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C0ZV17 (MEND_RHOE4) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 37. 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:
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase

Short name=SEPHCHC synthase
EC=2.2.1.9
Alternative name(s):
Menaquinone biosynthesis protein MenD
Gene names
Name:menD
Ordered Locus Names:RER_17040
OrganismRhodococcus erythropolis (strain PR4 / NBRC 100887) [Complete proteome] [HAMAP]
Taxonomic identifier234621 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length537 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) By similarity. HAMAP-Rule MF_01659

Catalytic activity

Isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2. HAMAP-Rule MF_01659

Cofactor

Magnesium or manganese By similarity. HAMAP-Rule MF_01659

Binds 1 thiamine pyrophosphate per subunit By similarity.

Pathway

Cofactor biosynthesis; menaquinone biosynthesis; menaquinone-2 from chorismate: step 2/8. HAMAP-Rule MF_01659

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01659

Sequence similarities

Belongs to the TPP enzyme family. MenD subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5375372-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659
PRO_1000215861

Sequences

Sequence LengthMass (Da)Tools
C0ZV17 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 77FA0F6247E6CBF6

FASTA53755,603
        10         20         30         40         50         60 
MNPSTAQATA VVDELVRGGV REVVLCPGSR NAPLAFALQA ADLDGRLRLH MRIDERTAGF 

        70         80         90        100        110        120 
LALGLAIAGK RPVPIVMTSG TAVANLGPAV LEANYARVPL VVLSANRPYE MLGTGANQTV 

       130        140        150        160        170        180 
EQLGLFGSQV RATISLGLAE DDSTQNSQWR SAVCRVLAAA RGTRSGNAGP VHFDIPLREP 

       190        200        210        220        230        240 
LVPDVHVHGP VPEGRPGGAA WTTTQNATLD VPVDLDLTAD TVVISGHGSA LRPELAGLPT 

       250        260        270        280        290        300 
VAEPTAPMHG IALHPLALSQ LKPKQAIITG RPTLHRQVSK VLADPSVDVY ALTTGPRWPD 

       310        320        330        340        350        360 
VSGNVLATGT RAVVTGTPDP AWIARCAALT EHAETAVRKQ LDAHPKATGL HVAAAVMDAL 

       370        380        390        400        410        420 
ADGDQLLLGA SNPVRDAALV SYPKPAVRVL SNRGVAGIDG TVSAAVGAAL AYEGGRTVAL 

       430        440        450        460        470        480 
MGDLTFLHDA SGLLIGTGEP RPSDLTIVVA NDDGGGIFEL LEQGDPQYAG VFERVFGTPH 

       490        500        510        520        530 
GMDLAALCAA YRVPHAAVTV DALATTLAQP ANGIRVLEVA TDRSGLRELH ASVRAQL 

« Hide

References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PR4 / NBRC 100887.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008957 Genomic DNA. Translation: BAH32412.1.
RefSeqYP_002765151.1. NC_012490.1.

3D structure databases

ProteinModelPortalC0ZV17.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234621.RER_17040.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH32412; BAH32412; RER_17040.
GeneID7715197.
KEGGrer:RER_17040.
PATRIC23189778. VBIRhoEry66701_2190.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1165.
HOGENOMHOG000218359.
KOK02551.
OMAWRSAVCR.
OrthoDBEOG6NWBQW.

Enzyme and pathway databases

BioCycRERY234621:GHDE-1723-MONOMER.
UniPathwayUPA00079; UER00164.

Family and domain databases

Gene3D3.40.50.970. 2 hits.
HAMAPMF_01659. MenD.
InterProIPR004433. MenaQ_synth_MenD.
IPR029061. THDP-binding.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamPF02775. TPP_enzyme_C. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFPIRSF004983. MenD. 1 hit.
SUPFAMSSF52518. SSF52518. 2 hits.
TIGRFAMsTIGR00173. menD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMEND_RHOE4
AccessionPrimary (citable) accession number: C0ZV17
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: June 11, 2014
This is version 37 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