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Q3M3Y3 (MEND_ANAVT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:Ava_4706
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length583 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 ABA24303.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5835832-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659
PRO_0000341700

Sequences

Sequence LengthMass (Da)Tools
Q3M3Y3 [UniParc].

Last modified July 1, 2008. Version 2.
Checksum: 8F1C11A039C39BD9

FASTA58365,551
        10         20         30         40         50         60 
MPIAYKNINQ LWAYVFTETL KRLGLAYAVI CPGSRSTPLA VAFAQQAPDI EGISILDERS 

        70         80         90        100        110        120 
AAFFALGLAK ATNRPVAIVC TSGTAGANFY PAVIEAQESR VPLLLLTADR PPELRDCHSG 

       130        140        150        160        170        180 
QTIDQVKLFG SYPNWQTELA LPVSDMGMLG YLRQTVIHSW YRMQAPTPGP VHLNIPFRDP 

       190        200        210        220        230        240 
LAPIPDGADL SYLLTKFHPE EFFAGITDTT SLPDHSQLSI PPEWLKSQRG IIIAGVAQPQ 

       250        260        270        280        290        300 
QPQEYCRAIA RLSQTLQWPV LAEGLSPIRN YADLNPYLIS TYDLILRNQQ LATRLAPDMV 

       310        320        330        340        350        360 
IQIGDMPTSK ELRTWIDTHQ PRRWVIDPSD QNLDPLHGRT THLRIRVEEL GCKGVEEDKS 

       370        380        390        400        410        420 
SVSEYLQLWC NAETKVRVNV DETLDKMEDL VECKAAWLLS QILPPETPLF IANSMPVRDV 

       430        440        450        460        470        480 
EFFWKPNNLR VRSHFNRGAN GIDGTLSTAL GIAHRHQSSV LITGDLALLH DTNGFLIRNK 

       490        500        510        520        530        540 
FVGHLTIILI NNNGGGIFEM LPIAKFEPPF EEFFGTPQDI DFAQLCTTYN VQHELIHSWV 

       550        560        570        580 
HLQQRLNPLP NTGIRVLELR TNRKIDAQWR RDNLSNFAAD NII 

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000117 Genomic DNA. Translation: ABA24303.1. Different initiation.
RefSeqYP_325198.1. NC_007413.1.

3D structure databases

ProteinModelPortalQ3M3Y3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING240292.Ava_4706.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA24303; ABA24303; Ava_4706.
GeneID3679725.
KEGGava:Ava_4706.
PATRIC35430897. VBIAnaVar43351_5969.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1165.
HOGENOMHOG000218359.
KOK02551.
OrthoDBEOG6NWBQW.
ProtClustDBPRK07449.

Enzyme and pathway databases

BioCycAVAR240292:GCY3-4767-MONOMER.
UniPathwayUPA00079; UER00164.

Family and domain databases

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

Entry information

Entry nameMEND_ANAVT
AccessionPrimary (citable) accession number: Q3M3Y3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 57 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