Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A3Q3N5 (KGD_MYCSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Mjls_3987
OrganismMycobacterium sp. (strain JLS) [Complete proteome] [HAMAP]
Taxonomic identifier164757 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length1264 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 – 12641264Multifunctional 2-oxoglutarate metabolism enzyme
PRO_0000310719

Regions

Region1 – 41412-oxoglutarate dehydrogenase E1, N-terminal part
Region42 – 10261Linker
Region103 – 373271Succinyltransferase E2
Region374 – 12648912-oxoglutarate dehydrogenase E1, C-terminal part
Region577 – 5782Thiamine pyrophosphate binding By similarity
Region642 – 6443Thiamine pyrophosphate binding By similarity
Region681 – 6833Thiamine pyrophosphate binding By similarity
Region1125 – 11284Allosteric activator By similarity
Region1185 – 11862Allosteric activator By similarity
Coiled coil819 – 85032 Potential

Sites

Active site3521Proton acceptor; for succinyltransferase activity By similarity
Metal binding6811Magnesium By similarity
Metal binding7141Magnesium By similarity
Metal binding7161Magnesium; via carbonyl oxygen By similarity
Binding site61712-oxoglutarate By similarity
Binding site64212-oxoglutarate By similarity
Binding site9881Thiamine pyrophosphate By similarity
Binding site105612-oxoglutarate By similarity
Binding site10741Allosteric activator By similarity
Binding site10901Allosteric activator By similarity
Binding site11781Allosteric activator By similarity

Sequences

Sequence LengthMass (Da)Tools
A3Q3N5 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: C5068956C2130DAC

FASTA1,264139,593
        10         20         30         40         50         60 
MSSSPSPFGQ NEWLVEEMYR KFREDPSSVD PSWHEFLVDY NPEPTTDSSA SENGQQTRTA 

        70         80         90        100        110        120 
APKAPPEPAP APAPKSQDSK SQAPKQDSKP QESKPQAKAK PAESKSSTKP ADAKSEKSGK 

       130        140        150        160        170        180 
SGTNGAAKPA AQPADDSDQN QVLRGAAAAV AKNMSASLDV PTATSVRAIP AKLMIDNRVV 

       190        200        210        220        230        240 
INNHLKRTRG GKISFTHLIG YAIVAAVKKF PNMNRHFAEV DGKPNAVTPA HTNLGLAIDL 

       250        260        270        280        290        300 
QGKDGNRQLV VAAIKKADTM RFGQFIAAYE DIVRRARDGK LTAEDFSGVT ISLTNPGTIG 

       310        320        330        340        350        360 
TVHSVPRLMR GQGAIIGVGA MEYPAEFQGA SEERIADLGI GKLITLTSTY DHRIIQGAES 

       370        380        390        400        410        420 
GDFLRTVHQL LLSDDFFDEI FRELGIPYEP VRWRTDNPDS IEDKNARVIE LIAAYRNRGH 

       430        440        450        460        470        480 
LMADIDPLRL DSNRFRSHPD LDVLTHGLTL WDLDREFKVN GFAGAERKKL RDVLAVLRDA 

       490        500        510        520        530        540 
YCRHIGVEYT HILEPEQQQW LQERIEGKHE KPTVAQQKYI LSRLNAAEAF ETFLQTKYVG 

       550        560        570        580        590        600 
QKRFSLEGAE TVIPAMDAVI DQCAEHALDE VVIGMPHRGR LNVLANIVGK PYSQIFSEFE 

       610        620        630        640        650        660 
GNLNPSQAHG SGDVKYHLGS SGTYLQMFGD NDITVSLTAN PSHLEAVDPV MEGLVRAKQD 

       670        680        690        700        710        720 
LLDKGDTEDG YTVVPLMLHG DAAFAGQGVV AETLNLALLR GYRTGGTIHL IVNNQIGFTT 

       730        740        750        760        770        780 
SPAAAKSSEY CTDVAKMIGA PIFHVNGDDP EAAVWVSRLA VDFRQKFKKD VVIDLLCYRR 

       790        800        810        820        830        840 
RGHNEGDDPS MTQPSMYDVI DTKRGVRKSY TEALIGRGDI SMKEAEDALR DYQGQLEQVF 

       850        860        870        880        890        900 
NEVRELEKHE IEPSESVEAD QQIPAKLATA VDKSLLARIG DAHLAVPEGF TVHPRVKPVL 

       910        920        930        940        950        960 
EKRREMAYEG KVDWAFAELL ALGTMISEGK LVRLSGQDTR RGTFTQRHSV VIDRKTGKEF 

       970        980        990       1000       1010       1020 
TPLQLLATDS DGNPTGGKFL VYDSPLSEFA AVGFEYGYSV GNPDAMVLWE AQFGDFINGA 

      1030       1040       1050       1060       1070       1080 
QSIIDEFISS GEAKWGQLSD VVLLLPHGHE GQGPDHTSGR IERFLQLWAE GSMTIALPST 

      1090       1100       1110       1120       1130       1140 
PANYFHLLRR HSLDGIQRPL IVFTPKSMLR NKAAVSDIRD FTEQKFRSVL EEPTYTDGDG 

      1150       1160       1170       1180       1190       1200 
DRNKVTRILL TSGKIYYELV ARKNKESRDD VAIVRIEQLA PLPKRRLAET LDKYPNVDEK 

      1210       1220       1230       1240       1250       1260 
FWVQEEPANQ GAWPTFGLTL PEMLPDHFTG IKRISRRAMS APSSGSSKVH AVEQQEILDE 


AFAP 

« Hide

References

[1]"Complete sequence of Mycobacterium sp. JLS."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J., Sims R.C., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JLS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000580 Genomic DNA. Translation: ABN99762.1.
RefSeqYP_001072253.1. NC_009077.1.

3D structure databases

ProteinModelPortalA3Q3N5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING164757.Mjls_3987.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN99762; ABN99762; Mjls_3987.
GeneID4879696.
KEGGmjl:Mjls_3987.
PATRIC18094212. VBIMycSp51234_4021.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000259587.
KOK01616.
OMAGHQNANL.
OrthoDBEOG6V1M1F.

Enzyme and pathway databases

BioCycMSP164757:GHV3-4022-MONOMER.
UniPathwayUPA00223; UER00997.
UPA00223; UER01001.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
3.40.50.970. 2 hits.
InterProIPR001078. 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]
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]
SUPFAMSSF52518. SSF52518. 2 hits.
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKGD_MYCSJ
AccessionPrimary (citable) accession number: A3Q3N5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: April 3, 2007
Last modified: June 11, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways