o-succinylbenzoate synthase - Escherichia coli (strain K12)

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P29208 (MENC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 125. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Menaquinone biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	menaquinone biosynthetic process Inferred from mutant phenotype PubMed 393800. Source: EcoCyc
Molecular_function	hydro-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 320

320

o-succinylbenzoate synthase HAMAP-Rule MF_00470

PRO_0000171270

Sites

Active site

133

Proton donor

Active site

235

Proton acceptor

Metal binding

161

Magnesium

Metal binding

190

Magnesium

Metal binding

213

Magnesium

Experimental info

Sequence conflict

176 – 177

Missing in AAA71917. Ref.1

Secondary structure

320

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P29208 [UniParc].

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

FASTA

320

35,477

        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' referencesShow '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. 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 277:1453-1474(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.

PIR

C64997.

RefSeq

NP_416764.1. NC_000913.2.
YP_490501.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FHU	X-ray	1.65	A	1-320	[»]
1FHV	X-ray	1.77	A	1-320	[»]
1R6W	X-ray	1.62	A	1-320	[»]
2OFJ	X-ray	2.30	A/B/C/D	1-320	[»]

ProteinModelPortal

P29208.

SMR

P29208. Positions 1-320.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10184N.

IntAct

P29208. 5 interactions.

MINT

MINT-1305669.

STRING

511145.b2261.

Proteomic databases

PaxDb

P29208.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75321; AAC75321; b2261.
BAA16085; BAA16085; BAA16085.

GeneID

12931509.
946734.

KEGG

ecj:Y75_p2225.
eco:b2261.

PATRIC

32119889. VBIEscCol129921_2354.

Organism-specific databases

EchoBASE

EB1494.

EcoGene

EG11532. menC.

Phylogenomic databases

eggNOG

COG1441.

HOGENOM

HOG000271247.

K02549.

OMA

YEANRDG.

ProtClustDB

PRK05105.

Enzyme and pathway databases

BioCyc

EcoCyc:O-SUCCINYLBENZOATE-COA-SYN-MONOMER.
ECOL316407:JW2256-MONOMER.
MetaCyc:O-SUCCINYLBENZOATE-COA-SYN-MONOMER.

BRENDA

4.2.1.113. 2026.

SABIO-RK

P29208.

UniPathway

UPA00079; UER00165.

Gene expression databases

Genevestigator

P29208.

Family and domain databases

HAMAP

MF_00470. MenC_1.

InterPro

IPR013342. Mandelate_racemase_C.
IPR010196. OSB_synthase.
[Graphical view]

Pfam

PF01188. MR_MLE. 1 hit.
[Graphical view]

SMART

SM00922. MR_MLE. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01927. menC_gamma/gm+. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P29208.

Entry information

Entry name

MENC_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 125 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents