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Protein

o-succinylbenzoate synthase

Gene

menC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB).UniRule annotation2 Publications

Catalytic activityi

(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O.UniRule annotation2 Publications

Cofactori

Mg2+1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei133 – 1331Proton donorUniRule annotation1 Publication
Metal bindingi161 – 1611MagnesiumUniRule annotation1 Publication
Metal bindingi190 – 1901MagnesiumUniRule annotation1 Publication
Metal bindingi213 – 2131MagnesiumUniRule annotation1 Publication
Active sitei235 – 2351Proton acceptorUniRule annotation1 Publication

GO - Molecular functioni

  1. hydro-lyase activity Source: EcoCyc
  2. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. menaquinone biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Menaquinone biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:O-SUCCINYLBENZOATE-COA-SYN-MONOMER.
ECOL316407:JW2256-MONOMER.
MetaCyc:O-SUCCINYLBENZOATE-COA-SYN-MONOMER.
BRENDAi4.2.1.113. 2026.
SABIO-RKP29208.
UniPathwayiUPA00079.
UPA01057; UER00165.

Names & Taxonomyi

Protein namesi
Recommended name:
o-succinylbenzoate synthase1 PublicationUniRule annotation (EC:4.2.1.113UniRule annotation2 Publications)
Short name:
OSB synthaseUniRule annotationCurated
Short name:
OSBSUniRule annotationCurated
Alternative name(s):
4-(2'-carboxyphenyl)-4-oxybutyric acid synthaseUniRule annotationCurated
o-succinylbenzoic acid synthaseUniRule annotationCurated
Gene namesi
Name:menCUniRule annotation
Ordered Locus Names:b2261, JW2256
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11532. menC.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320o-succinylbenzoate synthasePRO_0000171270Add
BLAST

Proteomic databases

PaxDbiP29208.

Expressioni

Gene expression databases

GenevestigatoriP29208.

Interactioni

Protein-protein interaction databases

IntActiP29208. 5 interactions.
MINTiMINT-1305669.
STRINGi511145.b2261.

Structurei

Secondary structure

1
320
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1312Combined sources
Beta strandi26 – 3611Combined sources
Beta strandi39 – 457Combined sources
Turni49 – 513Combined sources
Beta strandi52 – 543Combined sources
Helixi56 – 7015Combined sources
Helixi81 – 9414Combined sources
Beta strandi109 – 1113Combined sources
Helixi114 – 1229Combined sources
Beta strandi126 – 1338Combined sources
Beta strandi135 – 1373Combined sources
Helixi139 – 15214Combined sources
Beta strandi156 – 1616Combined sources
Helixi168 – 1769Combined sources
Turni180 – 1823Combined sources
Helixi183 – 1853Combined sources
Beta strandi186 – 1905Combined sources
Beta strandi193 – 1953Combined sources
Helixi196 – 20611Combined sources
Beta strandi210 – 2134Combined sources
Helixi214 – 2174Combined sources
Beta strandi229 – 2346Combined sources
Helixi236 – 2394Combined sources
Helixi242 – 25413Combined sources
Beta strandi258 – 2625Combined sources
Helixi268 – 28114Combined sources
Helixi292 – 2943Combined sources
Beta strandi298 – 3014Combined sources
Helixi313 – 3153Combined sources
Beta strandi316 – 3183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FHUX-ray1.65A1-320[»]
1FHVX-ray1.77A1-320[»]
1R6WX-ray1.62A1-320[»]
2OFJX-ray2.30A/B/C/D1-320[»]
ProteinModelPortaliP29208.
SMRiP29208. Positions 1-320.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29208.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1441.
HOGENOMiHOG000271247.
InParanoidiP29208.
KOiK02549.
OMAiEEPCKTP.
OrthoDBiEOG6VXFBR.
PhylomeDBiP29208.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00470. MenC_1.
InterProiIPR029065. Enolase_C-like.
IPR029017. Enolase_N_like.
IPR013342. Mandelate_racemase_C.
IPR001354. MR/MLE/MAL.
IPR010196. OSB_synthase.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PfamiPF01188. MR_MLE. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01927. menC_gamma/gm+. 1 hit.

Sequencei

Sequence statusi: Complete.

