Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

  ⌊ FunctionalDomain uncharacterized muconate cycloisomerase subgroup sequence (ID 300270)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Thermus sp. RLM Taxon ID: 456163 495906129 WP_008630708.1 (RefSeq) URP
Thermus sp. RLM Taxon ID: 456163 380452253 EIA39852.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a H7GDR0 H7GDR0_9DEIN (TrEMBL)

Sequence

Length of Enzyme (full-length): 369 | Length of Functional Domain: 369

1       10        20        30        40        50        60

MRIEAAELRILELPLKFRFETSFGVQTKRTILLLRLFGEGLEGLGEGVMERLPLYREETV
AGARYLLEEVFLPRVLGRDLPNPEALREALAPFRGNPMAKAVLEMAFFDLWAKALGRPLW
QVLGGVRQAVEVGVSLGIQPTVEDTLKVVERHLEEGYRRIKLKIKPGWDYEVLKAVREAF
PEATLTADANSAYSLADLARLKRLDELWLDYLEQPLAYDDLLDHAKLQRELATPICLDES
LTGAEKARKAIELGAGRVFNVKPARLGGHGESLRVHALAQSAGIPLWMGGMLEAGVGRAH
NLHLATLPGFTKPGDVSSASRYWEEDLIEEALEAKDGLMPVPEGVGIGVHLKLPFVERVT
LWQRYMSAS
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
188 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
213 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
238 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
163 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11747448
188 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
213 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
238 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
2ZC8 Crystal Structure Of N-Acylamino Acid Racemase From Thermus Thermophilus Hb8 N-Acylamino Acid Racemase 6 1.95 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, 2:46 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.