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P29208 (MENC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
o-succinylbenzoate synthase

Short name=OSB synthase
Short name=OSBS
EC=4.2.1.113
Alternative name(s):
4-(2'-carboxyphenyl)-4-oxybutyric acid synthase
o-succinylbenzoic acid synthase
Gene names
Name:menC
Ordered Locus Names:b2261, JW2256
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts SHCHC to OSB. HAMAP-Rule MF_00470

Catalytic activity

(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O. HAMAP-Rule MF_00470

Cofactor

Magnesium.

Pathway

Cofactor biosynthesis; menaquinone biosynthesis; menaquinone-2 from chorismate: step 4/8. HAMAP-Rule MF_00470

Sequence similarities

Belongs to the mandelate racemase/muconate lactonizing enzyme family. MenC type 1 subfamily.

Ontologies

Keywords
   Biological processMenaquinone biosynthesis
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmenaquinone biosynthetic process

Inferred from mutant phenotype PubMed 393800. Source: EcoCyc

   Molecular_functionhydro-lyase activity

Inferred from direct assay Ref.5. Source: EcoCyc

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320o-succinylbenzoate synthase HAMAP-Rule MF_00470
PRO_0000171270

Sites

Active site1331Proton donor
Active site2351Proton acceptor
Metal binding1611Magnesium
Metal binding1901Magnesium
Metal binding2131Magnesium

Experimental info

Sequence conflict176 – 1772Missing in AAA71917. Ref.1

Secondary structure

....................................................... 320
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29208 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: E20245EC13D06839

FASTA32035,477
        10         20         30         40         50         60 
MRSAQVYRWQ IPMDAGVVLR DRRLKTRDGL YVCLREGERE GWGEISPLPG FSQETWEEAQ 

        70         80         90        100        110        120 
SVLLAWVNNW LAGDCELPQM PSVAFGVSCA LAELTDTLPQ AANYRAAPLC NGDPDDLILK 

       130        140        150        160        170        180 
LADMPGEKVA KVKVGLYEAV RDGMVVNLLL EAIPDLHLRL DANRAWTPLK GQQFAKYVNP 

       190        200        210        220        230        240 
DYRDRIAFLE EPCKTRDDSR AFARETGIAI AWDESLREPD FAFVAEEGVR AVVIKPTLTG 

       250        260        270        280        290        300 
SLEKVREQVQ AAHALGLTAV ISSSIESSLG LTQLARIAAW LTPDTIPGLD TLDLMQAQQV 

       310        320 
RRWPGSTLPV VEVDALERLL 

« Hide

References

« Hide 'large scale' references
[1]"Menaquinone (vitamin K2) biosynthesis: cloning, nucleotide sequence, and expression of the menC gene from Escherichia coli."
Sharma V., Meganathan R., Hudspeth M.E.S.
J. Bacteriol. 175:4917-4921(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Unexpected divergence of enzyme function and sequence: 'N-acylamino acid racemase' is o-succinylbenzoate synthase."
Palmer D.R., Garrett J.B., Sharma V., Meganathan R., Babbitt P.C., Gerlt J.A.
Biochemistry 38:4252-4258(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Evolution of enzymatic activity in the enolase superfamily: structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg(2+) and o-Succinylbenzoate."
Thompson T.B., Garrett J.B., Taylor E.A., Meganathan R., Gerlt J.A., Rayment I.
Biochemistry 39:10662-10676(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07256 Unassigned DNA. Translation: AAA71917.1.
U00096 Genomic DNA. Translation: AAC75321.1.
AP009048 Genomic DNA. Translation: BAA16085.2.
PIRC64997.
RefSeqNP_416764.1. NC_000913.3.
YP_490501.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FHUX-ray1.65A1-320[»]
1FHVX-ray1.77A1-320[»]
1R6WX-ray1.62A1-320[»]
2OFJX-ray2.30A/B/C/D1-320[»]
ProteinModelPortalP29208.
SMRP29208. Positions 1-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP29208. 5 interactions.
MINTMINT-1305669.
STRING511145.b2261.

Proteomic databases

PaxDbP29208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75321; AAC75321; b2261.
BAA16085; BAA16085; BAA16085.
GeneID12931509.
946734.
KEGGecj:Y75_p2225.
eco:b2261.
PATRIC32119889. VBIEscCol129921_2354.

Organism-specific databases

EchoBASEEB1494.
EcoGeneEG11532. menC.

Phylogenomic databases

eggNOGCOG1441.
HOGENOMHOG000271247.
KOK02549.
OMAYEANRDG.
OrthoDBEOG6VXFBR.
PhylomeDBP29208.
ProtClustDBPRK05105.

Enzyme and pathway databases

BioCycEcoCyc:O-SUCCINYLBENZOATE-COA-SYN-MONOMER.
ECOL316407:JW2256-MONOMER.
MetaCyc:O-SUCCINYLBENZOATE-COA-SYN-MONOMER.
BRENDA4.2.1.113. 2026.
SABIO-RKP29208.
UniPathwayUPA00079; UER00165.

Gene expression databases

GenevestigatorP29208.

Family and domain databases

HAMAPMF_00470. MenC_1.
InterProIPR013342. Mandelate_racemase_C.
IPR010196. OSB_synthase.
[Graphical view]
PfamPF01188. MR_MLE. 1 hit.
[Graphical view]
SMARTSM00922. MR_MLE. 1 hit.
[Graphical view]
TIGRFAMsTIGR01927. menC_gamma/gm+. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP29208.
PROP29208.

Entry information

Entry nameMENC_ECOLI
AccessionPrimary (citable) accession number: P29208
Secondary accession number(s): P76476, P76931
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 131 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene