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Q8FSB6 (MEND_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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:CE0478
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length543 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 caution

The sequence BAC17288.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5435432-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659
PRO_0000341727

Sequences

Sequence LengthMass (Da)Tools
Q8FSB6 [UniParc].

Last modified July 1, 2008. Version 2.
Checksum: 8462D61D2D35CDF4

FASTA54357,989
        10         20         30         40         50         60 
MSVTPAQELA REVIEALSPH ITDVVLCPGS RNSPLSLEVL SREDLRVHVR IDERSAAFLA 

        70         80         90        100        110        120 
LGLARVQRRP VPVIMTSGTA VSNCLPAVTE AAHAHIPLLV VSADRPAHLI GTGSSQTIDQ 

       130        140        150        160        170        180 
TDIFGALAPT VTVAAPEHVG RISQALGNGA SQSPRHINVA LDMPLVAPDL PELHGQRGPV 

       190        200        210        220        230        240 
DWEQRWVDHG VVDVDLSRNT LVIAGDEAWE IEELAEVPTI AEPTAPVAYH PVHPLAAEFL 

       250        260        270        280        290        300 
LKDQVSAEGY VVTTRPDHII VVGHPTLHRG VLKLMTDPTI ELTVLSRTDV ITDPGRHADR 

       310        320        330        340        350        360 
VGSRVKVTGE QQKQWLKICD AASDLAAEGV REVLAKEEHG FTGLHVAAAV ADGLGTGDTV 

       370        380        390        400        410        420 
FCAASNPIRD LSIVGLPFAG VDVHSPRGTA GIDGSVSQAI GTALAIQARH PDEIRAPRTV 

       430        440        450        460        470        480 
ALLGDLAFIH DAGGLLIGPD EPRPENLTIV VANDNGGGIF ELLETGAPGL RSRFERAFGT 

       490        500        510        520        530        540 
PHDVNISDLC DAYGVDYRRA NTLQDLLMEL EDTIEIPGFT VIEAVTVRDT RRALQRELTA 


KVR 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC17288.1. Different initiation.
RefSeqNP_737088.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FSB6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196164.CE0478.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC17288; BAC17288; BAC17288.
GeneID1032597.
KEGGcef:CE0478.
PATRIC21487112. VBICorEff9312_0502.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000218359.
KOK02551.
OrthoDBEOG6NWBQW.
ProtClustDBPRK07449.

Enzyme and pathway databases

BioCycCEFF196164:GJW8-487-MONOMER.
UniPathwayUPA00079; UER00164.

Family and domain databases

HAMAPMF_01659. MenD.
InterProIPR004433. MenaQ_synth_MenD.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
[Graphical view]
PfamPF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFPIRSF004983. MenD. 1 hit.
TIGRFAMsTIGR00173. menD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMEND_COREF
AccessionPrimary (citable) accession number: Q8FSB6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 68 of the entry and version 2 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