Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

  ⌊ FunctionalDomain uncharacterized muconate cycloisomerase subgroup sequence (ID 1858971)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli Taxon ID: 562 585320539 WP_024202205.1 (RefSeq) URP

Sequence

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

1       10        20        30        40        50        60

MRSAQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLREGEREGWGEISPLPGFSQETWEEAQ
SVLLAWVNNWLAGDCELPQMPSVAFGVSCALAELTDTLPQAANYRAAPLCNGDPDDLILK
LADMPGEKVAKVKVGLYEAVRDGMVVNLLLEAIPDLHLRLDANRAWTPLKGQQFAKYVNP
DYRDRIAFLEEPCKTRDDSRAFARETGIAIAWDESLREPDFAFVAEEGVRAVVINPTLTG
SLEKVREQVQAAHALGLTAVISSSIESSLGLTQLARIAAWLTPDTIPGLDTLDLMQAQQV
RRWPGSTLPVVEVDALERLL
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

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1FHU Crystal Structure Analysis Of O-Succinylbenzoate Synthase From E. Coli O-Succinylbenzoate Synthase 265 1.65 CSA • PDB • PDBSum
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
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
2OFJ Crystal Structure Of The E190A Mutant Of O-Succinylbenzoate Synthase From Escherichia Coli O-Succinylbenzoate Synthase 263 2.3 Yes 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, 2:47 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.