Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

     ⌊ Family o-succinylbenzoate synthase

  ⌊ FunctionalDomain o-succinylbenzoate synthase (ID 278169)

Superfamily Assignment Evidence Code(s) IEA
Family Assignment Evidence Code IEA
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli Taxon ID: 562 447178368 WP_001255624.1 (RefSeq) URP
Escherichia coli UMEA 3899-1 Taxon ID: 1281275 535911329 ERA42112.1 (Genbank) URP
Escherichia coli HVH 187 (4-4471660) Taxon ID: 1281114 535221255 EQT65035.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A0E0V852 A0A0E0V852_ECOLX (TrEMBL)

Sequence

Length of Enzyme (full-length): 320 | Length of Functional Domain: 320

1       10        20        30        40        50        60

MRSAQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLREGEREGWGEISPLPGFSQETWEEAQ
SVLLAWVNNWLAGDCELPQMPSVAFGVSCALAELTDALPQAANYRAAPLCNGDPDDLILK
LADMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIPDLHLRLDANRAWTPLKGQQFAKYVNP
DYRHRIAFLEEPCKTRDDSRAFARETGIAIAWDESLREPDFAFVAEEGVRAVVIKPTLTG
SLDKVREQVKAAHALGLTAVISSSIESSLGLTQLARIAAWLTPDTIPGLDTLDLMQAQQV
RRWPGSPLPLVDVDALERLL
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
161 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
190 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
213 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
Subgroup CAR This EFD conserves 4/4 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
133 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11747448
161 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
190 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
213 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
Family CAR This EFD conserves 5/5 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
133 Lys (K) side chain base (abstracts alpha proton), acid (donates proton to leaving group) proton relay -- reactant ICS PubMed:14661953
161 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:10978150
190 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:10978150
213 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:10978150
235 Lys (K) side chain stabilizes intermediate through cation-pi interaction electrostatic stabiliser -- spectator ICS PubMed:14661953

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1FHV Crystal Structure Analysis Of O-Succinylbenzoate Synthase From E. Coli Complexed With Mg And Osb O-Succinylbenzoate Synthase 265 1.77 Magnesium Ion • 2-Succinylbenzoate CSA • PDB • PDBSum
1FHU Crystal Structure Analysis Of O-Succinylbenzoate Synthase From E. Coli O-Succinylbenzoate Synthase 265 1.65 CSA • PDB • PDBSum
2OFJ Crystal Structure Of The E190A Mutant Of O-Succinylbenzoate Synthase From Escherichia Coli O-Succinylbenzoate Synthase 263 2.3 Yes CSA • PDB • PDBSum
1R6W Crystal Structure Of The K133R Mutant Of O-Succinylbenzoate Synthase (Osbs) From Escherichia Coli. Complex With Shchc O-Succinylbenzoate Synthase 263 1.62 Yes Magnesium Ion • 2-(3-Carboxypropionyl)-6-Hydroxy-Cyclohexa-2,4-Diene Carboxylic Acid CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
Aug. 1, 2014, 3:12 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.