Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

  ⌊ FunctionalDomain Uncharacterized Muconate cycloisomerase subgroup sequence (ID 39067)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bacillus cereus AH1272 Taxon ID: 526993 228739390 EEL89822.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a C2Z2G0 C2Z2G0_BACCE (TrEMBL)

Sequence

Length of Enzyme (full-length): 225 | Length of Functional Domain: 225

1       10        20        30        40        50        60

MAEEAVSMIQKGYQSFKMKVGTNVKEDVKRIEAVRERVGSDIAIRVDVNQGWKNSANTLT
ALRSLGHLNIDWIEQPVIADDIDAMAHIRSKTDLPLMIDEGLKGSREMRQIIKLDAADKV
NIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSVASSAGFHVAFSKKIITSVELTGP
LKFTKDIGNLHYDVPFIRLNEKPGLGIEINEDTLQELIVFQDVVR
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
47 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
74 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
99 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
19 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11747448
47 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
74 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
99 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
2P8B Crystal Structure Of N-Succinyl Arg/Lys Racemase From Bacillus Cereus Atcc 14579 Complexed With N-Succinyl Lys. Mandelate Racemase/Muconate Lactonizing Enzymefamily Protein 115 1.7 Magnesium Ion • N-Succinyl Lysine CSA • PDB • PDBSum
2P8C Crystal Structure Of N-Succinyl Arg/Lys Racemase From Bacillus Cereus Atcc 14579 Complexed With N-Succinyl Arg. Mandelate Racemase/Muconate Lactonizing Enzymefamily Protein 115 2.0 Magnesium Ion • N~2~-(3-Carboxypropanoyl)-L-Arginine CSA • PDB • PDBSum
2P88 Crystal Structure Of N-Succinyl Arg/Lys Racemase From Bacillus Cereus Atcc 14579 Mandelate Racemase/Muconate Lactonizing Enzymefamily Protein 115 2.4 Magnesium Ion 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
Nov. 3, 2014, 2:42 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.