EzCatDB: D00283
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DB codeD00283
RLCP classification4.1034.769660.650 : Addition
8.113.594730.651 : Isomerization
CATH domainDomain 13.30.390.10 : Enolase-like; domain 1
Domain 23.20.20.120 : TIM BarrelCatalytic domain
E.C.5.5.1.7

CATH domainRelated DB codes (homologues)
3.20.20.120 : TIM BarrelD00261,D00273,D00282
3.30.390.10 : Enolase-like; domain 1D00261,D00273,D00282

Enzyme Name
UniProtKBKEGG

P05404P27099
Protein nameChloromuconate cycloisomeraseChloromuconate cycloisomerasechloromuconate cycloisomerase
muconate cycloisomerase II
SynonymsEC 5.5.1.7
Muconate cycloisomerase II
EC 5.5.1.7
Muconate cycloisomerase II
RefSeqYP_025386.1 (Protein)
NC_005912.1 (DNA/RNA sequence)
YP_293620.1 (Protein)
NC_007337.1 (DNA/RNA sequence)

PfamPF01188 (MR_MLE)
PF02746 (MR_MLE_N)
[Graphical view]
PF02746 (MR_MLE_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00361gamma-Hexachlorocyclohexane degradation
MAP00364Fluorobenzoate degradation
MAP006271,4-Dichlorobenzene degradation

UniProtKB:Accession NumberP05404P27099
Entry nameTFDD1_RALEJTCBD_PSESQ
Activity2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3- chloro-cis,cis-muconate.2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3- chloro-cis,cis-muconate.
Subunit

Subcellular location

CofactorManganese.Manganese.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00034C03585C04431C01327I00070C04522
CompoundManganese3-Chloro-cis,cis-muconatecis-4-Carboxymethylenebut-2-en-4-olideHCl2-Chloro-2,5-dihydro-5-oxofuran-2-enolate2-Chloro-2,5-dihydro-5-oxofuran-2-acetate
Typeheavy metalcarboxyl group,halidecarboxyl group,aromatic ring (with hetero atoms other than nitrogen atoms)halide

ChEBI18291
35154
1472
18371
17883


PubChem23930
5280608
5459914
313
18348331


              
1chrA01UnboundUnboundUnboundUnboundUnboundUnbound
1chrB01UnboundUnboundUnboundUnboundUnboundUnbound
2chrA01UnboundUnboundUnboundUnboundUnboundUnbound
1nu5A01UnboundUnboundUnboundUnboundUnboundUnbound
1chrA02Bound:_MNUnboundUnboundAnalogue:_CLUnboundUnbound
1chrB02Bound:_MNUnboundUnboundUnboundUnboundUnbound
2chrA02Bound:_MNUnboundUnboundAnalogue:_CLUnboundUnbound
1nu5A02Bound:_MNUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P05404, P27099 & literature [7]
pdbCatalytic residuesCofactor-binding residues
          
1chrA01 
 
1chrB01 
 
2chrA01 
 
1nu5A01 
 
1chrA02LYS 163;LYS 165;LYS 269;GLU 323
ASP 194;GLU 220;ASP 245(Manganese binding)
1chrB02LYS 163;LYS 165;LYS 269;GLU 323
ASP 194;GLU 220;ASP 245(Manganese binding)
2chrA02LYS 163;LYS 165;LYS 269;GLU 323
ASP 194;GLU 220;ASP 245(Manganese binding)
1nu5A02LYS 163;LYS 165;LYS 269;GLU 323
ASP 194;GLU 220;ASP 245(Manganese binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]p.10400-10401
[7]Fig.1, p.132-135
[8]Fig.7, p.4558-4559
[12]p.1857-1858

