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A1UK81

- KGD_MYCSK

UniProt

A1UK81 - KGD_MYCSK

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Protein
Multifunctional 2-oxoglutarate metabolism enzyme
Gene
kgd, Mkms_4047
Organism
Mycobacterium sp. (strain KMS)
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 sitei357 – 3571Proton acceptor; for succinyltransferase activity By similarity
Binding sitei622 – 62212-oxoglutarate By similarity
Binding sitei647 – 64712-oxoglutarate By similarity
Metal bindingi686 – 6861Magnesium By similarity
Metal bindingi719 – 7191Magnesium By similarity
Metal bindingi721 – 7211Magnesium; via carbonyl oxygen By similarity
Binding sitei993 – 9931Thiamine pyrophosphate By similarity
Binding sitei1061 – 106112-oxoglutarate By similarity
Binding sitei1079 – 10791Allosteric activator By similarity
Binding sitei1095 – 10951Allosteric activator By similarity
Binding sitei1183 – 11831Allosteric 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

BioCyciMSP189918:GH4X-4086-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:Mkms_4047
OrganismiMycobacterium sp. (strain KMS)
Taxonomic identifieri189918 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000638: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12691269Multifunctional 2-oxoglutarate metabolism enzyme
PRO_0000310720Add
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

STRINGi189918.Mkms_4047.

Structurei

3D structure databases

ProteinModelPortaliA1UK81.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 41412-oxoglutarate dehydrogenase E1, N-terminal part
Add
BLAST
Regioni42 – 10766Linker
Add
BLAST
Regioni108 – 378271Succinyltransferase E2
Add
BLAST
Regioni379 – 12698912-oxoglutarate dehydrogenase E1, C-terminal part
Add
BLAST
Regioni582 – 5832Thiamine pyrophosphate binding By similarity
Regioni647 – 6493Thiamine pyrophosphate binding By similarity
Regioni686 – 6883Thiamine pyrophosphate binding By similarity
Regioni1130 – 11334Allosteric activator By similarity
Regioni1190 – 11912Allosteric activator By similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili824 – 85532 Reviewed prediction
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.
OMAiDPLEYKQ.
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.

A1UK81-1 [UniParc]FASTAAdd to Basket

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MSSSPSPFGQ NEWLVEEMYR KFREDPSSVD PSWHEFLVDY NPEPTTDSSA     50
SENGQQTRTA APKAPPEPAP APAPKTPDSK TPDSKSQAPK QDSKPQESKP 100
QAKAKPAESK SSTKPADAKS EKSGKSGTNG AAKPAAQPAD DSDQNQVLRG 150
AAAAVAKNMS ASLDVPTATS VRAIPAKLMI DNRVVINNHL KRTRGGKISF 200
THLIGYAIVA AVKKFPNMNR HFAEVDGKPN AVTPAHTNLG LAIDLQGKDG 250
NRQLVVAAIK KADTMRFGQF IAAYEDIVRR ARDGKLTAED FSGVTISLTN 300
PGTIGTVHSV PRLMRGQGAI IGVGAMEYPA EFQGASEERI ADLGIGKLIT 350
LTSTYDHRII QGAESGDFLR TVHQLLLSDD FFDEIFRELG IPYEPVRWRT 400
DNPDSIEDKN ARVIELIAAY RNRGHLMADI DPLRLDSNRF RSHPDLDVLT 450
HGLTLWDLDR EFKVNGFAGA ERKKLRDVLA VLRDAYCRHI GVEYTHILEP 500
EQQQWLQERI EGKHEKPTVA QQKYILSRLN AAEAFETFLQ TKYVGQKRFS 550
LEGAETVIPA MDAVIDQCAE HALDEVVIGM PHRGRLNVLA NIVGKPYSQI 600
FSEFEGNLNP SQAHGSGDVK YHLGSSGTYL QMFGDNDITV SLTANPSHLE 650
AVDPVMEGLV RAKQDLLDKG DTEDGYTVVP LMLHGDAAFA GQGVVAETLN 700
LALLRGYRTG GTIHLIVNNQ IGFTTSPAAA KSSEYCTDVA KMIGAPIFHV 750
NGDDPEAAVW VSRLAVDFRQ KFKKDVVIDL LCYRRRGHNE GDDPSMTQPS 800
MYDVIDTKRG VRKSYTEALI GRGDISMKEA EDALRDYQGQ LEQVFNEVRE 850
LEKHEIEPSE SVEADQQIPA KLATAVDKSL LARIGDAHLA VPEGFTVHPR 900
VKPVLEKRRE MAYEGKVDWA FAELLALGTM ISEGKLVRLS GQDTRRGTFT 950
QRHSVVIDRK TGKEFTPLQL LATDSDGNPT GGKFLVYDSP LSEFAAVGFE 1000
YGYSVGNPDA MVLWEAQFGD FINGAQSIID EFISSGEAKW GQLSDVVLLL 1050
PHGHEGQGPD HTSGRIERFL QLWAEGSMTI ALPSTPANYF HLLRRHSLDG 1100
IQRPLIVFTP KSMLRNKAAV SDIRDFTEQK FRSVLEEPTY TDGDGDRNKV 1150
TRILLTSGKI YYELVARKNK ESRDDVAIVR IEQLAPLPKR RLAETLDKYP 1200
NVEEKFWVQE EPANQGAWPT FGLTLPEMLP DHFTGIKRIS RRAMSAPSSG 1250
SSKVHAVEQQ EILDEAFAP 1269
Length:1,269
Mass (Da):140,119
Last modified:February 6, 2007 - v1
Checksum:iF6F4221B80E76B83
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000518 Genomic DNA. Translation: ABL93239.1.
RefSeqiYP_940029.1. NC_008705.1.

Genome annotation databases

EnsemblBacteriaiABL93239; ABL93239; Mkms_4047.
GeneIDi4611987.
KEGGimkm:Mkms_4047.
PATRICi18107106. VBIMycSp70743_4570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000518 Genomic DNA. Translation: ABL93239.1 .
RefSeqi YP_940029.1. NC_008705.1.

3D structure databases

ProteinModelPortali A1UK81.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 189918.Mkms_4047.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL93239 ; ABL93239 ; Mkms_4047 .
GeneIDi 4611987.
KEGGi mkm:Mkms_4047.
PATRICi 18107106. VBIMycSp70743_4570.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00997 .
UPA00223 ; UER01001 .
BioCyci MSP189918:GH4X-4086-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: KMS.

Entry informationi

Entry nameiKGD_MYCSK
AccessioniPrimary (citable) accession number: A1UK81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 56 of the entry and version 1 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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