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A0R2B1

- KGD_MYCS2

UniProt

A0R2B1 - KGD_MYCS2

Protein

Multifunctional 2-oxoglutarate metabolism enzyme

Gene

kgd

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (09 Jan 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.2 Publications

    Catalytic activityi

    2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2.1 Publication
    2-oxoglutarate = succinate semialdehyde + CO2.1 Publication
    2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.1 Publication
    Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.1 Publication

    Cofactori

    Magnesium.1 Publication
    Thiamine pyrophosphate.1 Publication

    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. Both the phosphoadenosine and acetyl moieties of acetyl-CoA are important for activation because neither CoA nor the synthetic compound S-(2-acetamidoethyl)-ethanethioate (which mimics the terminal acetyl-phosphopantetheine group of acetyl-CoA) has an activation effect.2 Publications

    Kineticsi

    1. KM=0.54 mM for alpha-ketoglutarate1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei314 – 3141Proton acceptor; for succinyltransferase activityBy similarity
    Binding sitei579 – 57912-oxoglutarate
    Binding sitei604 – 60412-oxoglutarate
    Metal bindingi645 – 6451Magnesium
    Metal bindingi678 – 6781Magnesium
    Metal bindingi680 – 6801Magnesium; via carbonyl oxygen
    Binding sitei952 – 9521Thiamine pyrophosphate
    Binding sitei1020 – 102012-oxoglutarate
    Binding sitei1038 – 10381Allosteric activator
    Binding sitei1054 – 10541Allosteric activator
    Binding sitei1142 – 11421Allosteric activator

    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

    BioCyciMSME246196:GJ4Y-5048-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
    Synonyms:sucA
    Ordered Locus Names:MSMEG_5049, MSMEI_4922
    OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
    Taxonomic identifieri246196 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000757: Chromosome, UP000006158: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene do not show any ODH activity, in contrast to wild-type, demonstrating that this protein is part of a functional ODH complex in mycobacteria.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi539 – 5391H → A: Loss of KG decarboxylase activity. 1 Publication
    Mutagenesisi579 – 5791H → A: Loss of KG decarboxylase activity. 1 Publication
    Mutagenesisi747 – 7471H → A: 40-fold decrease in KG decarboxylase activity. 1 Publication
    Mutagenesisi781 – 7811R → A: Increase in KG decarboxylase activity. 1 Publication
    Mutagenesisi1020 – 10201H → A: Loss of KG decarboxylase activity. 1 Publication
    Mutagenesisi1034 – 10341E → A: Loss of activation by acetyl-CoA. 1 Publication
    Mutagenesisi1062 – 10621R → A: Loss of activation by acetyl-CoA. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12271227Multifunctional 2-oxoglutarate metabolism enzymePRO_0000310718Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer. Interacts with the FHA domain of unphosphorylated GarA. The 2-oxoglutarate dehydrogenase (ODH) complex contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).2 Publications

    Protein-protein interaction databases

    IntActiA0R2B1. 1 interaction.
    STRINGi246196.MSMEG_5049.

    Structurei

    Secondary structure

    1
    1227
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi124 – 1329
    Helixi134 – 14916
    Helixi157 – 17115
    Helixi173 – 1764
    Beta strandi178 – 18912
    Beta strandi196 – 1994
    Beta strandi213 – 2164
    Helixi219 – 2213
    Helixi224 – 23815
    Turni239 – 2413
    Helixi245 – 2473
    Beta strandi252 – 2565
    Beta strandi275 – 2806
    Helixi294 – 3007
    Beta strandi305 – 3139
    Turni314 – 3163
    Helixi319 – 33214
    Helixi336 – 34510
    Helixi367 – 38014
    Helixi381 – 3833
    Helixi395 – 3984
    Turni401 – 4033
    Helixi406 – 4083
    Helixi412 – 4143
    Beta strandi416 – 4194
    Beta strandi429 – 4313
    Helixi432 – 44312
    Beta strandi444 – 4507
    Helixi457 – 46711
    Helixi476 – 49924
    Beta strandi500 – 5023
    Helixi504 – 5063
    Helixi514 – 52714
    Beta strandi531 – 5366
    Helixi542 – 5487
    Helixi554 – 5574
    Turni558 – 5603
    Helixi567 – 5704
    Beta strandi571 – 5733
    Helixi576 – 5783
    Beta strandi582 – 5876
    Beta strandi589 – 5924
    Beta strandi594 – 5996
    Turni606 – 6094
    Helixi610 – 62415
    Beta strandi630 – 6323
    Beta strandi637 – 6448
    Helixi645 – 6506
    Helixi652 – 6587
    Turni659 – 6624
    Turni664 – 6663
    Beta strandi672 – 6776
    Helixi686 – 6894
    Beta strandi691 – 6944
    Helixi697 – 7026
    Beta strandi706 – 7105
    Helixi714 – 73118
    Beta strandi735 – 7406
    Helixi753 – 7553
    Helixi758 – 7647
    Helixi770 – 78011
    Helixi786 – 81227
    Helixi822 – 8243
    Helixi837 – 84610
    Turni858 – 8603
    Helixi861 – 87313
    Helixi878 – 89114
    Beta strandi895 – 9006
    Turni901 – 9055
    Beta strandi913 – 9164
    Turni918 – 9203
    Helixi926 – 9316
    Beta strandi942 – 9476
    Helixi953 – 96513
    Beta strandi969 – 9746
    Helixi978 – 9847
    Helixi985 – 9906
    Turni991 – 9944
    Helixi995 – 9995
    Beta strandi1006 – 10105
    Beta strandi1014 – 10163
    Helixi1025 – 10317
    Beta strandi1034 – 10363
    Beta strandi1038 – 10403
    Helixi1045 – 105713
    Beta strandi1064 – 10685
    Helixi1071 – 10744
    Beta strandi1076 – 10783
    Helixi1082 – 10865
    Beta strandi1092 – 10943
    Helixi1097 – 11004
    Helixi1106 – 11083
    Beta strandi1111 – 11155
    Helixi1119 – 113012
    Beta strandi1135 – 11406
    Beta strandi1142 – 11454
    Helixi1148 – 11569
    Beta strandi1163 – 11719
    Beta strandi1174 – 11763
    Helixi1177 – 118711
    Helixi1189 – 11924
    Beta strandi1196 – 12005
    Beta strandi1204 – 12074
    Helixi1211 – 122515