P29208-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSAQVYRWQ IPMDAGVVLR DRRLKTRDGL YVCLREGERE GWGEISPLPG
60 70 80 90 100
FSQETWEEAQ SVLLAWVNNW LAGDCELPQM PSVAFGVSCA LAELTDTLPQ
110 120 130 140 150
AANYRAAPLC NGDPDDLILK LADMPGEKVA KVKVGLYEAV RDGMVVNLLL
160 170 180 190 200
EAIPDLHLRL DANRAWTPLK GQQFAKYVNP DYRDRIAFLE EPCKTRDDSR
210 220 230 240 250
AFARETGIAI AWDESLREPD FAFVAEEGVR AVVIKPTLTG SLEKVREQVQ
260 270 280 290 300
AAHALGLTAV ISSSIESSLG LTQLARIAAW LTPDTIPGLD TLDLMQAQQV
310 320
RRWPGSTLPV VEVDALERLL
Length:320
Mass (Da):35,477
Last modified:November 1, 1997 - v2
Checksum:iE20245EC13D06839
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1772Missing in AAA71917 (PubMed:8335646).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07256 Unassigned DNA. Translation: AAA71917.1.
U00096 Genomic DNA. Translation: AAC75321.1.
AP009048 Genomic DNA. Translation: BAA16085.2.
PIRiC64997.
RefSeqiNP_416764.1. NC_000913.3.
YP_490501.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75321; AAC75321; b2261.
BAA16085; BAA16085; BAA16085.
GeneIDi12931509.
946734.
KEGGiecj:Y75_p2225.
eco:b2261.
PATRICi32119889. VBIEscCol129921_2354.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07256 Unassigned DNA. Translation: AAA71917.1.
U00096 Genomic DNA. Translation: AAC75321.1.
AP009048 Genomic DNA. Translation: BAA16085.2.
PIRiC64997.
RefSeqiNP_416764.1. NC_000913.3.
YP_490501.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FHUX-ray1.65A1-320[»]
1FHVX-ray1.77A1-320[»]
1R6WX-ray1.62A1-320[»]
2OFJX-ray2.30A/B/C/D1-320[»]
ProteinModelPortaliP29208.
SMRiP29208. Positions 1-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP29208. 5 interactions.
MINTiMINT-1305669.
STRINGi511145.b2261.

Proteomic databases

PaxDbiP29208.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75321; AAC75321; b2261.
BAA16085; BAA16085; BAA16085.
GeneIDi12931509.
946734.
KEGGiecj:Y75_p2225.
eco:b2261.
PATRICi32119889. VBIEscCol129921_2354.

Organism-specific databases

EchoBASEiEB1494.
EcoGeneiEG11532. menC.

Phylogenomic databases

eggNOGiCOG1441.
HOGENOMiHOG000271247.
InParanoidiP29208.
KOiK02549.
OMAiEEPCKTP.
OrthoDBiEOG6VXFBR.
PhylomeDBiP29208.

Enzyme and pathway databases

UniPathwayiUPA00079.
UPA01057; UER00165.
BioCyciEcoCyc:O-SUCCINYLBENZOATE-COA-SYN-MONOMER.
ECOL316407:JW2256-MONOMER.
MetaCyc:O-SUCCINYLBENZOATE-COA-SYN-MONOMER.
BRENDAi4.2.1.113. 2026.
SABIO-RKP29208.

Miscellaneous databases

EvolutionaryTraceiP29208.
PROiP29208.

Gene expression databases

GenevestigatoriP29208.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00470. MenC_1.
InterProiIPR029065. Enolase_C-like.
IPR029017. Enolase_N_like.
IPR013342. Mandelate_racemase_C.
IPR001354. MR/MLE/MAL.
IPR010196. OSB_synthase.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PfamiPF01188. MR_MLE. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01927. menC_gamma/gm+. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
    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.
    , 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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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(2005) [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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH 2-SUCCINYLBENZOIC ACID AND MAGNESIUM, COFACTOR.

Entry informationi

Entry nameiMENC_ECOLI
AccessioniPrimary (citable) accession number: P29208
Secondary accession number(s): P76476, P76931
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 1, 1997
Last modified: February 4, 2015
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.