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B0RCZ5 (MEND_CLAMS) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 48. 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:CMS3017
OrganismClavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum) [Complete proteome] [HAMAP]
Taxonomic identifier31964 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeClavibacter

Protein attributes

Sequence length589 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 – 5895892-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659
PRO_0000341725

Sequences

Sequence LengthMass (Da)Tools
B0RCZ5 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 82920B3D1DDA1B78

FASTA58961,555
        10         20         30         40         50         60 
MAAADALPTS SASASASADG PRTGNPSTDR AIAMLLALVR EGVTDVVLCP GSRSQALALV 

        70         80         90        100        110        120 
AAELERVDGV RLHVRIDERA AGFLALGLGV ESGRPAPVIT TSGTAVANLH PAVLEGWHSG 

       130        140        150        160        170        180 
VPMLLLTGDR PAELRGIASN QTTRQPGMFG DRVACIDVPA PEETDDDLAR DALLARDAYR 

       190        200        210        220        230        240 
RARDERTPVH VNVAFRDPLS VAVPDLTEAV AEVRAAAPAT PAPAGPATAD VLDLPHGPRT 

       250        260        270        280        290        300 
LVVAGHAAGE AAEELARAGG WPLAAEISSG SHFGPNLVVS FRELLAREGF GDRVERVIVF 

       310        320        330        340        350        360 
GHPTLTREVP LLVGREDVEA IVVGSTGGED YDPRHRVTAH PAAVRVVGEP ADPAEARRWL 

       370        380        390        400        410        420 
GTWVHESRAI LDEATAAESA PLLPSGTTPA ERRDFARAEL AAVRADVTRR HLVRALWQAT 

       430        440        450        460        470        480 
WPHDRLVLGA SRLIREADRA LPGKRVRVHA NRGLAGIDGT ISTGLGIALA SQAGSGSAAA 

       490        500        510        520        530        540 
GITRVLVGDL TLLHDVGSLL IGTGERVPRI QVIVGNDGGG TIFDGLEVSR TAAPASIDRV 

       550        560        570        580 
MFTPQRVDLA SLARAYGWAH LRAATHGELE AALTTASEAP LLIEVPLAR 

« Hide

References

[1]"Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp. sepedonicus suggests recent niche adaptation."
Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J., Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D., Parkhill J., Ishimaru C.A.
J. Bacteriol. 190:2150-2160(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM849034 Genomic DNA. Translation: CAQ03087.1.
RefSeqYP_001711643.1. NC_010407.1.

3D structure databases

ProteinModelPortalB0RCZ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING31964.CMS_3017.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ03087; CAQ03087; CMS3017.
GeneID6158519.
KEGGcms:CMS_3017.
PATRIC21463057. VBIClaMic4666_3062.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1165.
KOK02551.
OMAWRSAVCR.
OrthoDBEOG6NWBQW.

Enzyme and pathway databases

BioCycCMIC31964:GJBN-3011-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_CLAMS
AccessionPrimary (citable) accession number: B0RCZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: April 8, 2008
Last modified: June 11, 2014
This is version 48 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