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A0R2B1

- KGD_MYCS2

UniProt

A0R2B1 - KGD_MYCS2

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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: 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

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
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.
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 – 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.
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

        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.
RefSeqiYP_006569661.1. NC_018289.1.
YP_889299.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK74238; ABK74238; MSMEG_5049.
AFP41366; AFP41366; MSMEI_4922.
GeneIDi4535402.
KEGGimsm: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 .
RefSeqi YP_006569661.1. NC_018289.1.
YP_889299.1. NC_008596.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 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

« 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: November 26, 2014
This is version 69 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

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