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Protein

o-succinylbenzoate synthase

Gene

menC

Organism
Thermobifida fusca (strain YX)
Status
Unreviewed-Annotation score: Annotation score: 3 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 annotationSAAS annotation

Catalytic activityi

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

Cofactori

a divalent metal cationUniRule annotation

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 annotationSAAS annotation
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (menD)
  3. no protein annotated in this organism
  4. o-succinylbenzoate synthase (menC), o-succinylbenzoate synthase (menC)
  5. no protein annotated in this organism
  6. 1,4-dihydroxy-2-naphthoyl-CoA synthase (menB)
  7. no protein annotated in this organism
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 annotationSAAS annotation
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei97 – 971Proton donorUniRule annotation
Metal bindingi128 – 1281MagnesiumUniRule annotationCombined sources
Metal bindingi154 – 1541MagnesiumUniRule annotationCombined sources
Metal bindingi177 – 1771MagnesiumUniRule annotationCombined sources
Active sitei201 – 2011Proton acceptorUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotation

Keywords - Biological processi

Menaquinone biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

MagnesiumUniRule annotationCombined sourcesSAAS annotation, Metal-bindingUniRule annotationCombined sourcesSAAS annotation

Enzyme and pathway databases

BioCyciTFUS269800:GI42-1419-MONOMER.
UniPathwayiUPA00079.
UPA01057; UER00165.

Names & Taxonomyi

Protein namesi
Recommended name:
o-succinylbenzoate synthaseUniRule annotationSAAS annotation (EC:4.2.1.113UniRule annotation)
Short name:
OSB synthaseUniRule annotation
Short name:
OSBSUniRule annotation
Alternative name(s):
4-(2'-carboxyphenyl)-4-oxybutyric acid synthaseUniRule annotation
o-succinylbenzoic acid synthaseUniRule annotation
Gene namesi
Name:menCUniRule annotation
Ordered Locus Names:Tfu_1410Imported
OrganismiThermobifida fusca (strain YX)Imported
Taxonomic identifieri269800 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptosporangialesNocardiopsaceaeThermobifida
Proteomesi
  • UP000000434 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi269800.Tfu_1410.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OPJX-ray1.60A2-317[»]
2QVHX-ray1.76A/B2-317[»]
ProteinModelPortaliQ47Q21.
SMRiQ47Q21. Positions 1-310.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ47Q21.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 17399MR_MLEInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IDS. Bacteria.
COG4948. LUCA.
HOGENOMiHOG000249513.
KOiK02549.
OMAiAGWGEFS.
OrthoDBiEOG6M6JSW.

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.
IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
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.
PROSITEiPS00909. MR_MLE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q47Q21-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGRAFAIPL RTRFRGITVR EGMLVRGAAG WGEFSPFAEY GPRECARWWA
60 70 80 90 100
ACYEAAELGW PAPVRDTVPV NATVPAVGPE EAARIVASSG CTTAKVKVAE
110 120 130 140 150
RGQSEANDVA RVEAVRDALG PRGRVRIDVN GAWDVDTAVR MIRLLDRFEL
160 170 180 190 200
EYVEQPCATV DELAEVRRRV SVPIAADESI RRAEDPLRVR DAEAADVVVL
210 220 230 240 250
KVQPLGGVRA ALRLAEECGL PVVVSSAVET SVGLAAGVAL AAALPELPYA
260 270 280 290 300
CGLATLRLLH ADVCDDPLLP VHGVLPVRRV DVSEQRLAEV EIDPAAWQAR
310
LAAARAAWEQ VEREPGP
Length:317
Mass (Da):34,100
Last modified:September 13, 2005 - v1
Checksum:i6EE0C6BF295A81B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000088 Genomic DNA. Translation: AAZ55448.1.
RefSeqiWP_011291844.1. NC_007333.1.

Genome annotation databases

EnsemblBacteriaiAAZ55448; AAZ55448; Tfu_1410.
KEGGitfu:Tfu_1410.
PATRICi23903370. VBITheFus33945_1510.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000088 Genomic DNA. Translation: AAZ55448.1.
RefSeqiWP_011291844.1. NC_007333.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OPJX-ray1.60A2-317[»]
2QVHX-ray1.76A/B2-317[»]
ProteinModelPortaliQ47Q21.
SMRiQ47Q21. Positions 1-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269800.Tfu_1410.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ55448; AAZ55448; Tfu_1410.
KEGGitfu:Tfu_1410.
PATRICi23903370. VBITheFus33945_1510.

Phylogenomic databases

eggNOGiENOG4108IDS. Bacteria.
COG4948. LUCA.
HOGENOMiHOG000249513.
KOiK02549.
OMAiAGWGEFS.
OrthoDBiEOG6M6JSW.

Enzyme and pathway databases

UniPathwayiUPA00079.
UPA01057; UER00165.
BioCyciTFUS269800:GI42-1419-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ47Q21.

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.
IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
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.
PROSITEiPS00909. MR_MLE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: YXImported.
  2. "Crystal structure of O-succinylbenzoate synthase."
    Sugadev R., Burley S.K., Swaminathan S.
    Submitted (JAN-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-317.
  3. "Crystal structure of O-succinylbenzoate synthase complexed with O-succinyl benzoate."
    Sugadev R., Burley S.K., Swaminathan S.
    Submitted (AUG-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 2-317 IN COMPLEX WITH MAGNESIUM.

Entry informationi

Entry nameiQ47Q21_THEFY
AccessioniPrimary (citable) accession number: Q47Q21
Entry historyi
Integrated into UniProtKB/TrEMBL: September 13, 2005
Last sequence update: September 13, 2005
Last modified: June 8, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.