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Protein

Multifunctional 2-oxoglutarate metabolism enzyme

Gene

kgd

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:
  • Mg2+1 Publication
  • thiamine diphosphate1 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

    Pathway:itricarboxylic acid cycle

    This protein is involved in step 1 of the subpathway that synthesizes succinate from 2-oxoglutarate (transferase route).1 Publication
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Multifunctional 2-oxoglutarate metabolism enzyme (kgd)
    2. no protein annotated in this organism
    This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinate from 2-oxoglutarate (transferase route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

    Pathway:itricarboxylic acid cycle

    This protein is involved in step 1 of the subpathway that synthesizes succinyl-CoA from 2-oxoglutarate (dehydrogenase route).1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Multifunctional 2-oxoglutarate metabolism enzyme (kgd)
    This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinyl-CoA from 2-oxoglutarate (dehydrogenase route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

    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

    GO - Biological processi

    Complete GO annotation...

    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.
    BRENDAi4.1.1.71. 3512.
    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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
    ProteomesiUP000006158 Componenti: Chromosome UP000000757 Componenti: 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 – 1329Combined sources
    Helixi134 – 14916Combined sources
    Helixi157 – 17115Combined sources
    Helixi173 – 1764Combined sources
    Beta strandi178 – 18912Combined sources
    Beta strandi196 – 1994Combined sources
    Beta strandi213 – 2164Combined sources
    Helixi219 – 2213Combined sources
    Helixi224 – 23815Combined sources
    Turni239 – 2413Combined sources
    Helixi245 – 2473Combined sources
    Beta strandi252 – 2565Combined sources
    Beta strandi275 – 2806Combined sources
    Helixi294 – 3007Combined sources
    Beta strandi305 – 3139Combined sources
    Turni314 – 3163Combined sources
    Helixi319 – 33214Combined sources
    Helixi336 – 34510Combined sources
    Helixi367 – 38014Combined sources
    Helixi381 – 3833Combined sources
    Helixi395 – 3984Combined sources
    Turni401 – 4033Combined sources
    Helixi406 – 4083Combined sources
    Helixi412 – 4143Combined sources
    Beta strandi416 – 4194Combined sources
    Beta strandi429 – 4313Combined sources
    Helixi432 – 44312Combined sources
    Beta strandi444 – 4507Combined sources
    Helixi457 – 46711Combined sources
    Helixi476 – 49924Combined sources
    Beta strandi500 – 5023Combined sources
    Helixi504 – 5063Combined sources
    Helixi514 – 52714Combined sources
    Beta strandi531 – 5366Combined sources
    Helixi542 – 5487Combined sources
    Helixi554 – 5574Combined sources
    Turni558 – 5603Combined sources
    Helixi567 – 5704Combined sources
    Beta strandi571 – 5733Combined sources
    Helixi576 – 5783Combined sources
    Beta strandi582 – 5876Combined sources
    Beta strandi589 – 5924Combined sources
    Beta strandi594 – 5996Combined sources
    Turni606 – 6094Combined sources
    Helixi610 – 62415Combined sources
    Beta strandi630 – 6323Combined sources
    Beta strandi637 – 6448Combined sources
    Helixi645 – 6506Combined sources
    Helixi652 – 6587Combined sources
    Turni659 – 6624Combined sources
    Turni664 – 6663Combined sources
    Beta strandi672 – 6776Combined sources
    Helixi686 – 6894Combined sources
    Beta strandi691 – 6944Combined sources
    Helixi697 – 7026Combined sources
    Beta strandi706 – 7105Combined sources
    Helixi714 – 73118Combined sources
    Beta strandi735 – 7406Combined sources
    Helixi753 – 7553Combined sources
    Helixi758 – 7647Combined sources
    Helixi770 – 78011Combined sources
    Helixi786 – 81227Combined sources
    Helixi822 – 8243Combined sources
    Helixi837 – 84610Combined sources
    Turni858 – 8603Combined sources
    Helixi861 – 87313Combined sources
    Helixi878 – 89114Combined sources
    Beta strandi895 – 9006Combined sources
    Turni901 – 9055Combined sources
    Beta strandi913 – 9164Combined sources
    Turni918 – 9203Combined sources
    Helixi926 – 9316Combined sources
    Beta strandi942 – 9476Combined sources
    Helixi953 – 96513Combined sources
    Beta strandi969 – 9746Combined sources
    Helixi978 – 9847Combined sources
    Helixi985 – 9906Combined sources
    Turni991 – 9944Combined sources
    Helixi995 – 9995Combined sources
    Beta strandi1006 – 10105Combined sources
    Beta strandi1014 – 10163Combined sources
    Helixi1025 – 10317Combined sources
    Beta strandi1034 – 10363Combined sources
    Beta strandi1038 – 10403Combined sources
    Helixi1045 – 105713Combined sources
    Beta strandi1064 – 10685Combined sources
    Helixi1071 – 10744Combined sources
    Beta strandi1076 – 10783Combined sources
    Helixi1082 – 10865Combined sources
    Beta strandi1092 – 10943Combined sources
    Helixi1097 – 11004Combined sources
    Helixi1106 – 11083Combined sources
    Beta strandi1111 – 11155Combined sources
    Helixi1119 – 113012Combined sources
    Beta strandi1135 – 11406Combined sources
    Beta strandi1142 – 11454Combined sources
    Helixi1148 – 11569Combined sources
    Beta strandi1163 – 11719Combined sources
    Beta strandi1174 – 11763Combined sources
    Helixi1177 – 118711Combined sources
    Helixi1189 – 11924Combined sources
    Beta strandi1196 – 12005Combined sources
    Beta strandi1204 – 12074Combined sources
    Helixi1211 – 122515Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    OMAiQNQGAWF.
    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

