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Q55725 (MEND_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:sll0603
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length595 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 – 5955952-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659
PRO_0000341878

Sequences

Sequence LengthMass (Da)Tools
Q55725 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 62CF0EA48B20D87E

FASTA59566,133
        10         20         30         40         50         60 
MVDFTNPNTL AASVLVETLF RLGLQQAVIC PGSRSSPLTV ALARHGGIDC VVSLDERSAS 

        70         80         90        100        110        120 
FFALGHGKRT GQPVALVCTS GTAAANFLPA IIEAHYSQVP LLVLTGDRPP RLRHCRAGQT 

       130        140        150        160        170        180 
IDQTKLYGHY PQWQTELALP EPNMDYCHYL RQTALHSWQK CFWPGLGVVH LNCPFDEPLV 

       190        200        210        220        230        240 
PLEHARESLQ HLAEEFSKEH FYRGLTTFTT MNRGEAISLP VNFSIFSFPS PQLDFSPLGL 

       250        260        270        280        290        300 
ILVGVMPGGE TPSLLTDILA IARGLGYPVL CDALCSLRNY DDGQTALITN YDFLIRCPRW 

       310        320        330        340        350        360 
AEQLVPEQII QIGELPTSKA LRHWLGTIDC PRYILNFHGE NLDPLQGQTI YLSASVAQVA 

       370        380        390        400        410        420 
EYIHNQGFIP DAEQKNYAHS WLEKQRQSQT IIISALADAH TPLMVAQLAH CLPPQTNLFV 

       430        440        450        460        470        480 
ANSLPVRWLE FFWPANGDHH RIFVNRGANG IDGTLSTAMG IAHRSRGETV LLTGDLSLLH 

       490        500        510        520        530        540 
DSNGFLNQSQ MRGNLTIILL NNNGGGIFQT LPIAQCEDVF ETYFATPQGV DFGQLCRTYG 

       550        560        570        580        590 
VEHKIITNLW DLKEQWPSNN SSPIRVLEII GDRHQEAQWL KSLQAQFCCA DSLIQ 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA10366.1.
PIRS76520.
RefSeqNP_442296.1. NC_000911.1.
YP_005652356.1. NC_017277.1.
YP_007452172.1. NC_020286.1.

3D structure databases

ProteinModelPortalQ55725.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1148.sll0603.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA10366; BAA10366; BAA10366.
GeneID12253576.
14617850.
952514.
KEGGsyn:sll0603.
syy:SYNGTS_2403.
syz:MYO_124280.
PATRIC23842248. VBISynSp132158_2664.

Phylogenomic databases

eggNOGCOG1165.
HOGENOMHOG000218359.
KOK02551.
OMADGGGIFH.
OrthoDBEOG6NWBQW.
PhylomeDBQ55725.
ProtClustDBPRK07449.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13897.
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_SYNY3
AccessionPrimary (citable) accession number: Q55725
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways