Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

o-succinylbenzoate synthase

Gene

Aaar

Organism
Amycolatopsis sp.
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 annotation

Catalytic activityi

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

Cofactori

a divalent metal cationUniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei161 – 1611Proton donorUniRule annotation
Metal bindingi189 – 1891MagnesiumCombined sources
Metal bindingi191 – 1911MagnesiumCombined sources
Metal bindingi214 – 2141MagnesiumCombined sources
Metal bindingi239 – 2391MagnesiumCombined sources
Active sitei263 – 2631Proton acceptorUniRule annotation

GO - Molecular functioni

  1. catalytic activity Source: InterPro
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotation

Keywords - Biological processi

Menaquinone biosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

SABIO-RKQ44244.
UniPathwayiUPA00079.
UPA01057; UER00165.

Names & Taxonomyi

Protein namesi
Recommended name:
o-succinylbenzoate synthaseUniRule 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:AaarImported
Synonyms:menCUniRule annotation
OrganismiAmycolatopsis sp.Imported
Taxonomic identifieri37632 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeAmycolatopsis

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SJAX-ray2.30A/B/C/D1-368[»]
1SJBX-ray2.20A/B/C/D1-368[»]
1SJCX-ray2.10A/B/C/D1-368[»]
1SJDX-ray1.87A/B/C/D1-368[»]
4A6GX-ray2.71A/B/C/D1-368[»]
ProteinModelPortaliQ44244.
SMRiQ44244. Positions 1-368.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ44244.

Family & Domainsi

Sequence similaritiesi

Belongs to the mandelate racemase/muconate lactonizing enzyme family. MenC type 2 subfamily.UniRule annotation

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_01933. MenC_2.
InterProiIPR029065. Enolase_C-like.
IPR029017. Enolase_N_like.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N_dom.
IPR001354. MR/MLE/MAL.
IPR010197. OSB_synthase_MenC_2.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PTHR13794:SF8. PTHR13794:SF8. 1 hit.
PfamiPF01188. MR_MLE. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01928. menC_lowGC/arch. 1 hit.

Sequencei

Sequence statusi: Complete.

Q44244-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSGVELRR VQMPLVAPFR TSFGTQSVRE LLLLRAVTPA GEGWGECVTM
60 70 80 90 100
AGPLYSSEYN DGAEHVLRHY LIPALLAAED ITAAKVTPLL AKFKGHRMAK
110 120 130 140 150
GALEMAVLDA ELRAHERSFA AELGSVRDSV PCGVSVGIMD TIPQLLDVVG
160 170 180 190 200
GYLDEGYVRI KLKIEPGWDV EPVRAVRERF GDDVLLQVDA NTAYTLGDAP
210 220 230 240 250
QLARLDPFGL LLIEQPLEEE DVLGHAELAR RIQTPICLDE SIVSARAAAD
260 270 280 290 300
AIKLGAVQIV NIKPGRVGGY LEARRVHDVC AAHGIPVWCG GMIETGLGRA
310 320 330 340 350
ANVALASLPN FTLPGDTSAS DRFYKTDITE PFVLSGGHLP VPTGPGLGVA
360
PIPELLDEVT TAKVWIGS
Length:368
Mass (Da):39,406
Last modified:November 1, 1996 - v1
Checksum:i623A27548DA0E8C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30738 Genomic DNA. Translation: BAA06400.1.
PIRiI39598.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30738 Genomic DNA. Translation: BAA06400.1.
PIRiI39598.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SJAX-ray2.30A/B/C/D1-368[»]
1SJBX-ray2.20A/B/C/D1-368[»]
1SJCX-ray2.10A/B/C/D1-368[»]
1SJDX-ray1.87A/B/C/D1-368[»]
4A6GX-ray2.71A/B/C/D1-368[»]
ProteinModelPortaliQ44244.
SMRiQ44244. Positions 1-368.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00079.
UPA01057; UER00165.
SABIO-RKQ44244.

Miscellaneous databases

EvolutionaryTraceiQ44244.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_01933. MenC_2.
InterProiIPR029065. Enolase_C-like.
IPR029017. Enolase_N_like.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N_dom.
IPR001354. MR/MLE/MAL.
IPR010197. OSB_synthase_MenC_2.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PTHR13794:SF8. PTHR13794:SF8. 1 hit.
PfamiPF01188. MR_MLE. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01928. menC_lowGC/arch. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning, DNA sequencing and heterologous expression of the gene for thermostable N-acylamino acid racemase from Amycolatopsis sp. TS-1-60 in Escherichia coli."
    Tokuyama S., Hatano K.
    Appl. Microbiol. Biotechnol. 42:884-889(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: TS-1-60Imported.
  2. "Evolution of enzymatic activity in the enolase superfamily: structural studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis."
    Thoden J.B., Taylor Ringia E.A., Garrett J.B., Gerlt J.A., Holden H.M., Rayment I.
    Biochemistry 43:5716-5727(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
  3. "An improved racemase/acylase biotransformation for the preparation of enantiomerically pure amino acids."
    Baxter S., Royer S., Grogan G., Brown F., Holt-Tiffin K.E., Taylor I.N., Fotheringham I.G., Campopiano D.J.
    J. Am. Chem. Soc. 134:19310-19313(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.

Entry informationi

Entry nameiQ44244_9PSEU
AccessioniPrimary (citable) accession number: Q44244
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: April 29, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.