Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

  ⌊ muconate cycloisomerase (syn) like

  ⌊ FunctionalDomain muconate cycloisomerase (ID 5895)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Pseudomonas putida Taxon ID: 303 6730036 URP
Pseudomonas putida Taxon ID: 303 6730035 URP

Uniprot

Protein NameAccessionEC Number Identifier
Muconate cycloisomerase 1 P08310 CATB_PSEPU (Swiss-Prot)

Sequence

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

1       10        20        30        40        50        60

ALIERIDAIIVDLPTIRPHKLAMHTMQQQTLVVLRVRCSDGVEGIGEATTVGGLAYGYES
PEGIKANIDAHLAPALIGLAADNINAAMLKLDKLAKGNTFAKSGIESALLDAQGKRLGLP
VSELLGGRVRDSLEVAWTLASGDTARDIAEARHMLEIRRHRVFKLKIGANPVEQDLKHVV
TIKRELGDSASVRVDVNQYWDESQAIRACQVLGDNGIDLIEQPISRINRGGQVRLNQRTP
APIMADESIESVEDAFSLAADGAASIFALKIAKNGGPRAVLRTAQIAEAAGIGLYGGTML
EGSIGTLASAHAFLTLRQLTWGTELFGPLLLTEEIVNEPPQYRDFQLHIPRTPGLGLTLD
EQRLARFAR
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
195 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
221 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
246 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
164 Lys (K) side chain Electrostatic stabilization of transition state electrostatic stabiliser -- spectator ISS PubMed:10336378
166 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:10336378
195 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:9724714
221 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:9724714
246 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:9724714
270 Lys (K) side chain Stabilizes enolate anion intermediate electrostatic stabiliser -- spectator ICS PubMed:19220063
324 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

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
3MUC Muconate Cycloisomerase Variant I54V Protein (Muconate Cycloisomerase) 42 2.3 Yes Manganese (Ii) Ion CSA • PDB • PDBSum
1MUC Structure Of Muconate Lactonizing Enzyme At 1.85 Angstroms Resolution Muconate Lactonizing Enzyme 42 1.85 Manganese (Ii) Ion CSA • PDB • PDBSum
2MUC Muconate Cycloisomerase Variant F329I Protein (Muconate Cycloisomerase) 40 2.3 Yes Manganese (Ii) Ion CSA • PDB • PDBSum
1BKH Muconate Lactonizing Enzyme From Pseudomonas Putida Muconate Lactonizing Enzyme 42 2.1 CSA • PDB • PDBSum
1F9C Crystal Structure Of Mle D178N Variant Protein (Muconate Cycloisomerase I) 37 2.5 Yes Manganese (Ii) 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, 2:34 a.m. update curation agent sbrown setDomainBoundaries.py
Oct. 15, 2015, 3:27 a.m. update curation agent setDomainBoundaries.py sbrown
remove family assignment evidence code IEA -
remove family muconate cycloisomerase (syn) -
update name muconate cycloisomerase (syn) muconate cycloisomerase
update subgroup muconate cycloisomerase muconate cycloisomerase (syn) like
update superfamily assignment evidence code IEA ISS
Feb. 10, 2017, 3:03 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.