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A2CAW2 (MEND_PROM3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:P9303_18801
OrganismProchlorococcus marinus (strain MIT 9303) [Complete proteome] [HAMAP]
Taxonomic identifier59922 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length582 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 ABM78622.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5825822-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659
PRO_0000341802

Sequences

Sequence LengthMass (Da)Tools
A2CAW2 [UniParc].

Last modified July 1, 2008. Version 2.
Checksum: 808A6C03071EBCE5

FASTA58263,295
        10         20         30         40         50         60 
MGLRHLVLCP GSRSGPLALA AGGMARTNLL RLSTAIDERS AAFLALGFST ATGTAAAVVT 

        70         80         90        100        110        120 
TSGTAVANLL PAAVEADRSC QPLLLLTADR PYRLKDCGAN QTVNQETFLS PACRWIGQGP 

       130        140        150        160        170        180 
REGLHLFSTE TLESFAEEAW QRAHHPAGAV HLNLPFEEPL HLSEEEQRVI WKGWSPKIPR 

       190        200        210        220        230        240 
SAPITPTNLA MAAEGTEGVT DRAPFALDPF RPGVVIAGAW RGLSKDLFAF QQSLREWQAL 

       250        260        270        280        290        300 
SGWPVLADPL SALPSDQPGL IRSWELLLAA GLLGSHEQLQ VLRLGPMSAS RSLEAWLKSF 

       310        320        330        340        350        360 
GDGQLLITEG DSRCLDPLGL SVQWSHGLTT WWQHHHHRWI DADAASQQAT QPLLKKWQII 

       370        380        390        400        410        420 
DRFAQDWLDQ QLPLQGAITE PALARWLSRL LPAELSIMLA ASSPVRDWLA YADKSLFSRR 

       430        440        450        460        470        480 
CFSFRGASGI DGTLSLSMGL AMALGPTLLV SGDLALLHDS NGWLLAHPQR PPLVVVLIDN 

       490        500        510        520        530        540 
GGGGIFEQLL VKKAPSEAFE QLFAMPQAVD PLVLAAAHNI PHRQVACLED LPAALEWGLF 

       550        560        570        580 
QTGPVLIRVC THRGQDSSMR QQLREGLVMH LQSISQNGHI DL 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9303.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000554 Genomic DNA. Translation: ABM78622.1. Different initiation.
RefSeqYP_001017887.1. NC_008820.1.

3D structure databases

ProteinModelPortalA2CAW2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59922.P9303_18801.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM78622; ABM78622; P9303_18801.
GeneID4778095.
KEGGpmf:P9303_18801.
PATRIC23001255. VBIProMar17757_1936.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1165.
HOGENOMHOG000218359.
KOK02551.
OrthoDBEOG6NWBQW.
ProtClustDBCLSK825891.

Enzyme and pathway databases

BioCycPMAR59922:GH54-1982-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_PROM3
AccessionPrimary (citable) accession number: A2CAW2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 49 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