Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

     ⌊ Family muconate cycloisomerase (anti)

  ⌊ FunctionalDomain muconate cycloisomerase (anti) (ID 4451)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:14769475
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Arthrobacter sp. BA-5-17 Taxon ID: 230309 42627730

Uniprot

Protein NameAccessionEC Number Identifier
n/a Q76CC6 Q76CC6_9MICC (TrEMBL)

Sequence

Length of Enzyme (full-length): 380 | Length of Functional Domain: 369

1       10        20        30        40        50        60

MKIERIEAIPYSIPYAKPLKFASGQVTEADHVLIRIHTDTGLVGTADTPPRPYTYGETQE
SIVAVITRIFAPALVGMDPLDRQKVHQVLARTIHNQTAKGGLDIALWDIIGQAAGLPVTR
LLGGFTDSMQVSHMLGFAPAQALLDEALRFRSEYGIGTFKLKVRRPLGLDIEACHVLRDG
LGEDTEIYLDANRGWTANEAMEVLRRTEGLGLSLLEEPCDAKEAMSRRRLVDKSPIPIVG
DESVPTAGDVSRELLSGGCNAVSIKTARSGFTEAQQILGLCTGLGVDVVMGNQIDTQIGT
IATVTFGAAHEATSRRAGELSNFLDMSDDLLAEPIVNQGRPDPGPPRSRRRGRDRRGKAG
PLPPGRQMTTGLPVPLKGTA
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
190 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
216 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
241 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
162 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11747448
190 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
216 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
241 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
162 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:19220063
190 Asp (D) side chain metal ligand metal ligand -- binding ICS PubMed:19220063
216 Glu (E) side chain metal ligand metal ligand -- binding ICS PubMed:19220063
241 Asp (D) side chain metal ligand metal ligand -- binding ICS PubMed:19220063
265 Lys (K) side chain stabilizes intermediate electrostatic stabiliser -- spectator ICS PubMed:19220063
293 Gln (Q) side chain hydrogen bond donors to the lactone carbonyl of (4S)-muconolactone electrostatic stabiliser -- spectator ICS PubMed:19220063

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, 2:34 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.