KEGG   ENZYME: 5.5.1.1Help
Entry
EC 5.5.1.1                  Enzyme                                 

Name muconate cycloisomerase;
muconate cycloisomerase I;
cis,cis-muconate-lactonizing enzyme;
cis,cis-muconate cycloisomerase;
muconate lactonizing enzyme;
4-carboxymethyl-4-hydroxyisocrotonolactone lyase (decyclizing);
CatB;
MCI
Class Isomerases;
Intramolecular lyases;
Intramolecular lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname 2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
Reaction(IUBMB) 2,5-dihydro-5-oxofuran-2-acetate = cis,cis-hexadienedioate
[RN:R03959]
Reaction(KEGG) R03959 > R06989;
(other) R04489 R05300 R05390 R08116
Show
Substrate 2,5-dihydro-5-oxofuran-2-acetate [CPD:C04105]
Product cis,cis-hexadienedioate [CPD:C02480]
Cofactor Manganese [CPD:C00034]
Comment Requires Mn2+. Also acts (in the reverse reaction) on
3-methyl-cis,cis-hexadienedioate and, very slowly, on
cis,trans-hexadienedioate. Not identical with EC 5.5.1.7
(chloromuconate cycloisomerase) or EC 5.5.1.11 (dichloromuconate
cycloisomerase).
Pathway PATH: ec00362  Benzoate degradation via hydroxylation
PATH: ec00364  Fluorobenzoate degradation
PATH: ec00622  Toluene and xylene degradation
PATH: ec00627  1,4-Dichlorobenzene degradation
PATH: ec01100  Metabolic pathways
Orthology KO: K01856  muconate cycloisomerase
Genes AFM: AFUA_6G11580
EFE: EFER_1479(catB)
ECA: ECA3116
KPN: KPN_01875
KPE: KPK_2481(catB)
KPU: KP1_2941
PAE: PA2509(catB)
PAU: PA14_32220(catB)
PAP: PSPA7_2730(catB)
PAG: PLES_27861(catB)
PPU: PP_3715(catB)
PPF: Pput_2053
PPG: PputGB1_2204
PPW: PputW619_2705
PFL: PFL_3862(catB)
PFO: Pfl01_2325 Pfl01_2963
PFS: PFLU5192
PEN: PSEEN3138(catB)
PSA: PST_1672(catB)
PCR: Pcryo_1270
ACI: ACIAD1446(catB)
ACB: A1S_1843
ABM: ABSDF1994(catB)
ABY: ABAYE1720(catB)
PAT: Patl_2790
FTW: FTW_0641
MMW: Mmwyl1_3042
RPI: Rpic_1361
RPF: Rpic12D_1425
REU: Reut_A1689 Reut_B4400 Reut_D6465 Reut_D6474
REH: H16_A1966(catB3) H16_B0536(catB4)
RME: Rmet_4878
BMA: BMAA0200(catB)
BMV: BMASAVP1_1375(catB)
BML: BMA10229_1572(catB)
BMN: BMA10247_A0231(catB)
BPS: BPSS1891(catB)
BPM: BURPS1710b_A0986(catB)
BPL: BURPS1106A_A2566(catB)
BPD: BURPS668_A2710(catB)
BTE: BTH_II0485
BVI: Bcep1808_4159
BUR: Bcep18194_A4351 Bcep18194_B2328 Bcep18194_C7044
BCN: Bcen_4593
BCH: Bcen2424_3770
BCM: Bcenmc03_3753
BCJ: BCAS0498(catB2)
BAM: Bamb_5499
BAC: BamMC406_6302
BMU: Bmul_3235
BMJ: BMULJ_05290(catB)
BXE: Bxe_A2108(catB) Bxe_C1041
BPT: Bpet1401(catB1) Bpet3349(catB3)
POL: Bpro_4404
PNA: Pnap_2119
AAV: Aave_0199
AJS: Ajs_0140
DIA: Dtpsy_0158
DDE: Dde_1177
MLO: mlr0803
MES: Meso_1539 Meso_2968
SME: SMa1461 SMc00459
ATU: Atu1648
ATC: AGR_C_3037
RET: RHE_CH02350(ypch00769)
RLE: RL2662
BME: BMEI0966
BMF: BAB1_1037
BMB: BruAb1_1023
BMS: BR1018
BOV: BOV_0985
BJA: blr5895
BRA: BRADO0023 BRADO4202 BRADO5087
BBT: BBta_0028 BBta_4577 BBta_5558
RPA: RPA3964
RPB: RPB_1626
RPC: RPC_1451
RPD: RPD_1635
RPE: RPE_1470
NWI: Nwi_1085
NHA: Nham_1314
XAU: Xaut_1132 Xaut_4358
CCR: CC_3113
SIL: SPO3606 SPO3667(catB)
RSP: RSP_1769
RSH: Rsph17029_0415
RSQ: Rsph17025_2483
JAN: Jann_0365 Jann_1408
RDE: RD1_1003
PDE: Pden_1174
HNE: HNE_2922
NAR: Saro_3828
SWI: Swit_0975
RRU: Rru_A2556
BCL: ABC3013
MSM: MSMEG_1910
RHA: RHA1_ro02372(catB)
RER: RER_54220(catB)
ROP: ROP_20860(catB)
SEN: SACE_4412 SACE_6327
RXY: Rxyl_3044
RBA: RB10855
AVA: Ava_3512
TTH: TTC1473
HBU: Hbut_0684
Taxonomy
Structures PDB: 1BKH  1F9C  1MUC  2MUC  2PGW  2ZAD  3CT2  3DGB  3FJ4  3I4K  
     3I6E  3MUC  
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:5330966]
Ornston LN.
The conversion of catechol and protocatechuate to beta-ketoadipate
by Pseudomonas putida. 3. Enzymes of the catechol pathway.
J. Biol. Chem. 241 (1966) 3795-9.
Pseudomonas putida [GN:ppu]
Reference
  Authors
  Title

  Journal
2
Ornston, L.N.
Conversion of catechol and protocatechuate to beta-ketoadipate
(Pseudomonas putida).
Methods Enzymol. 17A (1970) 529-549.
Reference
  Authors
  Title
  Journal
  Organism
3  [PMID:13211620]
SISTROM WR, STANIER RY.
The mechanism of formation of beta-ketoadipic acid by bacteria.
J. Biol. Chem. 210 (1954) 821-36.
Pseudomonas fluorescens
Other DBs ExplorEnz - The Enzyme Database: 5.5.1.1
IUBMB Enzyme Nomenclature: 5.5.1.1
ExPASy - ENZYME nomenclature database: 5.5.1.1
UM-BBD (Biocatalysis/Biodegradation Database): 5.5.1.1
BRENDA, the Enzyme Database: 5.5.1.1
CAS: 9023-72-7

DBGET integrated database retrieval system