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A1KI36

- KGD_MYCBP

UniProt

A1KI36 - KGD_MYCBP

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Protein
Multifunctional 2-oxoglutarate metabolism enzyme
Gene
kgd, BCG_1308c
Organism
Mycobacterium bovis (strain BCG / Pasteur 1173P2)
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 sitei316 – 3161Proton acceptor; for succinyltransferase activity By similarity
Binding sitei581 – 58112-oxoglutarate By similarity
Binding sitei606 – 60612-oxoglutarate By similarity
Metal bindingi649 – 6491Magnesium By similarity
Metal bindingi682 – 6821Magnesium By similarity
Metal bindingi684 – 6841Magnesium; via carbonyl oxygen By similarity
Binding sitei956 – 9561Thiamine pyrophosphate By similarity
Binding sitei1024 – 102412-oxoglutarate By similarity
Binding sitei1042 – 10421Allosteric activator By similarity
Binding sitei1058 – 10581Allosteric activator By similarity
Binding sitei1146 – 11461Allosteric 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
Complete GO annotation...

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

BioCyciMBOV410289:GJW7-1328-MONOMER.
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:BCG_1308c
OrganismiMycobacterium bovis (strain BCG / Pasteur 1173P2)
Taxonomic identifieri410289 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001472: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12311231Multifunctional 2-oxoglutarate metabolism enzyme
PRO_0000310715Add
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

STRINGi410289.BCG_1308c.

Structurei

3D structure databases

ProteinModelPortaliA1KI36.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 41412-oxoglutarate dehydrogenase E1, N-terminal part
Add
BLAST
Regioni42 – 8847Linker
Add
BLAST
Regioni89 – 337249Succinyltransferase E2
Add
BLAST
Regioni338 – 12318942-oxoglutarate dehydrogenase E1, C-terminal part
Add
BLAST
Regioni541 – 5422Thiamine pyrophosphate binding By similarity
Regioni606 – 6083Thiamine pyrophosphate binding By similarity
Regioni649 – 6513Thiamine pyrophosphate binding By similarity
Regioni1093 – 10964Allosteric activator By similarity
Regioni1153 – 11542Allosteric activator By similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili787 – 81731 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi61 – 11353Ala-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.
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.

A1KI36-1 [UniParc]FASTAAdd to Basket

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MANISSPFGQ NEWLVEAMYR KFRDDPSSVD PSWHEFLVDY SPEPTSQPAA     50
EPTRVTSPLV AERAAAAAPQ APPKPADTAA AGNGVVAALA AKTAVPPPAE 100
GDEVAVLRGA AAAVVKNMSA SLEVPTATSV RAVPAKLLID NRIVINNQLK 150
RTRGGKISFT HLLGYALVQA VKKFPNMNRH YTEVDGKPTA VTPAHTNLGL 200
AIDLQGKDGK RSLVVAGIKR CETMRFAQFV TAYEDIVRRA RDGKLTTEDF 250
AGVTISLTNP GTIGTVHSVP RLMPGQGAII GVGAMEYPAE FQGASEERIA 300
ELGIGKLITL TSTYDHRIIQ GAESGDFLRT IHELLLSDGF WDEVFRELSI 350
PYLPVRWSTD NPDSIVDKNA RVMNLIAAYR NRGHLMADTD PLRLDKARFR 400
SHPDLEVLTH GLTLWDLDRV FKVDGFAGAQ YKKLRDVLGL LRDAYCRHIG 450
VEYAHILDPE QKEWLEQRVE TKHVKPTVAQ QKYILSKLNA AEAFETFLQT 500
KYVGQKRFSL EGAESVIPMM DAAIDQCAEH GLDEVVIGMP HRGRLNVLAN 550
IVGKPYSQIF TEFEGNLNPS QAHGSGDVKY HLGATGLYLQ MFGDNDIQVS 600
LTANPSHLEA VDPVLEGLVR AKQDLLDHGS IDSDGQRAFS VVPLMLHGDA 650
AFAGQGVVAE TLNLANLPGY RVGGTIHIIV NNQIGFTTAP EYSRSSEYCT 700
DVAKMIGAPI FHVNGDDPEA CVWVARLAVD FRQRFKKDVV IDMLCYRRRG 750
HNEGDDPSMT NPYMYDVVDT KRGARKSYTE ALIGRGDISM KEAEDALRDY 800
QGQLERVFNE VRELEKHGVQ PSESVESDQM IPAGLATAVD KSLLARIGDA 850
FLALPNGFTA HPRVQPVLEK RREMAYEGKI DWAFGELLAL GSLVAEGKLV 900
RLSGQDSRRG TFSQRHSVLI DRHTGEEFTP LQLLATNSDG SPTGGKFLVY 950
DSPLSEYAAV GFEYGYTVGN PDAVVLWEAQ FGDFVNGAQS IIDEFISSGE 1000
AKWGQLSNVV LLLPHGHEGQ GPDHTSARIE RFLQLWAEGS MTIAMPSTPS 1050
NYFHLLRRHA LDGIQRPLIV FTPKSMLRHK AAVSEIKDFT EIKFRSVLEE 1100
PTYEDGIGDR NKVSRILLTS GKLYYELAAR KAKDNRNDLA IVRLEQLAPL 1150
PRRRLRETLD RYENVKEFFW VQEEPANQGA WPRFGLELPE LLPDKLAGIK 1200
RISRRAMSAP SSGSSKVHAV EQQEILDEAF G 1231
Length:1,231
Mass (Da):135,876
Last modified:November 13, 2007 - v2
Checksum:i02D4FD5F9718C330
GO

Sequence cautioni

The sequence CAL71295.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM408590 Genomic DNA. Translation: CAL71295.1. Different initiation.
RefSeqiYP_977400.1. NC_008769.1.

Genome annotation databases

EnsemblBacteriaiCAL71295; CAL71295; BCG_1308c.
GeneIDi4697169.
KEGGimbb:BCG_1308c.
PATRICi18013332. VBIMycBov80988_1432.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM408590 Genomic DNA. Translation: CAL71295.1 . Different initiation.
RefSeqi YP_977400.1. NC_008769.1.

3D structure databases

ProteinModelPortali A1KI36.
ModBasei Search...

Protein-protein interaction databases

STRINGi 410289.BCG_1308c.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL71295 ; CAL71295 ; BCG_1308c .
GeneIDi 4697169.
KEGGi mbb:BCG_1308c.
PATRICi 18013332. VBIMycBov80988_1432.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000259587.
KOi K01616.
OrthoDBi EOG6V1M1F.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00997 .
UPA00223 ; UER01001 .
BioCyci MBOV410289:GJW7-1328-MONOMER.

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: BCG / Pasteur 1173P2.

Entry informationi

Entry nameiKGD_MYCBP
AccessioniPrimary (citable) accession number: A1KI36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: June 11, 2014
This is version 53 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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