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A1UAX3 (MEND_MYCSK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Short name=SEPHCHC synthase
EC=2.2.1.9
Alternative name(s):
Menaquinone biosynthesis protein MenD
Gene names
Name:menD
Ordered Locus Names:Mkms_0765
OrganismMycobacterium sp. (strain KMS) [Complete proteome] [HAMAP]
Taxonomic identifier189918 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length547 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 – 5475472-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659
PRO_0000341782

Sequences

Sequence LengthMass (Da)Tools
A1UAX3 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 95627771DCCEF164

FASTA54757,160
        10         20         30         40         50         60 
MNPSTAQARV VVDELVRGGV HDVVLCPGSR NAPLAFALAD ADRAGRLRLH VRIDERTAGF 

        70         80         90        100        110        120 
LAIGLAVADR APVCVAMTSG TAVANLGPAV VEANYARVPL IVLSANRPYE LLGTGANQTF 

       130        140        150        160        170        180 
EQLGYFGNQV RANISLGLAP ELSSGSPGDM TSLNAQWRSA TCRVVVAATG SRSANAGPVQ 

       190        200        210        220        230        240 
FDIPLREPLV PTFDDDGSCP PGRPDGKPWT HTPPVTFDQP LDIDLTPDTV VIAGHGAGVH 

       250        260        270        280        290        300 
PNLADLPTVA EPTAPPAANP LHPMALRLLR PKQVIMLGRP TLHRPVSALL ADPSVPVYAL 

       310        320        330        340        350        360 
TTGPRWPDVS GNSQATGTRA VTSGTPDPAW LRRCKEVNDH AVAAVREQLA AHPLTTGLHV 

       370        380        390        400        410        420 
AAAVADAVRP GDQLVLGASN PVRDAALVGF TPHGVQVRSN RGVAGIDGTV STAIGAALAH 

       430        440        450        460        470        480 
DRTGGRTIAL MGDLTFVHDS SGLLIGPTEP TPRNLTIVVS NDNGGGIFEL LEQGDPRFSD 

       490        500        510        520        530        540 
VSSRVFGTPH DVDVGALCRA YHVDNRQIEV GQLADALDEP HEGMRVLEVK ADRSSLRALH 


ASIKAAL 

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References

[1]"Complete sequence of chromosome of Mycobacterium sp. KMS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KMS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000518 Genomic DNA. Translation: ABL89981.1.
RefSeqYP_936771.1. NC_008705.1.

3D structure databases

ProteinModelPortalA1UAX3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189918.Mkms_0765.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL89981; ABL89981; Mkms_0765.
GeneID4614965.
KEGGmkm:Mkms_0765.
PATRIC18100488. VBIMycSp70743_1295.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1165.
HOGENOMHOG000218359.
KOK02551.
OMAWRSAVCR.
OrthoDBEOG6NWBQW.
ProtClustDBPRK07449.

Enzyme and pathway databases

BioCycMSP189918:GH4X-769-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_MYCSK
AccessionPrimary (citable) accession number: A1UAX3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 55 of the entry and version 1 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