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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: 1,4-dihydroxy-2-naphthoate biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate.UniRule annotation1 Publication
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Isochorismate synthase MenF (menF)
  2. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (menD)
  3. 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (menH)
  4. o-succinylbenzoate synthase (menC)
  5. 2-succinylbenzoate--CoA ligase (menE)
  6. 1,4-dihydroxy-2-naphthoyl-CoA synthase (menB)
  7. 1,4-dihydroxy-2-naphthoyl-CoA hydrolase (menI)
This subpathway is part of the pathway 1,4-dihydroxy-2-naphthoate biosynthesis, which is itself part of Quinol/quinone metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate, the pathway 1,4-dihydroxy-2-naphthoate biosynthesis and in Quinol/quinone metabolism.

Pathwayi: menaquinone biosynthesis

This protein is involved in the pathway menaquinone biosynthesis, which is part of Quinol/quinone metabolism.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway menaquinone biosynthesis and in Quinol/quinone metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei133Proton donorUniRule annotation1 Publication1
Metal bindingi161MagnesiumUniRule annotation1 Publication1
Metal bindingi190MagnesiumUniRule annotation1 Publication1
Metal bindingi213MagnesiumUniRule annotation1 Publication1
Active sitei235Proton acceptorUniRule annotation1 Publication1

GO - Molecular functioni

  • hydro-lyase activity Source: EcoCyc
  • magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11532. menC.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001712701 – 320o-succinylbenzoate synthaseAdd BLAST320

Proteomic databases

PaxDbiP29208.
PRIDEiP29208.

Interactioni

Protein-protein interaction databases

BioGridi4260503. 22 interactors.
IntActiP29208. 5 interactors.
MINTiMINT-1305669.
STRINGi511145.b2261.

Chemistry databases

BindingDBiP29208.

Structurei

Secondary structure

1320
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 13Combined sources12
Beta strandi26 – 36Combined sources11
Beta strandi39 – 45Combined sources7
Turni49 – 51Combined sources3
Beta strandi52 – 54Combined sources3
Helixi56 – 70Combined sources15
Helixi81 – 94Combined sources14
Beta strandi109 – 111Combined sources3
Helixi114 – 122Combined sources9
Beta strandi126 – 133Combined sources8
Beta strandi135 – 137Combined sources3
Helixi139 – 152Combined sources14
Beta strandi156 – 161Combined sources6
Helixi168 – 176Combined sources9
Turni180 – 182Combined sources3
Helixi183 – 185Combined sources3
Beta strandi186 – 190Combined sources5
Beta strandi193 – 195Combined sources3
Helixi196 – 206Combined sources11
Beta strandi210 – 213Combined sources4
Helixi214 – 217Combined sources4
Beta strandi229 – 234Combined sources6
Helixi236 – 239Combined sources4
Helixi242 – 254Combined sources13
Beta strandi258 – 262Combined sources5
Helixi268 – 281Combined sources14
Helixi292 – 294Combined sources3
Beta strandi298 – 301Combined sources4
Helixi313 – 315Combined sources3
Beta strandi316 – 318Combined sources3

3D structure databases

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

eggNOGiENOG4105DNI. Bacteria.
COG1441. LUCA.
HOGENOMiHOG000271247.
InParanoidiP29208.
KOiK02549.
OMAiYEANRDG.
PhylomeDBiP29208.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00470. MenC_1. 1 hit.
InterProiIPR029065. Enolase_C-like.
IPR029017. Enolase_N-like.
IPR013342. Mandelate_racemase_C.
IPR001354. MR/MLE/MAL.
IPR010196. OSB_synthase_MenC1.
IPR010197. OSB_synthase_MenC_2.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PTHR13794:SF8. PTHR13794:SF8. 1 hit.
PfamiPF13378. MR_MLE_C. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 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)DescriptionActionsGraphical viewLength
Sequence conflicti176 – 177Missing in AAA71917 (PubMed:8335646).Curated2

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.
WP_001255628.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75321; AAC75321; b2261.
BAA16085; BAA16085; BAA16085.
GeneIDi946734.
KEGGiecj:JW2256.
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.
WP_001255628.1. NZ_LN832404.1.

3D structure databases

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

Protein-protein interaction databases

BioGridi4260503. 22 interactors.
IntActiP29208. 5 interactors.
MINTiMINT-1305669.
STRINGi511145.b2261.

Chemistry databases

BindingDBiP29208.

Proteomic databases

PaxDbiP29208.
PRIDEiP29208.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75321; AAC75321; b2261.
BAA16085; BAA16085; BAA16085.
GeneIDi946734.
KEGGiecj:JW2256.
eco:b2261.
PATRICi32119889. VBIEscCol129921_2354.

Organism-specific databases

EchoBASEiEB1494.
EcoGeneiEG11532. menC.

Phylogenomic databases

eggNOGiENOG4105DNI. Bacteria.
COG1441. LUCA.
HOGENOMiHOG000271247.
InParanoidiP29208.
KOiK02549.
OMAiYEANRDG.
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.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00470. MenC_1. 1 hit.
InterProiIPR029065. Enolase_C-like.
IPR029017. Enolase_N-like.
IPR013342. Mandelate_racemase_C.
IPR001354. MR/MLE/MAL.
IPR010196. OSB_synthase_MenC1.
IPR010197. OSB_synthase_MenC_2.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PTHR13794:SF8. PTHR13794:SF8. 1 hit.
PfamiPF13378. MR_MLE_C. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 149 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

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 one 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.