKIDW AFAELLALGS 900
    LVAEGKLVRL SGQDTKRGTF SQRHSVIIDR HTGEEFTPLQ LLANNPDGSP 950
    TGGKFLVYNS PLSEYAAVGF EYGYTVGNPD AVVLWEAQFG DFVNGAQSII 1000
    DEFINSGEAK WGQLSTVVLL LPHGHEGQGP DHTSGRIERF LQLWAEGSMT 1050
    FAVPSTPSNY FHLLRRHALD GIKRPLIVFT PKSMLRNKAA VSDIKDFTEI 1100
    KFRSVLEEPT YEDSIDDRSK VTRVLLTCGK LYYELAARKI KDNRDDVAIV 1150
    RIEQLAPLPR RRLGETLDRY ENAKEFFWVQ EEPANQGAWP RFGLELPELL 1200
    PRLTGIKRIS RRAMSAPSSG SSKVHAVEQQ EILDTAFG 1238
    Length:1,238
    Mass (Da):137,020
    Last modified:November 13, 2007 - v2
    Checksum:i62B154E8A1D9A0E8
    GO

    Sequence cautioni

    The sequence CAC31476.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL583920 Genomic DNA. Translation: CAC31476.1. Different initiation.
    PIRiA87046.
    RefSeqiNP_301802.2. NC_002677.1.

    Genome annotation databases

    EnsemblBacteriaiCAC31476; CAC31476; CAC31476.
    GeneIDi910185.
    KEGGimle:ML1095.
    PATRICi18054027. VBIMycLep78757_1959.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL583920 Genomic DNA. Translation: CAC31476.1 . Different initiation.
    PIRi A87046.
    RefSeqi NP_301802.2. NC_002677.1.

    3D structure databases

    ProteinModelPortali Q9CC97.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272631.ML1095.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC31476 ; CAC31476 ; CAC31476 .
    GeneIDi 910185.
    KEGGi mle:ML1095.
    PATRICi 18054027. VBIMycLep78757_1959.

    Organism-specific databases

    Lepromai ML1095.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00997 .
    UPA00223 ; UER01001 .

    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: TN.

    Entry informationi

    Entry nameiKGD_MYCLE
    AccessioniPrimary (citable) accession number: Q9CC97
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 80 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