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Q1B4V6 (KGD_MYCSS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Multifunctional 2-oxoglutarate metabolism enzyme
Alternative name(s):
2-hydroxy-3-oxoadipate synthase
Short name=HOA synthase
Short name=HOAS
EC=2.2.1.5
2-oxoglutarate carboxy-lyase
2-oxoglutarate decarboxylase
Alpha-ketoglutarate decarboxylase
Short name=KG decarboxylase
Short name=KGD
EC=4.1.1.71
Alpha-ketoglutarate-glyoxylate carboligase

Including the following 2 domains:

  1. 2-oxoglutarate dehydrogenase E1 component
    Short name=ODH E1 component
    EC=1.2.4.2
    Alternative name(s):
    Alpha-ketoglutarate dehydrogenase E1 component
    Short name=KDH E1 component
  2. 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 names
Name:kgd
Ordered Locus Names:Mmcs_3973
OrganismMycobacterium sp. (strain MCS) [Complete proteome] [HAMAP]
Taxonomic identifier164756 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length1269 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

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.

Cofactor

Magnesium By similarity.

Thiamine pyrophosphate By similarity.

Enzyme regulation

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.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2.

Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.

Subunit structure

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.

Domain

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 similarities

Belongs to the 2-oxoacid dehydrogenase family. Kgd subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12691269Multifunctional 2-oxoglutarate metabolism enzyme
PRO_0000310721

Regions

Region1 – 41412-oxoglutarate dehydrogenase E1, N-terminal part
Region42 – 10766Linker
Region108 – 378271Succinyltransferase E2
Region379 – 12698912-oxoglutarate dehydrogenase E1, C-terminal part
Region582 – 5832Thiamine pyrophosphate binding By similarity
Region647 – 6493Thiamine pyrophosphate binding By similarity
Region686 – 6883Thiamine pyrophosphate binding By similarity
Region1130 – 11334Allosteric activator By similarity
Region1190 – 11912Allosteric activator By similarity
Coiled coil824 – 85532 Potential

Sites

Active site3571Proton acceptor; for succinyltransferase activity By similarity
Metal binding6861Magnesium By similarity
Metal binding7191Magnesium By similarity
Metal binding7211Magnesium; via carbonyl oxygen By similarity
Binding site62212-oxoglutarate By similarity
Binding site64712-oxoglutarate By similarity
Binding site9931Thiamine pyrophosphate By similarity
Binding site106112-oxoglutarate By similarity
Binding site10791Allosteric activator By similarity
Binding site10951Allosteric activator By similarity
Binding site11831Allosteric activator By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1B4V6 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: F6F4221B80E76B83

FASTA1,269140,119
        10         20         30         40         50         60 
MSSSPSPFGQ NEWLVEEMYR KFREDPSSVD PSWHEFLVDY NPEPTTDSSA SENGQQTRTA 

        70         80         90        100        110        120 
APKAPPEPAP APAPKTPDSK TPDSKSQAPK QDSKPQESKP QAKAKPAESK SSTKPADAKS 

       130        140        150        160        170        180 
EKSGKSGTNG AAKPAAQPAD DSDQNQVLRG AAAAVAKNMS ASLDVPTATS VRAIPAKLMI 

       190        200        210        220        230        240 
DNRVVINNHL KRTRGGKISF THLIGYAIVA AVKKFPNMNR HFAEVDGKPN AVTPAHTNLG 

       250        260        270        280        290        300 
LAIDLQGKDG NRQLVVAAIK KADTMRFGQF IAAYEDIVRR ARDGKLTAED FSGVTISLTN 

       310        320        330        340        350        360 
PGTIGTVHSV PRLMRGQGAI IGVGAMEYPA EFQGASEERI ADLGIGKLIT LTSTYDHRII 

       370        380        390        400        410        420 
QGAESGDFLR TVHQLLLSDD FFDEIFRELG IPYEPVRWRT DNPDSIEDKN ARVIELIAAY 