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XT6X-ray2.74A/B116-1227[»]
    2XT9X-ray2.20A361-1227[»]
    2XTAX-ray2.20A/B/C/D361-1227[»]
    2Y0PX-ray2.40A/B/C/D361-1227[»]
    2YICX-ray1.96A/B/C/D361-1227[»]
    2YIDX-ray2.25A/B/C/D361-1227[»]
    3ZHQX-ray2.50A/B/C/D361-1227[»]
    3ZHRX-ray2.10A/B/C/D361-1227[»]
    3ZHSX-ray2.10A/B/C/D361-1227[»]
    3ZHTX-ray2.15A/B/C/D361-1227[»]
    3ZHUX-ray2.30A/B/C/D361-1227[»]
    3ZHVX-ray2.30A/B/C/D361-1227[»]
    ProteinModelPortaliA0R2B1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiA0R2B1.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 41412-oxoglutarate dehydrogenase E1, N-terminal partAdd
    BLAST
    Regioni42 – 8847LinkerAdd
    BLAST
    Regioni89 – 335247Succinyltransferase E2Add
    BLAST
    Regioni336 – 12278922-oxoglutarate dehydrogenase E1, C-terminal partAdd
    BLAST
    Regioni539 – 5402Thiamine pyrophosphate binding
    Regioni604 – 6063Thiamine pyrophosphate binding
    Regioni645 – 6473Thiamine pyrophosphate binding
    Regioni1089 – 10924Allosteric activator
    Regioni1149 – 11502Allosteric activator

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili783 – 81432Sequence 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.
    OMAiQHAPNKE.
    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.

    A0R2B1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSPSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY SPEPTTDSAS     50
    NGRTTTAAPV TPPTPAPAPA PEPKAAPKPA AKTEAKPAKP AKSATPAKGD 100
    ESQILRGAAA AVVKNMNASL EVPTATSVRA IPAKLMIDNR VVINNHLKRT 150
    RGGKISFTHL LGYAIVQAVK KFPNMNRHFA VVDGKPTAIT PAHTNLGLAI 200
    DLQGKDGNRS LVVAAIKRCE TMRFGQFIAA YEDIVRRARD GKLTAEDFSG 250
    VTISLTNPGT LGTVHSVPRL MQGQGAIIGA GAMEYPAEFQ GASEERIADL 300
    GIGKLITLTS TYDHRIIQGA ESGDFLRTIH QLLLDDDFFD EIFRELGIPY 350
    EPVRWRTDNP DSIEDKNARV IELIAAYRNR GHLMADIDPL RLDNTRFRSH 400
    PDLDVNSHGL TLWDLDREFK VDGFAGVQRK KLRDILSVLR DAYCRHVGVE 450
    YTHILEPEQQ RWIQERVETK HDKPTVAEQK YILSKLNAAE AFETFLQTKY 500
    VGQKRFSLEG AETVIPMMDA VIDQCAEHGL DEVVIAMPHR GRLNVLANIV 550
    GKPYSQIFSE FEGNLNPSQA HGSGDVKYHL GATGTYIQMF GDNDIEVSLT 600
    ANPSHLEAVD PVLEGLVRAK QDLLDTGEEG SDNRFSVVPL MLHGDAAFAG 650
    QGVVAETLNL ALLRGYRTGG TIHIVVNNQI GFTTAPTDSR SSEYCTDVAK 700
    MIGAPIFHVN GDDPEACAWV ARLAVDFRQA FKKDVVIDML CYRRRGHNEG 750
    DDPSMTQPYM YDVIDTKRGS RKAYTEALIG RGDISMKEAE DALRDYQGQL 800
    ERVFNEVREL EKHEIEPSES VEADQQIPSK LATAVDKAML QRIGDAHLAL 850
    PEGFTVHPRV RPVLEKRREM AYEGRIDWAF AELLALGSLI AEGKLVRLSG 900
    QDTQRGTFTQ RHAVIVDRKT GEEFTPLQLL ATNPDGTPTG GKFLVYNSAL 950
    SEFAAVGFEY GYSVGNPDAM VLWEAQFGDF VNGAQSIIDE FISSGEAKWG 1000
    QLSDVVLLLP HGHEGQGPDH TSGRIERFLQ LWAEGSMTIA MPSTPANYFH 1050
    LLRRHGKDGI QRPLIVFTPK SMLRNKAAVS DIRDFTESKF RSVLEEPMYT 1100
    DGEGDRNKVT RLLLTSGKIY YELAARKAKE NREDVAIVRI EQLAPLPRRR 1150
    LAETLDRYPN VKEKFWVQEE PANQGAWPSF GLTLPEILPD HFTGLKRISR 1200
    RAMSAPSSGS SKVHAVEQQE ILDTAFG 1227
    Length:1,227
    Mass (Da):135,944
    Last modified:January 9, 2007 - v1
    Checksum:i76C5BFFD1638A391
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK74238.1.
    CP001663 Genomic DNA. Translation: AFP41366.1.
    RefSeqiWP_011730279.1. NC_018289.1.
    YP_006569661.1. NC_018289.1.
    YP_889299.1. NC_008596.1.

