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O06421 (MEND_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. 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:Rv0555, MT0581
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length554 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 MF_01659

Catalytic activity

Isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2. HAMAP MF_01659

Cofactor

Magnesium or manganese By similarity. HAMAP MF_01659

Binds 1 thiamine pyrophosphate per subunit By similarity.

Pathway

Cofactor biosynthesis; menaquinone biosynthesis; menaquinone-2 from chorismate: step 2/8. HAMAP MF_01659

Subunit structure

Homodimer By similarity. HAMAP MF_01659

Miscellaneous

Was identified as a high-confidence drug target. HAMAP MF_01659

Sequence similarities

Belongs to the TPP enzyme family. MenD subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5545542-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP MF_01659
PRO_0000341784

Experimental info

Sequence conflict121V → I in AAK44804. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O06421 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 879423AAB00F36A5

FASTA55457,836
        10         20         30         40         50         60 
MNPSTTQARV VVDELIRGGV RDVVLCPGSR NAPLAFALQD ADRSGRIRLH VRIDERTAGY 

        70         80         90        100        110        120 
LAIGLAIGAG APVCVAMTSG TAVANLGPAV VEANYARVPL IVLSANRPYE LLGTGANQTM 

       130        140        150        160        170        180 
EQLGYFGTQV RASISLGLAE DAPERTSALN ATWRSATCRV LAAATGARTA NAGPVHFDIP 

       190        200        210        220        230        240 
LREPLVPDPE PLGAVTPPGR PAGKPWTYTP PVTFDQPLDI DLSVDTVVIS GHGAGVHPNL 

       250        260        270        280        290        300 
AALPTVAEPT APRSGDNPLH PLALPLLRPQ QVIMLGRPTL HRPVSVLLAD AEVPVFALTT 

       310        320        330        340        350        360 
GPRWPDVSGN SQATGTRAVT TGAPRPAWLD RCAAMNRHAI AAVREQLAAH PLTTGLHVAA 

       370        380        390        400        410        420 
AVSHALRPGD QLVLGASNPV RDVALAGLDT RGIRVRSNRG VAGIDGTVST AIGAALAYEG 

       430        440        450        460        470        480 
AHERTGSPDS PPRTIALIGD LTFVHDSSGL LIGPTEPIPR SLTIVVSNDN GGGIFELLEQ 

       490        500        510        520        530        540 
GDPRFSDVSS RIFGTPHDVD VGALCRAYHV ESRQIEVDEL GPTLDQPGAG MRVLEVKADR 

       550 
SSLRQLHAAI KAAL 

« Hide

References

[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842573 Genomic DNA. Translation: CAB08966.1.
AE000516 Genomic DNA. Translation: AAK44804.1.
PIRF70548.
RefSeqNP_215069.1. NC_000962.2.
NP_334990.1. NC_002755.2.

3D structure databases

ProteinModelPortalO06421.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000002000; EBMYCP00000002000; EBMYCG00000001998.
EBMYCT00000071602; EBMYCP00000069661; EBMYCG00000071597.
GeneID887554.
924945.
GenomeReviewsGene locus MT0581 in contig AE000516_GR.
Gene locus Rv0555 in contig AL123456_GR.
KEGGmtc:MT0581.
mtu:Rv0555.
PATRIC18122978. VBIMycTub22151_0623.
TIGRMT0581.

Organism-specific databases

TubercuListRv0555.

Phylogenomic databases

GeneTreeEBGT00050000015760.
HOGENOMHBG634405.
OMAIAEPTAP.
PhylomeDBO06421.
ProtClustDBPRK07449.

Family and domain databases

HAMAPMF_01659. MenD.
[Tree]
InterProIPR004433. MenaQ_synth_MenD.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
[Graphical view]
KOK02551.
PANTHERPTHR18968:SF3. PTHR18968:SF3. 1 hit.
PfamPF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFPIRSF004983. MenD. 1 hit.
TIGRFAMsTIGR00173. MenD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMEND_MYCTU
AccessionPrimary (citable) accession number: O06421
Secondary accession number(s): Q7D9N1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 1997
Last modified: January 25, 2012
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families