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS)
JournalActa Crystallogr D Biol Crystallogr
Year1994
Volume50
Pages75-84
AuthorsHoier H, Schloemann M, Hammer A, Glusker JP, Carrell HL, Goldman A, Stezowski JJ, Heinemann U
TitleCrystal structure of chloromuconate cycloisomerase from Alcaligenes eutrophus JMP134 (pJP4) at 3-A resolution.
Related PDB1chr
Related UniProtKBP05404
[2]
PubMed ID8110801
JournalBiochemistry
Year1994
Volume33
Pages1961-70
AuthorsMazur P, Pieken WA, Budihas SR, Williams SE, Wong S, Kozarich JW
TitleCis,cis-muconate lactonizing enzyme from Trichosporon cutaneum: evidence for a novel class of cycloisomerases in eucaryotes.
[3]
PubMed ID8021223
JournalJ Bacteriol
Year1994
Volume176
Pages4366-75
AuthorsVollmer MD, Fischer P, Knackmuss HJ, Schlomann M
TitleInability of muconate cycloisomerases to cause dehalogenation during conversion of 2-chloro-cis,cis-muconate.
[4]
PubMed ID7493952
JournalJ Biol Chem
Year1995
Volume270
Pages29229-35
AuthorsBlasco R, Wittich RM, Mallavarapu M, Timmis KN, Pieper DH
TitleFrom xenobiotic to antibiotic, formation of protoanemonin from 4-chlorocatechol by enzymes of the 3-oxoadipate pathway.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS)
JournalActa Crystallogr D Biol Crystallogr
Year1996
Volume52
Pages858-63
AuthorsKleywegt GJ, Jones TA
TitleA re-evaluation of the crystal structure of chloromuconate cycloisomerase.
Related PDB2chr
Related UniProtKBP05404
[6]
PubMed ID9724714
JournalProc Natl Acad Sci U S A
Year1998
Volume95
Pages10396-401
AuthorsHasson MS, Schlichting I, Moulai J, Taylor K, Barrett W, Kenyon GL, Babbitt PC, Gerlt JA, Petsko GA, Ringe D
TitleEvolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase.
[7]
PubMed ID10336378
JournalProteins
Year1999
Volume34
Pages125-36
AuthorsSchell U, Helin S, Kajander T, Schlomann M, Goldman A
TitleStructural basis for the activity of two muconate cycloisomerase variants toward substituted muconates.
[8]
PubMed ID11443090
JournalJ Bacteriol
Year2001
Volume183
Pages4551-61
AuthorsKaulmann U, Kaschabek SR, Schlomann M
TitleMechanism of chloride elimination from 3-chloro- and 2,4-dichloro-cis,cis-muconate: new insight obtained from analysis of muconate cycloisomerase variant CatB-K169A.
[9]
PubMed ID12218011
JournalJ Bacteriol
Year2002
Volume184
Pages5261-74
AuthorsPollmann K, Kaschabek S, Wray V, Reineke W, Pieper DH
TitleMetabolism of dichloromethylcatechols as central intermediates in the degradation of dichlorotoluenes by Ralstonia sp. strain PS12.
[10]
PubMed ID12218027
JournalJ Bacteriol
Year2002
Volume184
Pages5402-9
AuthorsSkiba A, Hecht V, Pieper DH
TitleFormation of protoanemonin from 2-chloro-cis,cis-muconate by the combined action of muconate cycloisomerase and muconolactone isomerase.
[11]
PubMed ID12859183
JournalBiochemistry
Year2003
Volume42
Pages8387-93
AuthorsSchmidt DM, Mundorff EC, Dojka M, Bermudez E, Ness JE, Govindarajan S, Babbitt PC, Minshull J, Gerlt JA
TitleEvolutionary potential of (beta/alpha)8-barrels: functional promiscuity produced by single substitutions in the enolase superfamily.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), AND COFACTOR
PubMed ID12930985
JournalProtein Sci
Year2003
Volume12
Pages1855-64
AuthorsKajander T, Lehtio L, Schlomann M, Goldman A
TitleThe structure of Pseudomonas P51 Cl-muconate lactonizing enzyme: co-evolution of structure and dynamics with the dehalogenation function.
Related PDB1nu5
Related UniProtKBP27099

comments
This enzyme is homologous to muconate cycloisomerase (E.C. 5.5.1.1; D00282 in EzCatDB), sharing the same reactions, although it further catalyzes dehalogenation.
According to the literature [7], [8], [12], this enzyme catalyzes the following reactions:
(A) Addition of carboxylate oxygen to the C4 double-bonded carbon, forming an enolate intermediate:
(B) Isomerization; Shift of double-bond position (from C=C-O to C-C=O):
(C) Eliminative double-bond formation; Elimination of halogen atom:
The first two reactions are the same as those by the homologous enzyme, muconate cycloisomerase (D00282 in EzCatDB). However, the mechanism of the third reaction has not been elucidated yet.

createdupdated
2004-04-062010-08-05


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