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A3Q3N5

- KGD_MYCSJ

UniProt

A3Q3N5 - KGD_MYCSJ

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Protein

Multifunctional 2-oxoglutarate metabolism enzyme

Gene

kgd

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).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 activityBy similarity
Binding sitei617 – 61712-oxoglutarateBy similarity
Binding sitei642 – 64212-oxoglutarateBy similarity
Metal bindingi681 – 6811MagnesiumBy similarity
Metal bindingi714 – 7141MagnesiumBy similarity
Metal bindingi716 – 7161Magnesium; via carbonyl oxygenBy similarity
Binding sitei988 – 9881Thiamine pyrophosphateBy similarity
Binding sitei1056 – 105612-oxoglutarateBy similarity
Binding sitei1074 – 10741Allosteric activatorBy similarity
Binding sitei1090 – 10901Allosteric activatorBy similarity
Binding sitei1178 – 11781Allosteric activatorBy 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).By similarity

Protein-protein interaction databases

STRINGi164757.Mjls_3987.

Structurei

3D structure databases

ProteinModelPortaliA3Q3N5.
ModBaseiSearch...
MobiDBiSearch...

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 bindingBy similarity
Regioni642 – 6443Thiamine pyrophosphate bindingBy similarity
Regioni681 – 6833Thiamine pyrophosphate bindingBy similarity
Regioni1125 – 11284Allosteric activatorBy similarity
Regioni1185 – 11862Allosteric activatorBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili819 – 85032Sequence AnalysisAdd
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSSPSPFGQ NEWLVEEMYR KFREDPSSVD PSWHEFLVDY NPEPTTDSSA
60 70 80 90 100
SENGQQTRTA APKAPPEPAP APAPKSQDSK SQAPKQDSKP QESKPQAKAK
110 120 130 140 150
PAESKSSTKP ADAKSEKSGK SGTNGAAKPA AQPADDSDQN QVLRGAAAAV
160 170 180 190 200
AKNMSASLDV PTATSVRAIP AKLMIDNRVV INNHLKRTRG GKISFTHLIG
210 220 230 240 250
YAIVAAVKKF PNMNRHFAEV DGKPNAVTPA HTNLGLAIDL QGKDGNRQLV
260 270 280 290 300
VAAIKKADTM RFGQFIAAYE DIVRRARDGK LTAEDFSGVT ISLTNPGTIG
310 320 330 340 350
TVHSVPRLMR GQGAIIGVGA MEYPAEFQGA SEERIADLGI GKLITLTSTY
360 370 380 390 400
DHRIIQGAES GDFLRTVHQL LLSDDFFDEI FRELGIPYEP VRWRTDNPDS
410 420 430 440 450
IEDKNARVIE LIAAYRNRGH LMADIDPLRL DSNRFRSHPD LDVLTHGLTL
460 470 480 490 500
WDLDREFKVN GFAGAERKKL RDVLAVLRDA YCRHIGVEYT HILEPEQQQW
510 520 530 540 550
LQERIEGKHE KPTVAQQKYI LSRLNAAEAF ETFLQTKYVG QKRFSLEGAE
560 570 580 590 600
TVIPAMDAVI DQCAEHALDE VVIGMPHRGR LNVLANIVGK PYSQIFSEFE
610 620 630 640 650
GNLNPSQAHG SGDVKYHLGS SGTYLQMFGD NDITVSLTAN PSHLEAVDPV
660 670 680 690 700
MEGLVRAKQD LLDKGDTEDG YTVVPLMLHG DAAFAGQGVV AETLNLALLR
710 720 730 740 750
GYRTGGTIHL IVNNQIGFTT SPAAAKSSEY CTDVAKMIGA PIFHVNGDDP
760 770 780 790 800
EAAVWVSRLA VDFRQKFKKD VVIDLLCYRR RGHNEGDDPS MTQPSMYDVI
810 820 830 840 850
DTKRGVRKSY TEALIGRGDI SMKEAEDALR DYQGQLEQVF NEVRELEKHE
860 870 880 890 900
IEPSESVEAD QQIPAKLATA VDKSLLARIG DAHLAVPEGF TVHPRVKPVL
910 920 930 940 950
EKRREMAYEG KVDWAFAELL ALGTMISEGK LVRLSGQDTR RGTFTQRHSV
960 970 980 990 1000
VIDRKTGKEF TPLQLLATDS DGNPTGGKFL VYDSPLSEFA AVGFEYGYSV
1010 1020 1030 1040 1050
GNPDAMVLWE AQFGDFINGA QSIIDEFISS GEAKWGQLSD VVLLLPHGHE
1060 1070 1080 1090 1100
GQGPDHTSGR IERFLQLWAE GSMTIALPST PANYFHLLRR HSLDGIQRPL
1110 1120 1130 1140 1150
IVFTPKSMLR NKAAVSDIRD FTEQKFRSVL EEPTYTDGDG DRNKVTRILL
1160 1170 1180 1190 1200
TSGKIYYELV ARKNKESRDD VAIVRIEQLA PLPKRRLAET LDKYPNVDEK
1210 1220 1230 1240 1250
FWVQEEPANQ GAWPTFGLTL PEMLPDHFTG IKRISRRAMS APSSGSSKVH
1260
AVEQQEILDE AFAP
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: October 1, 2014
This is version 57 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