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Q73WX4 (KGD_MYCPA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:MAP_2536
OrganismMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) [Complete proteome] [HAMAP]
Taxonomic identifier262316 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length1247 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 – 12471247Multifunctional 2-oxoglutarate metabolism enzyme
PRO_0000310717

Regions

Region1 – 41412-oxoglutarate dehydrogenase E1, N-terminal part
Region42 – 10463Linker
Region105 – 353249Succinyltransferase E2
Region354 – 12478942-oxoglutarate dehydrogenase E1, C-terminal part
Region557 – 5582Thiamine pyrophosphate binding By similarity
Region622 – 6243Thiamine pyrophosphate binding By similarity
Region665 – 6673Thiamine pyrophosphate binding By similarity
Region1109 – 11124Allosteric activator By similarity
Region1169 – 11702Allosteric activator By similarity
Coiled coil803 – 83331 Potential
Compositional bias51 – 12979Ala-rich

Sites

Active site3321Proton acceptor; for succinyltransferase activity By similarity
Metal binding6651Magnesium By similarity
Metal binding6981Magnesium By similarity
Metal binding7001Magnesium; via carbonyl oxygen By similarity
Binding site59712-oxoglutarate By similarity
Binding site62212-oxoglutarate By similarity
Binding site9721Thiamine pyrophosphate By similarity
Binding site104012-oxoglutarate By similarity
Binding site10581Allosteric activator By similarity
Binding site10741Allosteric activator By similarity
Binding site11621Allosteric activator By similarity

Sequences

Sequence LengthMass (Da)Tools
Q73WX4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D31E9876D146519A

FASTA1,247137,073
        10         20         30         40         50         60 
MSNISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY NPEPTGDSVL AAPASTDGPS 

        70         80         90        100        110        120 
APAPAAPQTA QPALPAQTAP PAQTAQPARP APQPAAAPGN GASTRPAKPA TPPPAEGDEL 

       130        140        150        160        170        180 
QTLRGAAAAV VKNMSASLEV PTATSVRAIP AKLLIDNRIV INNQLKRTRG GKISFTHLLG 

       190        200        210        220        230        240 
YALVQAIKKF PNMNRHYAEI DGKPTAITPA HTNLGLAIDL QGKDGKRSLV VAGIKNCETM 

       250        260        270        280        290        300 
RFAQFVTAYE DIVRRARDGK LTAEDFAGVT ISLTNPGTIG TVHSVPRLMN GQGAIIGVGA 

       310        320        330        340        350        360 
MEYPAEFQGA SEERIAELGI GKLITLTSTY DHRIIQGAES GDFLRTIHEM LLSDGFWDDI 

       370        380        390        400        410        420 
FRELSIPYLP IRWSTDNPDS IVDKNARVME LIAAYRNRGH LMADIDPLRL DGSRFRSHPD 

       430        440        450        460        470        480 
LEILNHGLTL WDLDRVFKVN GFAGAEYKKL RDILGLLRDA YCRHIGVEYT HILDPEQQEW 

       490        500        510        520        530        540 
LQQRVETKHV KPTVAEQKFI LSKLNAAEAF ETFLQTKYVG QKRFSLEGAE SVIPMMDAAI 

       550        560        570        580        590        600 
DQCAEHGLDE VVIGMPHRGR LNVLANIVGK PYSQIFSEFE GNLNPAQAHG SGDVKYHLGA 

       610        620        630        640        650        660 
TGVYLQMFGD NDIQVSLTAN PSHLEAVDPV LEGLVRAKQD LLDHGADDQG DEKAFSVVPM 

       670        680        690        700        710        720 
MLHGDAAFAG QGVVAETLNL THLPGYRVGG TIHIIVNNQI GFTTAPEHSR SSEYCTDVAK 

       730        740        750        760        770        780 
MIGAPIFHVN GDDPEACAWV AKLAVDFRQK FKKDVVIDML CYRKRGHNEG DDPSMTNPAM 

       790        800        810        820        830        840 
YDVVDIKRGV RKSYTEALIG RGDISMKEAE DALRDYQGQL ERVFNEVREL EKHGVGPSES 

       850        860        870        880        890        900 
VEADQMLPAG LATAVDKALL ARIGDAFLAL PEGFTAHPRV QPVLEKRREM AYEGKIDWAF 

       910        920        930        940        950        960 
AELLALGSLV AGGKLVRLSG QDTRRGTFSQ RHSVIIDRNT GEEFTPLQLL ATNPDGTPTG 

       970        980        990       1000       1010       1020 
GKFLVYDSPL SEYAAVGFEY GYTVGNPDAL VLWEAQFGDF VNGAQSIIDE FISSGEAKWG 

      1030       1040       1050       1060       1070       1080 
QLSNVVLLLP HGHEGQGPDH TSARIERFLQ LWAEGSMTIA MPSTPSNYFH LLRRHALDGI 

      1090       1100       1110       1120       1130       1140 
KRPLIVFTPK SMLRNKAAVS DIKDFTEIKF RSVLEEPTYE DGIGDRGKVS RVLLTSGKLY 

      1150       1160       1170       1180       1190       1200 
YELVARKNKD NRDDVAIVRI EQLAPLPKRR LGETLDRYPN VREYFWVQEE PANQGAWPRF 

      1210       1220       1230       1240 
GLELPELLPD KLTGLKRISR RAMSAPSSGS SKVHAVEQQE IIDTAFA 

« Hide

References

[1]"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-968 / K-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016958 Genomic DNA. Translation: AAS04853.1.
RefSeqNP_961470.1. NC_002944.2.

3D structure databases

ProteinModelPortalQ73WX4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262316.MAP2536.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS04853; AAS04853; MAP_2536.
GeneID2719042.
KEGGmpa:MAP2536.
PATRIC17997756. VBIMycAvi108102_2692.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
KOK01616.
OMAHILRRQL.
OrthoDBEOG6V1M1F.
ProtClustDBPRK12270.

Enzyme and pathway databases

BioCycMAVI262316:GCQR-2572-MONOMER.
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_MYCPA
AccessionPrimary (citable) accession number: Q73WX4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: July 5, 2004
Last modified: November 13, 2013
This is version 73 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