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Q0I316 (MEND_HISS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:HS_0617
OrganismHistophilus somni (strain 129Pt) (Haemophilus somnus) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length568 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 – 5685682-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659
PRO_0000341756

Sequences

Sequence LengthMass (Da)Tools
Q0I316 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 83A7C0CCC0908D3A

FASTA56863,786
        10         20         30         40         50         60 
MSASVFNRCW SKVILETLSR QGVSHFCIAP GSRSTPLTLE AIRLQENGRG TCHAHFDERS 

        70         80         90        100        110        120 
LGFFALGIAK ASKKPVAVIV TSGTATANLY PAIIEARQTD VPLIILTADR PPELLECGAN 

       130        140        150        160        170        180 
QAILQQNMFA QYPIASINLP RPSQNYSAQW LISVLDQACF RQKQGGVIHI NVPFAEPLYN 

       190        200        210        220        230        240 
ANNDEIDLHP WLSNIQSWLT QNKNWIQHQE QHTEVITHKY WDQWRTKKGI IIVGRLPSEQ 

       250        260        270        280        290        300 
AMGIAEWADN MGWIMITDIQ SHVKPTLPYA DIWLANQTVR KKLLQAEIVI QFGSGFIGKR 

       310        320        330        340        350        360 
INQFLAEFKG EYWIIENNQK AVDPYHHAHT RFNAKPHHWL RAHPPMRKKP WLLEPLALAK 

       370        380        390        400        410        420 
FCADFIKQRV GSNLNEASLA HNIELLLPKS NSVLFLGNSL FVRLADALSQ PSANYPIYTN 

       430        440        450        460        470        480 
RGASGIDGLL ATAAGIAVGS EQTLVAMIGD TSTLYDLNSF ALFKQLNQPA IIFVINNNGG 

       490        500        510        520        530        540 
AIFDMLPVDI AVKEKYYRMS HYLEFSHIAA MFDLKYARPY TWADLATVLK QAYSRRETTV 

       550        560 
IEIKVNPNDG SNIYKDLIDK IGHALIGV 

« Hide

References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI24894.1.
RefSeqYP_718829.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205914.HS_0617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI24894; ABI24894; HS_0617.
GeneID4240103.
KEGGhso:HS_0617.
PATRIC20281207. VBIHaeSom53361_0646.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1165.
HOGENOMHOG000218360.
KOK02551.
OMADGGGIFH.
OrthoDBEOG6NWBQW.
ProtClustDBPRK07449.

Enzyme and pathway databases

BioCycHSOM205914:GJ7V-644-MONOMER.
UniPathwayUPA00079; UER00164.

Family and domain databases

HAMAPMF_01659. MenD.
InterProIPR004433. MenaQ_synth_MenD.
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.
TIGRFAMsTIGR00173. menD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMEND_HISS1
AccessionPrimary (citable) accession number: Q0I316
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: October 3, 2006
Last modified: February 19, 2014
This is version 63 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