SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A0PVU7

- KGD_MYCUA

UniProt

A0PVU7 - KGD_MYCUA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Multifunctional 2-oxoglutarate metabolism enzyme
Gene
kgd, MUL_4500
Organism
Mycobacterium ulcerans (strain Agy99)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

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.

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 sitei322 – 3221Proton acceptor; for succinyltransferase activity By similarity
Binding sitei588 – 58812-oxoglutarate By similarity
Binding sitei613 – 61312-oxoglutarate By similarity
Metal bindingi656 – 6561Magnesium By similarity
Metal bindingi689 – 6891Magnesium By similarity
Metal bindingi691 – 6911Magnesium; via carbonyl oxygen By similarity
Binding sitei963 – 9631Thiamine pyrophosphate By similarity
Binding sitei1031 – 103112-oxoglutarate By similarity
Binding sitei1049 – 10491Allosteric activator By similarity
Binding sitei1065 – 10651Allosteric activator By similarity
Binding sitei1153 – 11531Allosteric activator By 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
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

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:MUL_4500
OrganismiMycobacterium ulcerans (strain Agy99)
Taxonomic identifieri362242 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000765: Chromosome

Organism-specific databases

GenoListiMUL_4500.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12381238Multifunctional 2-oxoglutarate metabolism enzyme
PRO_0000310724Add
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.

Protein-protein interaction databases

STRINGi362242.MUL_4500.

Structurei

3D structure databases

ProteinModelPortaliA0PVU7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 41412-oxoglutarate dehydrogenase E1, N-terminal part
Add
BLAST
Regioni42 – 9453Linker
Add
BLAST
Regioni95 – 343249Succinyltransferase E2
Add
BLAST
Regioni344 – 12388952-oxoglutarate dehydrogenase E1, C-terminal part
Add
BLAST
Regioni548 – 5492Thiamine pyrophosphate binding By similarity
Regioni613 – 6153Thiamine pyrophosphate binding By similarity
Regioni656 – 6583Thiamine pyrophosphate binding By similarity
Regioni1100 – 11034Allosteric activator By similarity
Regioni1160 – 11612Allosteric activator By similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili794 – 82431 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi48 – 11972Ala-rich
Add
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.
OMAiDPLEYKQ.
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.

A0PVU7-1 [UniParc]FASTAAdd to Basket

« Hide

MANISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY NPESTQEATE     50
PAVVKPAAAP AKPAPAPAPA KPAAGPPAAG NGSPAAAPSA KPAAAPAKAP 100
APPPAEGDEM QVLRGAAAAV VKNMSASLDV PTATSVRAVP AKLLIDNRIV 150
INNQLKRNRG GKISFTHLLG YALVQAVKKF PNMNRHYLDV DGKPNAVTPA 200
HTNLGLAIDL QGKDGKRALV VAGIKRCETM RFAQFVTAYE DIVRRARDGK 250
LTAEDFSGVT ISLTNPGTIG TVHSVPRLMA GQGAIIGVGA MEYPAEFQGA 300
SEERIAELGI GKLITLTSTY DHRIIQGAES GDFLRTIHQM LLADEFWDEI 350
FRELSIPYLP VRWRPDNPDS IVDKNARIIE LIAAYRNRGH LMADIDPLRL 400
DKTRFRSHPD LDVCTHGLTL WDLDRSFKVG GCFAGPQNMK LRDVLSILRD 450
TYCRHVGVEY THILEPEQQQ WLQQRVEAKH VKPTVAQQKY VLSKLNAAEA 500
FETFLQTKYV GQKRFSLEGA ESVIPMMDAA IDQCAEYGLD EVVIGMPHRG 550
RLNVLANIVG KPYSQIFSEF EGNLNPSQAH GSGDVKYHLG ATGVYLQMFG 600
DNDIQVSLTA NPSHLEAVDP VLEGLVRAKQ DLLEHGETDT ENQRAFSVVP 650
MMLHGDAAFA GQGVVAETLN LANLPGYRVG GTIHIIVNNQ IGFTTAPEYS 700
RSTEYCTDVA KTIGAPIFHV NGDDPEACVW VARLAVDFRQ RFNKDVIIDM 750
LCYRRRGHNE GDDPSMTNPR MYDVVDTKRG VRKSYTEALI GRGDISIKEA 800
EDALRDYQGQ LEQVFNEVRE LEKHGAQPSE SVESDQMIPA GLATAVDKSL 850
LARIGDAFLA VPDGFTTHPR VQPVLEKRRE MAYEGKIDWA FAELLALGSL 900
VAEGKLVRFS GQDTRRGTFS QRHSVIIDRH TREEFTPLQL LTTNKDGSPT 950
GGKFLVYDSP LSEYAAVGFE YGYTVGNPDA VVLWEAQFGD FVNGAQSIID 1000
EFISSGEAKW GQLSNVVLLL PHGHEGQGPD HTSGRIERFL QLWAEGSMTI 1050
AMPSTPSNYF HLLRRHALDG IQRPLIVFTP KSMLRNKAAV SDIKDFTEIK 1100
FRSVLEEPTY EDGVGDRNLV NRILLTSGKI YYEMVARKAK DKREDVAIVR 1150
VEQLAPLPRR RLRETLDRYP NAKEFFWVQE EPANQGAWPR FGLELPELLP 1200
EKLSGVKRIS RRAMSAPSSG SSKVHAVEQQ EILDTAFG 1238
Length:1,238
Mass (Da):136,742
Last modified:January 9, 2007 - v1
Checksum:iB9A7DB3108194D2A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000325 Genomic DNA. Translation: ABL06466.1.
RefSeqiYP_907937.1. NC_008611.1.

Genome annotation databases

EnsemblBacteriaiABL06466; ABL06466; MUL_4500.
GeneIDi4549927.
KEGGimul:MUL_4500.
PATRICi18176818. VBIMycUlc37413_5210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000325 Genomic DNA. Translation: ABL06466.1 .
RefSeqi YP_907937.1. NC_008611.1.

3D structure databases

ProteinModelPortali A0PVU7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 362242.MUL_4500.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL06466 ; ABL06466 ; MUL_4500 .
GeneIDi 4549927.
KEGGi mul:MUL_4500.
PATRICi 18176818. VBIMycUlc37413_5210.

Organism-specific databases

GenoListi MUL_4500.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000259587.
KOi K01616.
OMAi DPLEYKQ.
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. "Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
    Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.
    , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
    Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Agy99.

Entry informationi

Entry nameiKGD_MYCUA
AccessioniPrimary (citable) accession number: A0PVU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: January 9, 2007
Last modified: June 11, 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

Similar proteinsi