Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

  ⌊ muconate cycloisomerase (syn) like

  ⌊ FunctionalDomain 2-chloromuconate cycloisomerase (ID 3792010)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Halomonas organivorans Taxon ID: 257772 338221275

Uniprot

Protein NameAccessionEC Number Identifier
n/a F8J4S3 F8J4S3_9GAMM (TrEMBL)

Sequence

Length of Enzyme (full-length): 222 | Length of Functional Domain: 219

1       10        20        30        40        50        60

SRSFPRLDDGRHCDFKLKIGANALEQDVRHVADIKAALGDRASVRVDVNQAWDEATAVRG
IAALQEAGIALIEQAIPAREQAGLIRLAERFRVPMLADEAVADARDGLDLVAGGFSGAFA
LKIAKAGGPRPALELAQLALTAGVGLYGGTMLEGTIGTAASLHAWATLPEMAWGTEMFGP
LLLKDDIVAEPXRYHDFGVDLPAGPGLGIALDEDKLTHYSRK
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
47 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
73 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
98 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
16 Lys (K) side chain Electrostatic stabilization of transition state electrostatic stabiliser -- spectator ISS PubMed:10336378
18 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:10336378
47 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:9724714
73 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:9724714
98 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:9724714
122 Lys (K) side chain Stabilizes enolate anion intermediate electrostatic stabiliser -- spectator ICS PubMed:19220063
176 Glu (E) side chain general acid proton relay -- reactant ICS PubMed:7500361

Catalyzed Reaction

2-chloromuconate cycloisomerase (dehalogenating)

+
2-chloro-cis,cis-muconate(2-)
19504		 4-carboxymethylenebut-2-en-4-olide
11972		 hydrogen chloride
17883

EC: 5.5.1.- | IntEnz: 5.5.1.- | Kegg: 5.5.1.- | BioCyc: 5.5.1.- | BRENDA: 5.5.1.- |

Curation History
Time Change Annotation Old Value New Value
June 8, 2015, 3:14 a.m. update curation agent sbrown setDomainBoundaries.py
Oct. 15, 2015, 3:34 a.m. update curation agent setDomainBoundaries.py sbrown
update name uncharacterized muconate cycloisomerase subgroup sequence 2-chloromuconate cycloisomerase
update subgroup muconate cycloisomerase muconate cycloisomerase (syn) like
update superfamily assignment evidence code IEA ISS
Feb. 10, 2017, 3:18 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.