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C6E9T5 (C6E9T5_ECOBD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 28. 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 EMBL ACT44014.1
Ordered Locus Names:B21_02150, ECBD_1394, ECD_02191
OrganismEscherichia coli (strain B / BL21-DE3) [Complete proteome] [HAMAP]
Taxonomic identifier469008 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length556 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 SAAS SAAS012001

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 SAAS SAAS012001

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
C6E9T5 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 278201D02243E76D

FASTA55661,367
        10         20         30         40         50         60 
MSVSAFNRRW AAVILEALTR HGVRHICIAP GSRSTPLTLA AAENSAFIHH THFDERGLGH 

        70         80         90        100        110        120 
LALGLAKVSK QPVAVIVTSG TAVANLYPAL IEAGLTGEKL ILLTADRPPE LIDCGANQAI 

       130        140        150        160        170        180 
RQPGMFASHP THSISLPRPT QDIPARWLVS TIDHALGTLH AGGVHINCPF AEPLYGEMDD 

       190        200        210        220        230        240 
TGLSWQQRLG DWWQDDKPWL REAPRLESEK QRDWFFWRQK RGVVVAGRMS AEEGKKVALW 

       250        260        270        280        290        300 
AQTLGWPLIG DVLSQTGQPL PCADLWLGNA KATSELQQAQ IVVQLGSSLT GKRLLQWQAS 

       310        320        330        340        350        360 
CEPEEYWIVD DIEGRLDPAH HRGRRLIANI ADWLELHPAE KRQPWCVEIP RLAEQAMQAV 

       370        380        390        400        410        420 
IARRDAFGEA QLAHRICDYL PEQGQLFVGN SLVVRLIDAL SQLPAGYPVY SNRGASGIDG 

       430        440        450        460        470        480 
LLSTAAGVQR ASGKPTLAIV GDLSALYDLN ALALLRQVSA PLVLIVVNNN GGQIFSLLPT 

       490        500        510        520        530        540 
PQSERERFYL MPQNVHFEHA AAMFELKYHR PQNWQELETA FADAWRTPTT TVIEMVVNDT 

       550 
DGAQTLQQLL AQVSHL

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References

[1]"Genome sequences of Escherichia coli B strains REL606 and BL21(DE3)."
Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.
J. Mol. Biol. 394:644-652(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [Korea].
[2]"Sequencing and gene expression analysis of Escherichia coli BL21."
Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [Austria].
[3]"Complete sequence of Escherichia coli BL21(DE3)."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [JGI].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001665 Genomic DNA. Translation: ACT28457.1.
CP001509 Genomic DNA. Translation: ACT44014.1.
AM946981 Genomic DNA. Translation: CAQ32667.1.
RefSeqYP_002999930.1. NC_012892.2.
YP_003035642.1. NC_012947.1.
YP_003054785.1. NC_012971.2.

3D structure databases

SMRC6E9T5. Positions 1-556.
ModBaseSearch...

Protein-protein interaction databases

STRING469008.ECBD_1394.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT28457; ACT28457; ECBD_1394.
ACT44014; ACT44014; ECD_02191.
CAQ32667; CAQ32667; B21_02150.
GeneID8114728.
8156298.
8183069.
KEGGebd:ECBD_1394.
ebe:B21_02150.
ebl:ECD_02191.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1165.
HOGENOMHOG000218360.
KOK02551.
OMADGGGIFH.
ProtClustDBPRK07449.

Enzyme and pathway databases

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]
PANTHERPTHR18968:SF3. PTHR18968:SF3. 1 hit.
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 nameC6E9T5_ECOBD
AccessionPrimary (citable) accession number: C6E9T5
Secondary accession number(s): C5W703
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: May 1, 2013
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info