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C4L321 (C4L321_EXISA) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659

Short name=SEPHCHC synthase HAMAP-Rule MF_01659
EC=2.2.1.9 HAMAP-Rule MF_01659
Alternative name(s):
Menaquinone biosynthesis protein MenD HAMAP-Rule MF_01659
Gene names
Name:menD HAMAP-Rule MF_01659
Ordered Locus Names:EAT1b_2374 EMBL ACQ71295.1
OrganismExiguobacterium sp. (strain ATCC BAA-1283 / AT1b) [Complete proteome] [HAMAP] EMBL ACQ71295.1
Taxonomic identifier360911 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium

Protein attributes

Sequence length549 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 SAAS SAAS012001

Cofactor

Binds 1 thiamine pyrophosphate per subunit By similarity. HAMAP-Rule MF_01659 SAAS SAAS012001

Magnesium or manganese By similarity. HAMAP-Rule MF_01659 SAAS SAAS012001

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. HAMAP-Rule MF_01659

Sequences

Sequence LengthMass (Da)Tools
C4L321 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: 78269CD75FC2CCEB

FASTA54961,008
        10         20         30         40         50         60 
MNKVLTEWVA SMVNRLVTSG VKDVVISPGS RSTPLAVAAY LHPQIRHHII VDERSAGFFA 

        70         80         90        100        110        120 
LGLTRASETV RPVALICTSG TAATNYYSAV TEAFISQLPL VVLTTDRPHE LRNVGAPQAI 

       130        140        150        160        170        180 
NQVRLYGEQV KTSVDLPVPE EATLSFMQQT ITRFTNLSMQ APMGPVHLNV PFREPLLPDI 

       190        200        210        220        230        240 
ESLKQILKAD PVLPERQRIR PTQADKDIFS ERTSHKQLAF VVGPYTPTSW QKSIVEYASE 

       250        260        270        280        290        300 
RQIPIFADPL SGMRRFDGVL TNYDTWLASE HRTDWLPEVF VRFGAAPVSK RFNQWMAMAD 

       310        320        330        340        350        360 
QLVIDEPGSY RDPSSRATIC YGDALDFLPL IASANEPRYL ERLRFFEEIA ESAKSSLQGE 

       370        380        390        400        410        420 
VELTKRLLDT SIELLFVSNS MPIRDVDISL SAGTNIHVLA NRGANGIDGV LSTALGSSYD 

       430        440        450        460        470        480 
TSHGALLIGD LAFYHDSNAL QLLKHHPGKF SVVIANNNGG GIFSFLPQAA VDTQLFEDLF 

       490        500        510        520        530        540 
GTPLDLNIRG FADTYGLTYR LIERPDEIQE AIEDGIHLIE FPSNREENVM IHRGWTQSVC 


SRLITENES 

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References

[1]"Complete sequence of Exiguobacterium sp. AT1b."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G. expand/collapse author list , Ramaley R.F., Rodrigues D.F., Vishnivetskaya T.A., Kathariou S., Tiedje J.M., Richardson P.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1283 / AT1b.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001615 Genomic DNA. Translation: ACQ71295.1.
RefSeqYP_002886740.1. NC_012673.1.

3D structure databases

ProteinModelPortalC4L321.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360911.EAT1b_2374.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ71295; ACQ71295; EAT1b_2374.
GeneID7870423.
KEGGeat:EAT1b_2374.
PATRIC21879986. VBIExiSp39724_2357.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1165.
HOGENOMHOG000218359.
KOK02551.
OMADGGGIFH.
OrthoDBEOG6NWBQW.
ProtClustDBCLSK2489050.

Enzyme and pathway databases

BioCycESP360911:GI4R-2453-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 nameC4L321_EXISA
AccessionPrimary (citable) accession number: C4L321
Entry history
Integrated into UniProtKB/TrEMBL: July 7, 2009
Last sequence update: July 7, 2009
Last modified: February 19, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)