    Genome annotation databases

    EnsemblBacteriaiABK74238; ABK74238; MSMEG_5049.
    AFP41366; AFP41366; MSMEI_4922.
    GeneIDi4535402.
    KEGGimsg:MSMEI_4922.
    msm:MSMEG_5049.
    PATRICi18082397. VBIMycSme59918_4927.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK74238.1 .
    CP001663 Genomic DNA. Translation: AFP41366.1 .
    RefSeqi WP_011730279.1. NC_018289.1.
    YP_006569661.1. NC_018289.1.
    YP_889299.1. NC_008596.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XT6 X-ray 2.74 A/B 116-1227 [» ]
    2XT9 X-ray 2.20 A 361-1227 [» ]
    2XTA X-ray 2.20 A/B/C/D 361-1227 [» ]
    2Y0P X-ray 2.40 A/B/C/D 361-1227 [» ]
    2YIC X-ray 1.96 A/B/C/D 361-1227 [» ]
    2YID X-ray 2.25 A/B/C/D 361-1227 [» ]
    3ZHQ X-ray 2.50 A/B/C/D 361-1227 [» ]
    3ZHR X-ray 2.10 A/B/C/D 361-1227 [» ]
    3ZHS X-ray 2.10 A/B/C/D 361-1227 [» ]
    3ZHT X-ray 2.15 A/B/C/D 361-1227 [» ]
    3ZHU X-ray 2.30 A/B/C/D 361-1227 [» ]
    3ZHV X-ray 2.30 A/B/C/D 361-1227 [» ]
    ProteinModelPortali A0R2B1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi A0R2B1. 1 interaction.
    STRINGi 246196.MSMEG_5049.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABK74238 ; ABK74238 ; MSMEG_5049 .
    AFP41366 ; AFP41366 ; MSMEI_4922 .
    GeneIDi 4535402.
    KEGGi msg:MSMEI_4922.
    msm:MSMEG_5049.
    PATRICi 18082397. VBIMycSme59918_4927.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00997 .
    UPA00223 ; UER01001 .
    BioCyci MSME246196:GJ4Y-5048-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei A0R2B1.

    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. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
      Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
      Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
      Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
      Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
      Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 700084 / mc(2)155.
    4. Cited for: FUNCTION IN 2-OXOGLUTARATE DECARBOXYLATION, ENZYME REGULATION, KINETIC PARAMETERS, INTERACTION WITH GARA.
      Strain: ATCC 700084 / mc(2)155.
    5. "Functional plasticity and allosteric regulation of alpha-ketoglutarate decarboxylase in central mycobacterial metabolism."
      Wagner T., Bellinzoni M., Wehenkel A., O'Hare H.M., Alzari P.M.
      Chem. Biol. 18:1011-1020(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 116-1227 IN COMPLEXES WITH THIAMINE PYROPHOSPHATE; ACETYL-COA; ENAMINE-THDP REACTION INTERMEDIATE AND MAGNESIUM, FUNCTION AS A MULTIFUNCTIONAL ENZYME, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT, PATHWAY, MUTAGENESIS OF HIS-539; HIS-579; HIS-747; ARG-781; HIS-1020; GLU-1034 AND ARG-1062, DISRUPTION PHENOTYPE.
      Strain: ATCC 700084 / mc(2)155.

    Entry informationi

    Entry nameiKGD_MYCS2
    AccessioniPrimary (citable) accession number: A0R2B1
    Secondary accession number(s): I7GDF5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 67 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

    3D-structure, Allosteric enzyme, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3