Skip Header

Contribute Send feedback
Read comments (?) or add your own

E4W8B1 (E4W8B1_RHOE1) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 17. Feed History...

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

Names and origin

Protein namesRecommended name:
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659
Short name=SEPHCHC synthase HAMAP-Rule MF_01659
EC=2.2.1.9 HAMAP-Rule MF_01659
Alternative name(s):
Menaquinone biosynthesis protein MenD HAMAP-Rule MF_01659
Gene names
Name:menD HAMAP-Rule MF_01659 EMBL CBH49686.1
Ordered Locus Names:REQ_36990 EMBL CBH49686.1
OrganismRhodococcus equi (strain 103S) (Corynebacterium equi) [Complete proteome] [HAMAP]
Taxonomic identifier685727 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus ›

Protein attributes

Sequence length548 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 SAAS SAAS012001

Catalytic activity

Isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2. HAMAP-Rule MF_01659 SAAS SAAS012001

Cofactor

Binds 1 thiamine pyrophosphate per subunit By similarity. HAMAP-Rule MF_01659 SAAS SAAS012001

Magnesium or manganese By similarity. HAMAP-Rule MF_01659 SAAS SAAS012001

Pathway

Cofactor biosynthesis; menaquinone biosynthesis; menaquinone-2 from chorismate: step 2/8. HAMAP-Rule MF_01659 SAAS SAAS012001

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01659 SAAS SAAS012001

Sequence similarities

Belongs to the TPP enzyme family. MenD subfamily. HAMAP-Rule MF_01659

Sequences

Sequence LengthMass (Da)Tools
E4W8B1 [UniParc].

Last modified February 8, 2011. Version 1.
Checksum: 864CFE51D4C22D8B

FASTA54857,229
        10         20         30         40         50         60 
MNPSTAQATA VVDELIRGGV REVVLCPGSR NAPLAFALQA ADAAGRLRLH LRIDERTAGF 

        70         80         90        100        110        120 
LAIGLAVASG QPVPVVMTSG TAVANLGPAV LEANYARIPL IVLSANRPYE MLGTGANQTV 

       130        140        150        160        170        180 
EQFGLFGSQV RAAISLGLAE EAGDESQRGI RFDEQNSQWR SAVCRVLAAA RGTRSGNAGP 

       190        200        210        220        230        240 
VHFDIPLREP LVPDVRPRGL VPEGRPGGAA WTTTVHATLD VPMDLDITAD TVVVSGHGSA 

       250        260        270        280        290        300 
YRPELAGLPT VAEPTAPLHG IPLHPLALPQ LKPRQAIITG RPTLHRPVSK LLADPSVAVY 

       310        320        330        340        350        360 
ALTTGPRWPD VSGNVLATGT RAVVTGEPDP AWIARCRHLS EHADKAVRSQ LDAHPTATGL 

       370        380        390        400        410        420 
HVAAAVMEAL SDGDQLLLGA SNPVRDAALV SYPRPGVKVL SNRGVAGIDG TVSTAVGAAL 

       430        440        450        460        470        480 
AYESEGRTVA LLGDLTFLHD ASGLLIGTGE PRPTDLTIVV ANDDGGGIFE LLEQGDPQYA 

       490        500        510        520        530        540 
GVFERVFGTP HGMDLAALCA AYRVPHRRVD LAELTAVLTA PGDGIRVLEV TTERSGLREL 


HAAVRAQL

« Hide

References

[1]"The genome of a pathogenic rhodococcus: cooptive virulence underpinned by key gene acquisitions."
Letek M., Gonzalez P., Macarthur I., Rodriguez H., Freeman T.C., Valero-Rello A., Blanco M., Buckley T., Cherevach I., Fahey R., Hapeshi A., Holdstock J., Leadon D., Navas J., Ocampo A., Quail M.A., Sanders M., Scortti M.M. expand/collapse author list , Prescott J.F., Fogarty U., Meijer W.G., Parkhill J., Bentley S.D., Vazquez-Boland J.A.
PLoS Genet. 6:E1001145-E1001145(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 103S.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FN563149 Genomic DNA. Translation: CBH49686.1.
RefSeqYP_004008365.1. NC_014659.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBH49686; CBH49686; REQ_36990.
GeneID9965964.
KEGGreq:REQ_36990.
PATRIC42664885. VBIRhoEqu141084_3702.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000218359.
KOK02551.
OMAANRPYEM.

Enzyme and pathway databases

BioCycREQU685727:GHKP-4151-MONOMER.
UniPathwayUPA00079; UER00164.

Family and domain databases

HAMAPMF_01659. MenD.
InterProIPR004433. MenaQ_synth_MenD.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
[Graphical view]
PANTHERPTHR18968:SF3. PTHR18968:SF3. 1 hit.
PfamPF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFPIRSF004983. MenD. 1 hit.
TIGRFAMsTIGR00173. menD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameE4W8B1_RHOE1
AccessionPrimary (citable) accession number: E4W8B1
Entry history
Integrated into UniProtKB/TrEMBL: February 8, 2011
Last sequence update: February 8, 2011
Last modified: May 1, 2013
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info