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A3QJ17 (MEND_SHELP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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:Shew_3599
OrganismShewanella loihica (strain ATCC BAA-1088 / PV-4) [Complete proteome] [HAMAP]
Taxonomic identifier323850 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length567 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 – 5675672-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659
PRO_0000341833

Sequences

Sequence LengthMass (Da)Tools
A3QJ17 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: A875ADE0A0FA446A

FASTA56761,598
        10         20         30         40         50         60 
MQIEKTAELN LLWGSLILEE LARLEVQHVC MAPGSRSTPL TLAAAKQTKL KQHLHFDERG 

        70         80         90        100        110        120 
LGFLALGLAK ASRAPVAIIT TSGTAVANLY PAIVEAWLTQ VPLIVLSGDR PPELLGCGAN 

       130        140        150        160        170        180 
QAIVQPAIFA DYAKQVNLPT PDMAIPPQAL LTLLDESVAN AKGPIHVNCM YREPLYPGSM 

       190        200        210        220        230        240 
SADFTHYLSP LGNWQHSALP YNQFADAQLV SAPTSDALAR FVHGKGVIIA GTLAPEQQPE 

       250        260        270        280        290        300 
QLIELAQKLG WPLLTDAQSQ LRQHGAAIGN IDQLLLQPKA KALLQEADTV LVFGGRLLSK 

       310        320        330        340        350        360 
RLISYLSEQK WKRYWQVLPQ QTRLDPSHSA KQVWISPLAA FAQLPWPRSS EANWALQLIE 

       370        380        390        400        410        420 
ANEQLATLFQ QQIDDAEFGE AQVVRTIAGR GEQQLFIGNS LPVRLYDMYA PITPIAPRVF 

       430        440        450        460        470        480 
TNRGASGIDG LLATACGIAA HKASSTTLVI GDLSQLHDLN SLALAAKQQG TLVIVILNND 

       490        500        510        520        530        540 
GGNIFNLLPV PDEKLRSGYY RLAHGLEFGY GAAMFGLPYN RVEDIVSFNE AYDDALAYPG 

       550        560 
ASVIEVCVAQ DQASEQIARL AAWIKQS 

« Hide

References

[1]"Complete sequence of Shewanella loihica PV-4."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G., Fredrickson J., Tiedje J., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1088 / PV-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000606 Genomic DNA. Translation: ABO25465.1.
RefSeqYP_001095724.1. NC_009092.1.

3D structure databases

ProteinModelPortalA3QJ17.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323850.Shew_3599.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO25465; ABO25465; Shew_3599.
GeneID4922504.
KEGGslo:Shew_3599.
PATRIC23519149. VBISheLoi132094_3602.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1165.
HOGENOMHOG000218360.
KOK02551.
OMAADCTHRI.
OrthoDBEOG6NWBQW.
ProtClustDBPRK07449.

Enzyme and pathway databases

BioCycSLOI323850:GHQJ-3716-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_SHELP
AccessionPrimary (citable) accession number: A3QJ17
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: April 17, 2007
Last modified: February 19, 2014
This is version 56 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