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

Q9CC97 (KGD_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 79. 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:ML1095
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [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 caution

The sequence CAC31476.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12381238Multifunctional 2-oxoglutarate metabolism enzyme
PRO_0000310716

Regions

Region1 – 41412-oxoglutarate dehydrogenase E1, N-terminal part
Region42 – 9756Linker
Region98 – 346249Succinyltransferase E2
Region347 – 12388922-oxoglutarate dehydrogenase E1, C-terminal part
Region550 – 5512Thiamine pyrophosphate binding By similarity
Region615 – 6173Thiamine pyrophosphate binding By similarity
Region657 – 6593Thiamine pyrophosphate binding By similarity
Region1101 – 11044Allosteric activator By similarity
Region1161 – 11622Allosteric activator By similarity
Coiled coil795 – 82531 Potential

Sites

Active site3251Proton acceptor; for succinyltransferase activity By similarity
Metal binding6571Magnesium By similarity
Metal binding6901Magnesium By similarity
Metal binding6921Magnesium; via carbonyl oxygen By similarity
Binding site59012-oxoglutarate By similarity
Binding site61512-oxoglutarate By similarity
Binding site9641Thiamine pyrophosphate By similarity
Binding site103212-oxoglutarate By similarity
Binding site10501Allosteric activator By similarity
Binding site10661Allosteric activator By similarity
Binding site11541Allosteric activator By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CC97 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 62B154E8A1D9A0E8

FASTA1,238137,020
        10         20         30         40         50         60 
MANISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY NPESTAEPVL TDPTSTDKQP 

        70         80         90        100        110        120 
SATPQAKPAA AADPVASRAK PATTPTVANG TAAGSAAAPA KTTTTPPIEG DELQVLRGAA 

       130        140        150        160        170        180 
AVVVKNMSAS LDVPTATSVR AVPAKLMIDN RTVINNQLKR NRGGKISFTH LLGYALVQAV 

       190        200        210        220        230        240 
KKFPNINRHY AEIDGKPIAV TPAHTNLGLA IDLQGKDGKR SLVVAGIKRC EELRFAQFVT 

       250        260        270        280        290        300 
AYEDIVRRAR DGKLTAEDFA GVTISLTNPG TIGTVHSVPR LMTGQGAIIG VGAMEYPAEF 

       310        320        330        340        350        360 
QGASAERIAE LGIGKLITLT STYDHRIIQG AESGDFLRTI HEMVLSDSFW DEIFRELSIP 

       370        380        390        400        410        420 
YLPVRWRTDN PDSIVDKNAR VMELIAAYRN RGHLMADIDP LRLDNTRFRS HPDLDLLTHG 

       430        440        450        460        470        480 
LTLWDLDRVF KVNGFGGWKY KKLRDVLGLL RDAYCRHIGV EYTHILDPEQ QEWLQQRVET 

       490        500        510        520        530        540 
KNVKPTVAEQ KYILSKLNAA EAFETFLHTK YVGQKRFSLE GAESVIPMMD AAIDQCAKHG 

       550        560        570        580        590        600 
LDEVVIGMPH RGRLNVLANI VGKPYSQIFT EFEGNLNPTL AHSSGDVKYH LGATGLYLQM 

       610        620        630        640        650        660 
FGDNDIQVSL TANPSHLEAV DPVLEGLVRA KQDLLNKDTN GNQDEAFSVV PMMLHGDAAF 

       670        680        690        700        710        720 
AGQGVVAETL NLANLPGYRV GGTIHIIVNN QIGFTTAPEY SRSSEYCTDV AKMIGAPIFH 

       730        740        750        760        770        780 
VNGDDPEACV WVAKLAVDFR QRFKKDVVID MLCYRRRGHN EGDDPSMTNP YMYDVVDTKR 

       790        800        810        820        830        840 
GARKSYTEAL IGRGDISLKE AEDALRDYQG QLERVFNEVR DLEKHGVQPS ESVESDQMIP 

       850        860        870        880        890        900 
AGLSTAVDKA LLARIGDAFL AVPEGFTVHP RVQPVLEKRR EMAYEGKIDW AFAELLALGS 

       910        920        930        940        950        960 
LVAEGKLVRL SGQDTKRGTF SQRHSVIIDR HTGEEFTPLQ LLANNPDGSP TGGKFLVYNS 

       970        980        990       1000       1010       1020 
PLSEYAAVGF EYGYTVGNPD AVVLWEAQFG DFVNGAQSII DEFINSGEAK WGQLSTVVLL 

      1030       1040       1050       1060       1070       1080 
LPHGHEGQGP DHTSGRIERF LQLWAEGSMT FAVPSTPSNY FHLLRRHALD GIKRPLIVFT 

      1090       1100       1110       1120       1130       1140 
PKSMLRNKAA VSDIKDFTEI KFRSVLEEPT YEDSIDDRSK VTRVLLTCGK LYYELAARKI 

      1150       1160       1170       1180       1190       1200 
KDNRDDVAIV RIEQLAPLPR RRLGETLDRY ENAKEFFWVQ EEPANQGAWP RFGLELPELL 

      1210       1220       1230 
PRLTGIKRIS RRAMSAPSSG SSKVHAVEQQ EILDTAFG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL583920 Genomic DNA. Translation: CAC31476.1. Different initiation.
PIRA87046.
RefSeqNP_301802.2. NC_002677.1.

3D structure databases

ProteinModelPortalQ9CC97.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML1095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC31476; CAC31476; CAC31476.
GeneID910185.
KEGGmle:ML1095.
PATRIC18054027. VBIMycLep78757_1959.

Organism-specific databases

LepromaML1095.
CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000259587.
KOK01616.
OrthoDBEOG6V1M1F.

Enzyme and pathway databases

UniPathwayUPA00223; UER00997.
UPA00223; UER01001.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
3.40.50.970. 2 hits.
InterProIPR001078. 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]
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]
SUPFAMSSF52518. SSF52518. 2 hits.
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKGD_MYCLE
AccessionPrimary (citable) accession number: Q9CC97
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: June 11, 2014
This is version 79 of the entry and version 2 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