Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A0PVU7 (KGD_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multifunctional 2-oxoglutarate metabolism enzyme
Alternative name(s):
2-hydroxy-3-oxoadipate synthase
Short name=HOA synthase
Short name=HOAS
EC=2.2.1.5
2-oxoglutarate carboxy-lyase
2-oxoglutarate decarboxylase
Alpha-ketoglutarate decarboxylase
Short name=KG decarboxylase
Short name=KGD
EC=4.1.1.71
Alpha-ketoglutarate-glyoxylate carboligase

Including the following 2 domains:

  1. 2-oxoglutarate dehydrogenase E1 component
    Short name=ODH E1 component
    EC=1.2.4.2
    Alternative name(s):
    Alpha-ketoglutarate dehydrogenase E1 component
    Short name=KDH E1 component
  2. 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 names
Name:kgd
Ordered Locus Names:MUL_4500
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length1238 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

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.

Cofactor

Magnesium By similarity.

Thiamine pyrophosphate By similarity.

Enzyme regulation

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.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2.

Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.

Subunit structure

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.

Domain

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 similarities

Belongs to the 2-oxoacid dehydrogenase family. Kgd subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12381238Multifunctional 2-oxoglutarate metabolism enzyme
PRO_0000310724

Regions

Region1 – 41412-oxoglutarate dehydrogenase E1, N-terminal part
Region42 – 9453Linker
Region95 – 343249Succinyltransferase E2
Region344 – 12388952-oxoglutarate dehydrogenase E1, C-terminal part
Region548 – 5492Thiamine pyrophosphate binding By similarity
Region613 – 6153Thiamine pyrophosphate binding By similarity
Region656 – 6583Thiamine pyrophosphate binding By similarity
Region1100 – 11034Allosteric activator By similarity
Region1160 – 11612Allosteric activator By similarity
Coiled coil794 – 82431 Potential
Compositional bias48 – 11972Ala-rich

Sites

Active site3221Proton acceptor; for succinyltransferase activity By similarity
Metal binding6561Magnesium By similarity
Metal binding6891Magnesium By similarity
Metal binding6911Magnesium; via carbonyl oxygen By similarity
Binding site58812-oxoglutarate By similarity
Binding site61312-oxoglutarate By similarity
Binding site9631Thiamine pyrophosphate By similarity
Binding site103112-oxoglutarate By similarity
Binding site10491Allosteric activator By similarity
Binding site10651Allosteric activator By similarity
Binding site11531Allosteric activator By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PVU7 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: B9A7DB3108194D2A

FASTA1,238136,742
        10         20         30         40         50         60 
MANISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY NPESTQEATE PAVVKPAAAP 

        70         80         90        100        110        120 
AKPAPAPAPA KPAAGPPAAG NGSPAAAPSA KPAAAPAKAP APPPAEGDEM QVLRGAAAAV 

       130        140        150        160        170        180 
VKNMSASLDV PTATSVRAVP AKLLIDNRIV INNQLKRNRG GKISFTHLLG YALVQAVKKF 

       190        200        210        220        230        240 
PNMNRHYLDV DGKPNAVTPA HTNLGLAIDL QGKDGKRALV VAGIKRCETM RFAQFVTAYE 

       250        260        270        280        290        300 
DIVRRARDGK LTAEDFSGVT ISLTNPGTIG TVHSVPRLMA GQGAIIGVGA MEYPAEFQGA 

       310        320        330        340        350        360 
SEERIAELGI GKLITLTSTY DHRIIQGAES GDFLRTIHQM LLADEFWDEI FRELSIPYLP 

       370        380        390        400        410        420 
VRWRPDNPDS IVDKNARIIE LIAAYRNRGH LMADIDPLRL DKTRFRSHPD LDVCTHGLTL 

       430        440        450        460        470        480 
WDLDRSFKVG GCFAGPQNMK LRDVLSILRD TYCRHVGVEY THILEPEQQQ WLQQRVEAKH 

       490        500        510        520        530        540 
VKPTVAQQKY VLSKLNAAEA FETFLQTKYV GQKRFSLEGA ESVIPMMDAA IDQCAEYGLD 

       550        560        570        580        590        600 
EVVIGMPHRG RLNVLANIVG KPYSQIFSEF EGNLNPSQAH GSGDVKYHLG ATGVYLQMFG 

       610        620        630        640        650        660 
DNDIQVSLTA NPSHLEAVDP VLEGLVRAKQ DLLEHGETDT ENQRAFSVVP MMLHGDAAFA 

       670        680        690        700        710        720 
GQGVVAETLN LANLPGYRVG GTIHIIVNNQ IGFTTAPEYS RSTEYCTDVA KTIGAPIFHV 

       730        740        750        760        770        780 
NGDDPEACVW VARLAVDFRQ RFNKDVIIDM LCYRRRGHNE GDDPSMTNPR MYDVVDTKRG 

       790        800        810        820        830        840 
VRKSYTEALI GRGDISIKEA EDALRDYQGQ LEQVFNEVRE LEKHGAQPSE SVESDQMIPA 

       850        860        870        880        890        900 
GLATAVDKSL LARIGDAFLA VPDGFTTHPR VQPVLEKRRE MAYEGKIDWA FAELLALGSL 

       910        920        930        940        950        960 
VAEGKLVRFS GQDTRRGTFS QRHSVIIDRH TREEFTPLQL LTTNKDGSPT GGKFLVYDSP 

       970        980        990       1000       1010       1020 
LSEYAAVGFE YGYTVGNPDA VVLWEAQFGD FVNGAQSIID EFISSGEAKW GQLSNVVLLL 

      1030       1040       1050       1060       1070       1080 
PHGHEGQGPD HTSGRIERFL QLWAEGSMTI AMPSTPSNYF HLLRRHALDG IQRPLIVFTP 

      1090       1100       1110       1120       1130       1140 
KSMLRNKAAV SDIKDFTEIK FRSVLEEPTY EDGVGDRNLV NRILLTSGKI YYEMVARKAK 

      1150       1160       1170       1180       1190       1200 
DKREDVAIVR VEQLAPLPRR RLRETLDRYP NAKEFFWVQE EPANQGAWPR FGLELPELLP 

      1210       1220       1230 
EKLSGVKRIS RRAMSAPSSG SSKVHAVEQQ EILDTAFG 

« Hide

References

[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL06466.1.
RefSeqYP_907937.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PVU7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362242.MUL_4500.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL06466; ABL06466; MUL_4500.
GeneID4549927.
KEGGmul:MUL_4500.
PATRIC18176818. VBIMycUlc37413_5210.

Organism-specific databases

GenoListMUL_4500.
CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000259587.
KOK01616.
OMAHILRRQL.
OrthoDBEOG6V1M1F.
ProtClustDBPRK12270.

Enzyme and pathway databases

UniPathwayUPA00223; UER00997.
UPA00223; UER01001.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
InterProIPR001078. 2-oxoacid_DH_actylTfrase.
IPR011603. 2oxoglutarate_DH_E1.
IPR023213. CAT-like_dom.
IPR001017. DH_E1.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERPTHR23152. PTHR23152. 1 hit.
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKGD_MYCUA
AccessionPrimary (citable) accession number: A0PVU7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: January 9, 2007
Last modified: November 13, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways