Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

  ⌊ muconate cycloisomerase (syn) like

  ⌊ FunctionalDomain muconate cycloisomerase (ID 420)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Rhodococcus opacus Taxon ID: 37919 5915882 URP
Rhodococcus opacus Taxon ID: 37919 1771524 URP

Uniprot

Protein NameAccessionEC Number Identifier
Muconate cycloisomerase 1 P95608 CATB_RHOOP (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 373 | Length of Functional Domain: 373

1       10        20        30        40        50        60

MTDLSIVSVETTILDVPLVRPHKFATTSMTAQPLLLVAVTTAGGVTGYGEGVVPGGPWWG
GESVETMQAIVERYIVPVLLGRGVDEITGIMPDIERVVANARFAKAAVDVALHDAWARSL
GVPVHTLLGGAFRKSVDVTWALGAAPAEEIIEEALDLVESKRHFSFKLKMGALDPAVDTA
RVVQIAQALQGKAGVRIDVNARWDRLTALKYVPRLVEGGVELIEQPTPGEQLEVLAELNR
LVPVPVMADESVQTPHDALEVARRGAADVIALKTTKCGGLQKSREVVAIAKAAGIACHGA
TSIEGPIGTAASIHFACAEPGIDFGTELFGPLLFSEELLQEPIRYADGQVFLPEGPGLGV
ELNMDAVKTWTRN
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
198 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
224 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
249 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
Subgroup CAR This EFD conserves 7/7 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
167 Lys (K) side chain Electrostatic stabilization of transition state electrostatic stabiliser -- spectator ISS PubMed:10336378
169 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:10336378
198 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:9724714
224 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:9724714
249 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:9724714
273 Lys (K) side chain Stabilizes enolate anion intermediate electrostatic stabiliser -- spectator ICS PubMed:19220063
327 Glu (E) side chain general acid proton relay -- reactant ICS PubMed:7500361

Catalyzed Reaction

muconate cycloisomerase

+
cis,cis-muconate
32379		 hydron
15378		 5-oxo-2,5-dihydro-2-furylacetate
58372

EC: 5.5.1.1 | IntEnz: 5.5.1.1 | Kegg: 5.5.1.1 | BioCyc: 5.5.1.1 | BRENDA: 5.5.1.1

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 2:33 a.m. update curation agent sbrown setDomainBoundaries.py
Aug. 10, 2015, 3:02 a.m. update curation agent setDomainBoundaries.py sbrown
update curation agent sbrown setDomainBoundaries.py
Oct. 15, 2015, 3:26 a.m. update curation agent setDomainBoundaries.py sbrown
remove family assignment evidence code IES -
remove family muconate cycloisomerase (syn) -
update name muconate cycloisomerase (syn) muconate cycloisomerase
update subgroup muconate cycloisomerase muconate cycloisomerase (syn) like
Feb. 10, 2017, 3:01 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.