       430        440        450        460        470        480 
RNRGHLMADI DPLRLDSNRF RSHPDLDVLT HGLTLWDLDR EFKVNGFAGA ERKKLRDVLA 

       490        500        510        520        530        540 
VLRDAYCRHI GVEYTHILEP EQQQWLQERI EGKHEKPTVA QQKYILSRLN AAEAFETFLQ 

       550        560        570        580        590        600 
TKYVGQKRFS LEGAETVIPA MDAVIDQCAE HALDEVVIGM PHRGRLNVLA NIVGKPYSQI 

       610        620        630        640        650        660 
FSEFEGNLNP SQAHGSGDVK YHLGSSGTYL QMFGDNDITV SLTANPSHLE AVDPVMEGLV 

       670        680        690        700        710        720 
RAKQDLLDKG DTEDGYTVVP LMLHGDAAFA GQGVVAETLN LALLRGYRTG GTIHLIVNNQ 

       730        740        750        760        770        780 
IGFTTSPAAA KSSEYCTDVA KMIGAPIFHV NGDDPEAAVW VSRLAVDFRQ KFKKDVVIDL 

       790        800        810        820        830        840 
LCYRRRGHNE GDDPSMTQPS MYDVIDTKRG VRKSYTEALI GRGDISMKEA EDALRDYQGQ 

       850        860        870        880        890        900 
LEQVFNEVRE LEKHEIEPSE SVEADQQIPA KLATAVDKSL LARIGDAHLA VPEGFTVHPR 

       910        920        930        940        950        960 
VKPVLEKRRE MAYEGKVDWA FAELLALGTM ISEGKLVRLS GQDTRRGTFT QRHSVVIDRK 

       970        980        990       1000       1010       1020 
TGKEFTPLQL LATDSDGNPT GGKFLVYDSP LSEFAAVGFE YGYSVGNPDA MVLWEAQFGD 

      1030       1040       1050       1060       1070       1080 
FINGAQSIID EFISSGEAKW GQLSDVVLLL PHGHEGQGPD HTSGRIERFL QLWAEGSMTI 

      1090       1100       1110       1120       1130       1140 
ALPSTPANYF HLLRRHSLDG IQRPLIVFTP KSMLRNKAAV SDIRDFTEQK FRSVLEEPTY 

      1150       1160       1170       1180       1190       1200 
TDGDGDRNKV TRILLTSGKI YYELVARKNK ESRDDVAIVR IEQLAPLPKR RLAETLDKYP 

      1210       1220       1230       1240       1250       1260 
NVEEKFWVQE EPANQGAWPT FGLTLPEMLP DHFTGIKRIS RRAMSAPSSG SSKVHAVEQQ 


EILDEAFAP

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References

[1]"Complete sequence of chromosome of Mycobacterium sp. MCS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000384 Genomic DNA. Translation: ABG10078.1.
RefSeqYP_641134.1. NC_008146.1.

3D structure databases

ProteinModelPortalQ1B4V6.
ModBaseSearch...

Protein-protein interaction databases

STRING164756.Mmcs_3973.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG10078; ABG10078; Mmcs_3973.
GeneID4112803.
KEGGmmc:Mmcs_3973.
PATRIC18118283. VBIMycSp106721_4071.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000259587.
KOK01616.
OMAIIKRGGA.
ProtClustDBPRK12270.

Enzyme and pathway databases

BioCycMSP164756:GHQ8-4259-MONOMER.
UniPathwayUPA00223; UER00997.
UPA00223; UER01001.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
InterProIPR001078. 2-oxoacid_DH_actylTfrase.
IPR011603. 2oxoglutarate_DH_E1.
IPR023213. CAT-like_dom.
IPR001017. DH_E1.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERPTHR23152. PTHR23152. 1 hit.
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKGD_MYCSS
AccessionPrimary (citable) accession number: Q1B4V6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: July 11, 2006
Last modified: May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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