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InterPro: IPR010196 O-succinylbenzoic acid (OSB) synthetase, gamma proteobacteria/archaea

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UniProtKB

Matches:

311 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR010196 OSB_synthase_proteobac/arc

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR01927	menC_gamma/gm+	311
Signatures in BioMart

InterPro Relationships Help

Contains

IPR001354 Mandelate racemase/muconate lactonizing enzyme

GO Term annotation Help

Process

GO:0009234 menaquinone biosynthetic process

Function

GO:0000287 magnesium ion binding
GO:0016836 hydro-lyase activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry describes the enzyme o-succinylbenzoic acid synthetase (MenC) that is involved in one of the steps of the menaquinone biosynthesis pathway. The biosynthesis of menaquinone has been studied most in Escherichia coli [1]. 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) is dehydrated by MenC to give the aromatic compound O-succinylbenzoate (OSB) [2]. MenC, which is a member of the enolase superfamily and x-ray structure has been determined [3, 4]. Many of the common names of the proteins in this family are incorrectly described as O-succinylbenzoyl-CoA synthase. Members are restricted to bacteria.

Structural links Help

PDB - click here

SCOP: c.1.11.2 , d.54.1.1

CATH: 3.20.20.120 , 3.30.390.10

Database links Help

Enzyme: EC:4.2.1.113

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR010196

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P29208 o-succinylbenzoate synthase

Q55117 Probable o-succinylbenzoate synthase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR010196	O-succinylbenzoic acid (OSB) synthetase, gamma proteobacteria/archaea
IPR001354	Mandelate racemase/muconate lactonizing enzyme
IPR013342	Mandelate racemase/muconate lactonizing enzyme, C-terminal
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Meganathan R. Biosynthesis of menaquinone (vitamin K2) and ubiquinone (coenzyme Q): a perspective on enzymatic mechanisms. Vitam. Horm. 61 173-218 2001 [PubMed: 11153266] http://dx.doi.org/10.1016/S0083-6729(01)61006-9
2.	Sharma V, Meganathan R, Hudspeth ME. Menaquinone (vitamin K2) biosynthesis: cloning, nucleotide sequence, and expression of the menC gene from Escherichia coli. J. Bacteriol. 175 4917-21 1993 [PubMed: 8335646] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8335646&action=stream&blobtype=pdf
3.	Palmer DR, Garrett JB, Sharma V, Meganathan R, Babbitt PC, Gerlt JA. Unexpected divergence of enzyme function and sequence: "N-acylamino acid racemase" is o-succinylbenzoate synthase. Biochemistry 38 4252-8 1999 [PubMed: 10194342] http://dx.doi.org/10.1021/bi990140p
4.	Thompson TB, Garrett JB, Taylor EA, Meganathan R, Gerlt JA, Rayment I. Evolution of enzymatic activity in the enolase superfamily: structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg2+ and o-succinylbenzoate. Biochemistry 39 10662-76 2000 [PubMed: 10978150] http://dx.doi.org/10.1021/bi000855o

Additional Reading Open in usermanual
	Nagatani RA, Gonzalez A, Shoichet BK, Brinen LS, Babbitt PC. Stability for function trade-offs in the enolase superfamily "catalytic module". Biochemistry 46 2007 6688-95 [PubMed: 17503785] http://dx.doi.org/10.1021/bi700507d
	Klenchin VA, Taylor Ringia EA, Gerlt JA, Rayment I. Evolution of enzymatic activity in the enolase superfamily: structural and mutagenic studies of the mechanism of the reaction catalyzed by o-succinylbenzoate synthase from Escherichia coli. Biochemistry 42 2003 14427-33 [PubMed: 14661953] http://dx.doi.org/10.1021/bi035545v

InterPro 23.1