Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

  ⌊ muconate cycloisomerase (syn) like

  ⌊ FunctionalDomain Uncharacterized (chloro)muconate cycloisomerase (syn) like subgroup sequence (ID 5885)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Rhodoferax sp. P230 Taxon ID: 103036 5881185 AAD55081.1 (Genbank)

Uniprot

Protein NameAccessionEC Number Identifier
n/a Q9RAD0 Q9RAD0_9BURK (TrEMBL)

Sequence

Length of Enzyme (full-length): 262 | Length of Functional Domain: 262

1       10        20        30        40        50        60

MKIEAISTTIVDVPTRRPLQMSFTTVHKQSYVIVQVTAGGLVGIGEGGSVGGPTWGSESA
ETIKVIIDNYLAPLLIGKDASNLSEARALMDRAVTGNLSAKAAIDIALHDLKARALNLSI
ADLIGGTMRKSIPIAWTLASGDTARDIDSALEMIEARRHNRFKVKLGARTPAQDLEHIRS
IVKAVGDKASVRVDVNQGWDEQTASIWIPRLEEAGVELVEQPVPRANFGALRRLTEQNGV
AILADESLSSLSSAFELARDRA
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
194 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
220 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
245 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
Subgroup CAR This EFD conserves 5/7 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
163 Lys (K) side chain Electrostatic stabilization of transition state electrostatic stabiliser -- spectator ISS PubMed:10336378
165 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:10336378
194 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:9724714
220 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:9724714
245 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:9724714

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1NU5 Crystal Structure Of Pseudomonas Sp. P51 Chloromuconate Lactonizing Enzyme Chloromuconate Cycloisomerase 8 1.95 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 updateSFLD2.py setDomainBoundaries.py
Oct. 15, 2015, 3:27 a.m. update curation agent setDomainBoundaries.py sbrown
remove family assignment evidence code IEA -
remove family chloromuconate cycloisomerase -
update name chloromuconate cycloisomerase Uncharacterized (chloro)muconate cycloisomerase (syn) like subgroup sequence
update subgroup muconate cycloisomerase muconate cycloisomerase (syn) like
update superfamily assignment evidence code IEA ISS
EC number assigned by UniProtKB accession ID.