Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

  ⌊ muconate cycloisomerase (syn) like

  ⌊ FunctionalDomain 2-chloromuconate cycloisomerase (ID 411)

Superfamily Assignment Evidence Code(s) ISS PubMed:8987982
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Plasmid pJP4 Taxon ID: 2580 150763 AAA98260.1 (Genbank)
Pseudomonas putida Taxon ID: 303 116506 URP

Uniprot

Protein NameAccessionEC Number Identifier
Chloromuconate cycloisomerase P11452 5.5.1.7 CLCB_PSEPU (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 370 | Length of Functional Domain: 370

1       10        20        30        40        50        60

MKIEAIDVTLVDVPASRPIQMSFTTVQKQSYAIVQIRAGGLVGIGEGSSVGGPTWSSECA
ETIKVIIETYLAPLLIGKDATNLRELQHLMERAVTGNYSAKAAIDVALHDLKARSLNLPL
SDLIGGAIQQGIPIAWTLASGDTQRDIAIAEEMIERRRHNRFKIKLGVRSPADDLRHIEK
IIERVGDRAAVRVDINQAWDENTASVWIPRLEAAGVELVEQPVARSNFDALRRLSADNGV
AILADESLSSLASAFELARHHCVDAFSLKLCNMGGVANTLKVAAIAEASGIASYGGTMLD
SSIGTAAALHVYATLPTMPFECELLGPWVLADTLTQTQLEIKDFEIRLPSGPGLGVDIDP
DKLRHFTRAG
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 7/7 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
269 Lys (K) side chain Stabilizes enolate anion intermediate electrostatic stabiliser -- spectator ICS PubMed:19220063
323 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
Nov. 3, 2014, 2:33 a.m. update curation agent pegg setDomainBoundaries.py
Oct. 15, 2015, 3:26 a.m. update curation agent setDomainBoundaries.py sbrown
remove family assignment evidence code ISS -
remove family chloromuconate cycloisomerase -
update name chloromuconate cycloisomerase 2-chloromuconate cycloisomerase
update subgroup muconate cycloisomerase muconate cycloisomerase (syn) like
update superfamily assignment evidence code FSM ISS
Feb. 10, 2017, 3:01 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.