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A3Q3N5

- KGD_MYCSJ

UniProt

A3Q3N5 - KGD_MYCSJ

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Protein

Multifunctional 2-oxoglutarate metabolism enzyme

Gene
kgd, Mjls_3987
Organism
Mycobacterium sp. (strain JLS)
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 sitei352 – 3521Proton acceptor; for succinyltransferase activity By similarity
Binding sitei617 – 61712-oxoglutarate By similarity
Binding sitei642 – 64212-oxoglutarate By similarity
Metal bindingi681 – 6811Magnesium By similarity
Metal bindingi714 – 7141Magnesium By similarity
Metal bindingi716 – 7161Magnesium; via carbonyl oxygen By similarity
Binding sitei988 – 9881Thiamine pyrophosphate By similarity
Binding sitei1056 – 105612-oxoglutarate By similarity
Binding sitei1074 – 10741Allosteric activator By similarity
Binding sitei1090 – 10901Allosteric activator By similarity
Binding sitei1178 – 11781Allosteric 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

BioCyciMSP164757:GHV3-4022-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:Mjls_3987
OrganismiMycobacterium sp. (strain JLS)
Taxonomic identifieri164757 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000002152: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12641264Multifunctional 2-oxoglutarate metabolism enzymePRO_0000310719Add
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

STRINGi164757.Mjls_3987.

Structurei

3D structure databases

ProteinModelPortaliA3Q3N5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 41412-oxoglutarate dehydrogenase E1, N-terminal partAdd
BLAST
Regioni42 – 10261LinkerAdd
BLAST
Regioni103 – 373271Succinyltransferase E2Add
BLAST
Regioni374 – 12648912-oxoglutarate dehydrogenase E1, C-terminal partAdd
BLAST
Regioni577 – 5782Thiamine pyrophosphate binding By similarity
Regioni642 – 6443Thiamine pyrophosphate binding By similarity
Regioni681 – 6833Thiamine pyrophosphate binding By similarity
Regioni1125 – 11284Allosteric activator By similarity
Regioni1185 – 11862Allosteric activator By similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili819 – 85032 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.
OMAiGHQNANL.
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.

A3Q3N5-1 [UniParc]FASTAAdd to Basket

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MSSSPSPFGQ NEWLVEEMYR KFREDPSSVD PSWHEFLVDY NPEPTTDSSA     50
SENGQQTRTA APKAPPEPAP APAPKSQDSK SQAPKQDSKP QESKPQAKAK 100
PAESKSSTKP ADAKSEKSGK SGTNGAAKPA AQPADDSDQN QVLRGAAAAV 150
AKNMSASLDV PTATSVRAIP AKLMIDNRVV INNHLKRTRG GKISFTHLIG 200
YAIVAAVKKF PNMNRHFAEV DGKPNAVTPA HTNLGLAIDL QGKDGNRQLV 250
VAAIKKADTM RFGQFIAAYE DIVRRARDGK LTAEDFSGVT ISLTNPGTIG 300
TVHSVPRLMR GQGAIIGVGA MEYPAEFQGA SEERIADLGI GKLITLTSTY 350
DHRIIQGAES GDFLRTVHQL LLSDDFFDEI FRELGIPYEP VRWRTDNPDS 400
IEDKNARVIE LIAAYRNRGH LMADIDPLRL DSNRFRSHPD LDVLTHGLTL 450
WDLDREFKVN GFAGAERKKL RDVLAVLRDA YCRHIGVEYT HILEPEQQQW 500
LQERIEGKHE KPTVAQQKYI LSRLNAAEAF ETFLQTKYVG QKRFSLEGAE 550
TVIPAMDAVI DQCAEHALDE VVIGMPHRGR LNVLANIVGK PYSQIFSEFE 600
GNLNPSQAHG SGDVKYHLGS SGTYLQMFGD NDITVSLTAN PSHLEAVDPV 650
MEGLVRAKQD LLDKGDTEDG YTVVPLMLHG DAAFAGQGVV AETLNLALLR 700
GYRTGGTIHL IVNNQIGFTT SPAAAKSSEY CTDVAKMIGA PIFHVNGDDP 750
EAAVWVSRLA VDFRQKFKKD VVIDLLCYRR RGHNEGDDPS MTQPSMYDVI 800
DTKRGVRKSY TEALIGRGDI SMKEAEDALR DYQGQLEQVF NEVRELEKHE 850
IEPSESVEAD QQIPAKLATA VDKSLLARIG DAHLAVPEGF TVHPRVKPVL 900
EKRREMAYEG KVDWAFAELL ALGTMISEGK LVRLSGQDTR RGTFTQRHSV 950
VIDRKTGKEF TPLQLLATDS DGNPTGGKFL VYDSPLSEFA AVGFEYGYSV 1000
GNPDAMVLWE AQFGDFINGA QSIIDEFISS GEAKWGQLSD VVLLLPHGHE 1050
GQGPDHTSGR IERFLQLWAE GSMTIALPST PANYFHLLRR HSLDGIQRPL 1100
IVFTPKSMLR NKAAVSDIRD FTEQKFRSVL EEPTYTDGDG DRNKVTRILL 1150
TSGKIYYELV ARKNKESRDD VAIVRIEQLA PLPKRRLAET LDKYPNVDEK 1200
FWVQEEPANQ GAWPTFGLTL PEMLPDHFTG IKRISRRAMS APSSGSSKVH 1250
AVEQQEILDE AFAP 1264
Length:1,264
Mass (Da):139,593
Last modified:April 3, 2007 - v1
Checksum:iC5068956C2130DAC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000580 Genomic DNA. Translation: ABN99762.1.
RefSeqiWP_011856407.1. NC_009077.1.
YP_001072253.1. NC_009077.1.

Genome annotation databases

EnsemblBacteriaiABN99762; ABN99762; Mjls_3987.
GeneIDi4879696.
KEGGimjl:Mjls_3987.
PATRICi18094212. VBIMycSp51234_4021.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000580 Genomic DNA. Translation: ABN99762.1 .
RefSeqi WP_011856407.1. NC_009077.1.
YP_001072253.1. NC_009077.1.

3D structure databases

ProteinModelPortali A3Q3N5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 164757.Mjls_3987.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABN99762 ; ABN99762 ; Mjls_3987 .
GeneIDi 4879696.
KEGGi mjl:Mjls_3987.
PATRICi 18094212. VBIMycSp51234_4021.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00997 .
UPA00223 ; UER01001 .
BioCyci MSP164757:GHV3-4022-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: JLS.

Entry informationi

Entry nameiKGD_MYCSJ
AccessioniPrimary (citable) accession number: A3Q3N5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: April 3, 2007
Last modified: September 3, 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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