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Q4L547 (MEND_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. 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:SH1919
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length556 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 – 5565562-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659
PRO_0000341865

Sequences

Sequence LengthMass (Da)Tools
Q4L547 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: FE88BE461C5A72D0

FASTA55663,095
        10         20         30         40         50         60 
MNHNEALTKQ VYTFASELYA YGVREVVISP GSRSTPLAIA FEAHPNIKTW IHPDERSAAF 

        70         80         90        100        110        120 
FALGLIKGSE RPVAILCTSG TAAANYTPAI AESQISRIPL IVLTSDRPHE LRSVGAPQAI 

       130        140        150        160        170        180 
NQVNMFANYV NFQFDMPVAD GTDYMLDAIY YQMQIASQYL YGPHRGPIHF NLPFREPLTP 

       190        200        210        220        230        240 
NLERQEWLTS YSKKLPHYQK NINVQDIRHI LKEKKGLIIV GDMQHQAIDQ ILTYATVHDI 

       250        260        270        280        290        300 
PILADPLSQL RKYNHPNVIT TYDLYYRAGL DIDVDFVIRV GKPVISKKLN QWLKRTNAYQ 

       310        320        330        340        350        360 
ILVQNNDKID VFPTPPSISY EISANDFFRN LIEEAAVDRK DWINMWRTLE SQARNTIDKH 

       370        380        390        400        410        420 
MTNATDEAAF VKILIDKLTK DDAIFVSNSM PVRDIDNLLY NSEVEVYANR GANGIDGVVS 

       430        440        450        460        470        480 
TAIGMAVHKK ITLIIGDLAF YHDMNGLLMA KINNINLNIV LLNNDGGGIF SYLPQKASAE 

       490        500        510        520        530        540 
AYFERLFGTP TGLNFEYTAL LYDFTFKRFN TVADFTQEKL SHVNSHIYEM VTNRDDNMSQ 

       550 
HQILYKKLSG ILNVTL 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC1435.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006716 Genomic DNA. Translation: BAE05228.1.
RefSeqYP_253834.1. NC_007168.1.

3D structure databases

ProteinModelPortalQ4L547.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279808.SH1919.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE05228; BAE05228; SH1919.
GeneID3482100.
KEGGsha:SH1919.
PATRIC19619943. VBIStaHae67511_1894.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1165.
HOGENOMHOG000218359.
KOK02551.
OMAQKPWLLE.
OrthoDBEOG6NWBQW.

Enzyme and pathway databases

BioCycSHAE279808:GJX7-1974-MONOMER.
UniPathwayUPA00079; UER00164.

Family and domain databases

Gene3D3.40.50.970. 2 hits.
HAMAPMF_01659. MenD.
InterProIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR004433. 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.
SUPFAMSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsTIGR00173. menD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMEND_STAHJ
AccessionPrimary (citable) accession number: Q4L547
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: August 2, 2005
Last modified: June 11, 2014
This is version 67 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