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Q9CC97

- KGD_MYCLE

UniProt

Q9CC97 - KGD_MYCLE

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Protein

Multifunctional 2-oxoglutarate metabolism enzyme

Gene
kgd, ML1095
Organism
Mycobacterium leprae (strain TN)
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 sitei325 – 3251Proton acceptor; for succinyltransferase activity By similarity
Binding sitei590 – 59012-oxoglutarate By similarity
Binding sitei615 – 61512-oxoglutarate By similarity
Metal bindingi657 – 6571Magnesium By similarity
Metal bindingi690 – 6901Magnesium By similarity
Metal bindingi692 – 6921Magnesium; via carbonyl oxygen By similarity
Binding sitei964 – 9641Thiamine pyrophosphate By similarity
Binding sitei1032 – 103212-oxoglutarate By similarity
Binding sitei1050 – 10501Allosteric activator By similarity
Binding sitei1066 – 10661Allosteric activator By similarity
Binding sitei1154 – 11541Allosteric 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:ML1095
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000806: Chromosome

Organism-specific databases

LepromaiML1095.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12381238Multifunctional 2-oxoglutarate metabolism enzymePRO_0000310716Add
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

STRINGi272631.ML1095.

Structurei

3D structure databases

ProteinModelPortaliQ9CC97.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 41412-oxoglutarate dehydrogenase E1, N-terminal partAdd
BLAST
Regioni42 – 9756LinkerAdd
BLAST
Regioni98 – 346249Succinyltransferase E2Add
BLAST
Regioni347 – 12388922-oxoglutarate dehydrogenase E1, C-terminal partAdd
BLAST
Regioni550 – 5512Thiamine pyrophosphate binding By similarity
Regioni615 – 6173Thiamine pyrophosphate binding By similarity
Regioni657 – 6593Thiamine pyrophosphate binding By similarity
Regioni1101 – 11044Allosteric activator By similarity
Regioni1161 – 11622Allosteric activator By similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili795 – 82531 Reviewed predictionAdd
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.
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.

Q9CC97-1 [UniParc]FASTAAdd to Basket

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MANISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY NPESTAEPVL     50
TDPTSTDKQP SATPQAKPAA AADPVASRAK PATTPTVANG TAAGSAAAPA 100
KTTTTPPIEG DELQVLRGAA AVVVKNMSAS LDVPTATSVR AVPAKLMIDN 150
RTVINNQLKR NRGGKISFTH LLGYALVQAV KKFPNINRHY AEIDGKPIAV 200
TPAHTNLGLA IDLQGKDGKR SLVVAGIKRC EELRFAQFVT AYEDIVRRAR 250
DGKLTAEDFA GVTISLTNPG TIGTVHSVPR LMTGQGAIIG VGAMEYPAEF 300
QGASAERIAE LGIGKLITLT STYDHRIIQG AESGDFLRTI HEMVLSDSFW 350
DEIFRELSIP YLPVRWRTDN PDSIVDKNAR VMELIAAYRN RGHLMADIDP 400
LRLDNTRFRS HPDLDLLTHG LTLWDLDRVF KVNGFGGWKY KKLRDVLGLL 450
RDAYCRHIGV EYTHILDPEQ QEWLQQRVET KNVKPTVAEQ KYILSKLNAA 500
EAFETFLHTK YVGQKRFSLE GAESVIPMMD AAIDQCAKHG LDEVVIGMPH 550
RGRLNVLANI VGKPYSQIFT EFEGNLNPTL AHSSGDVKYH LGATGLYLQM 600
FGDNDIQVSL TANPSHLEAV DPVLEGLVRA KQDLLNKDTN GNQDEAFSVV 650
PMMLHGDAAF AGQGVVAETL NLANLPGYRV GGTIHIIVNN QIGFTTAPEY 700
SRSSEYCTDV AKMIGAPIFH VNGDDPEACV WVAKLAVDFR QRFKKDVVID 750
MLCYRRRGHN EGDDPSMTNP YMYDVVDTKR GARKSYTEAL IGRGDISLKE 800
AEDALRDYQG QLERVFNEVR DLEKHGVQPS ESVESDQMIP AGLSTAVDKA 850
LLARIGDAFL AVPEGFTVHP RVQPVLEKRR EMAYEGKIDW AFAELLALGS 900
LVAEGKLVRL SGQDTKRGTF SQRHSVIIDR HTGEEFTPLQ LLANNPDGSP 950
TGGKFLVYNS PLSEYAAVGF EYGYTVGNPD AVVLWEAQFG DFVNGAQSII 1000
DEFINSGEAK WGQLSTVVLL LPHGHEGQGP DHTSGRIERF LQLWAEGSMT 1050
FAVPSTPSNY FHLLRRHALD GIKRPLIVFT PKSMLRNKAA VSDIKDFTEI 1100
KFRSVLEEPT YEDSIDDRSK VTRVLLTCGK LYYELAARKI KDNRDDVAIV 1150
RIEQLAPLPR RRLGETLDRY ENAKEFFWVQ EEPANQGAWP RFGLELPELL 1200
PRLTGIKRIS RRAMSAPSSG SSKVHAVEQQ EILDTAFG 1238
Length:1,238
Mass (Da):137,020
Last modified:November 13, 2007 - v2
Checksum:i62B154E8A1D9A0E8
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL583920 Genomic DNA. Translation: CAC31476.1. Different initiation.
PIRiA87046.
RefSeqiNP_301802.2. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC31476; CAC31476; CAC31476.
GeneIDi910185.
KEGGimle:ML1095.
PATRICi18054027. VBIMycLep78757_1959.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL583920 Genomic DNA. Translation: CAC31476.1 . Different initiation.
PIRi A87046.
RefSeqi NP_301802.2. NC_002677.1.

3D structure databases

ProteinModelPortali Q9CC97.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272631.ML1095.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC31476 ; CAC31476 ; CAC31476 .
GeneIDi 910185.
KEGGi mle:ML1095.
PATRICi 18054027. VBIMycLep78757_1959.

Organism-specific databases

Lepromai ML1095.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000259587.
KOi K01616.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TN.

Entry informationi

Entry nameiKGD_MYCLE
AccessioniPrimary (citable) accession number: Q9CC97
Entry historyi
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 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

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