            10         20         30         40         50
    MSSSPSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY SPEPTTDSAS
    60 70 80 90 100
    NGRTTTAAPV TPPTPAPAPA PEPKAAPKPA AKTEAKPAKP AKSATPAKGD
    110 120 130 140 150
    ESQILRGAAA AVVKNMNASL EVPTATSVRA IPAKLMIDNR VVINNHLKRT
    160 170 180 190 200
    RGGKISFTHL LGYAIVQAVK KFPNMNRHFA VVDGKPTAIT PAHTNLGLAI
    210 220 230 240 250
    DLQGKDGNRS LVVAAIKRCE TMRFGQFIAA YEDIVRRARD GKLTAEDFSG
    260 270 280 290 300
    VTISLTNPGT LGTVHSVPRL MQGQGAIIGA GAMEYPAEFQ GASEERIADL
    310 320 330 340 350
    GIGKLITLTS TYDHRIIQGA ESGDFLRTIH QLLLDDDFFD EIFRELGIPY
    360 370 380 390 400
    EPVRWRTDNP DSIEDKNARV IELIAAYRNR GHLMADIDPL RLDNTRFRSH
    410 420 430 440 450
    PDLDVNSHGL TLWDLDREFK VDGFAGVQRK KLRDILSVLR DAYCRHVGVE
    460 470 480 490 500
    YTHILEPEQQ RWIQERVETK HDKPTVAEQK YILSKLNAAE AFETFLQTKY
    510 520 530 540 550
    VGQKRFSLEG AETVIPMMDA VIDQCAEHGL DEVVIAMPHR GRLNVLANIV
    560 570 580 590 600
    GKPYSQIFSE FEGNLNPSQA HGSGDVKYHL GATGTYIQMF GDNDIEVSLT
    610 620 630 640 650
    ANPSHLEAVD PVLEGLVRAK QDLLDTGEEG SDNRFSVVPL MLHGDAAFAG
    660 670 680 690 700
    QGVVAETLNL ALLRGYRTGG TIHIVVNNQI GFTTAPTDSR SSEYCTDVAK
    710 720 730 740 750
    MIGAPIFHVN GDDPEACAWV ARLAVDFRQA FKKDVVIDML CYRRRGHNEG
    760 770 780 790 800
    DDPSMTQPYM YDVIDTKRGS RKAYTEALIG RGDISMKEAE DALRDYQGQL
    810 820 830 840 850
    ERVFNEVREL EKHEIEPSES VEADQQIPSK LATAVDKAML QRIGDAHLAL
    860 870 880 890 900
    PEGFTVHPRV RPVLEKRREM AYEGRIDWAF AELLALGSLI AEGKLVRLSG
    910 920 930 940 950
    QDTQRGTFTQ RHAVIVDRKT GEEFTPLQLL ATNPDGTPTG GKFLVYNSAL
    960 970 980 990 1000
    SEFAAVGFEY GYSVGNPDAM VLWEAQFGDF VNGAQSIIDE FISSGEAKWG
    1010 1020 1030 1040 1050
    QLSDVVLLLP HGHEGQGPDH TSGRIERFLQ LWAEGSMTIA MPSTPANYFH
    1060 1070 1080 1090 1100
    LLRRHGKDGI QRPLIVFTPK SMLRNKAAVS DIRDFTESKF RSVLEEPMYT
    1110 1120 1130 1140 1150
    DGEGDRNKVT RLLLTSGKIY YELAARKAKE NREDVAIVRI EQLAPLPRRR
    1160 1170 1180 1190 1200
    LAETLDRYPN VKEKFWVQEE PANQGAWPSF GLTLPEILPD HFTGLKRISR
    1210 1220
    RAMSAPSSGS SKVHAVEQQE ILDTAFG
    Length:1,227
    Mass (Da):135,944
    Last modified:January 9, 2007 - v1
    Checksum:i76C5BFFD1638A391
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000480 Genomic DNA. Translation: ABK74238.1.
    CP001663 Genomic DNA. Translation: AFP41366.1.
    RefSeqiWP_011730279.1. NZ_CP009494.1.
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000480 Genomic DNA. Translation: ABK74238.1.
    CP001663 Genomic DNA. Translation: AFP41366.1.
    RefSeqiWP_011730279.1. NZ_CP009494.1.
    YP_889299.1. NC_008596.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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...

    Protein-protein interaction databases

    IntActiA0R2B1. 1 interaction.
    STRINGi246196.MSMEG_5049.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000259587.
    KOiK01616.
    OMAiQNQGAWF.
    OrthoDBiEOG6V1M1F.

    Enzyme and pathway databases

    UniPathwayiUPA00223; UER00997.
    UPA00223; UER01001.
    BioCyciMSME246196:GJ4Y-5048-MONOMER.
    BRENDAi4.1.1.71. 3512.

    Miscellaneous databases

    EvolutionaryTraceiA0R2B1.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: July 22, 2015
    This is version 75 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.