KEGG   ENZYME: 2.3.1.223
Entry
EC 2.3.1.223                Enzyme                                 

Name
3-oxo-5,6-didehydrosuberyl-CoA thiolase;
paaJ (gene name)
Class
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
Sysname
2,3-didehydroadipoyl-CoA:acetyl-CoA C-didehydroadipoyltransferase (double bond migration)
Reaction(IUBMB)
2,3-didehydroadipoyl-CoA + acetyl-CoA = CoA + 3-oxo-5,6-didehydrosuberoyl-CoA [RN:R09839]
Reaction(KEGG)
R09839
Substrate
2,3-didehydroadipoyl-CoA;
acetyl-CoA [CPD:C00024]
Product
CoA [CPD:C00010];
3-oxo-5,6-didehydrosuberoyl-CoA [CPD:C19945]
Comment
The enzyme acts in the opposite direction. The enzymes from the bacteria Escherichia coli and Pseudomonas sp. Y2 also have the activity of EC 2.3.1.174 (3-oxoadipyl-CoA thiolase).
History
EC 2.3.1.223 created 2013
Pathway
ec00360  Phenylalanine metabolism
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K02615  3-oxo-5,6-didehydrosuberyl-CoA/3-oxoadipyl-CoA thiolase
Genes
ECO: b1397(paaJ)
ECJ: JW1392(paaJ)
ECD: ECDH10B_1522(paaJ)
EBW: BWG_1226(paaJ)
EOI: ECO111_1791(paaJ)
EOJ: ECO26_2001(paaJ)
EOH: ECO103_1534(paaJ)
ESL: O3K_13485
ESO: O3O_12145
ESM: O3M_13460
ECK: EC55989_1533(paaE)
ELH: ETEC_1472
ECW: EcE24377A_1582(pcaF)
EUN: UMNK88_1804(pcaF)
ECX: EcHS_A1484(pcaF)
ECY: ECSE_1482
ECR: ECIAI1_1397(paaE)
EKF: KO11_15245(paaJ)
EDJ: ECDH1ME8569_1341(paaJ)
ELW: ECW_m1531(paaE)
ELL: WFL_07480(paaJ)
ELP: P12B_c1729(paaJ)
ECOL: LY180_07305(fadA)
EFE: EFER_1599(paaE)
ENC: ECL_02144
ECLX: LI66_10290
ECLY: LI62_11085
ECLZ: LI64_10435
ECLO: ENC_11610
EEC: EcWSU1_02062(paaJ)
ECAN: CWI88_12185(pcaF)
ECHG: FY206_11755(pcaF)
ESH: C1N69_10565(pcaF)
LNI: CWR52_01805(pcaF)
EBG: FAI37_18900(pcaF)
KPN: KPN_01478(paaJ)
KPU: KP1_2481(paaJ)
KPP: A79E_2761
KPT: VK055_1032(pcaF2)
KPR: KPR_2865(paaJ)
KPJ: N559_2853
KPX: PMK1_03796(paaJ)
KPNU: LI86_14235
KPNK: BN49_2540(paaJ)
KVA: Kvar_2889
KPE: KPK_2991(paaJ)
KOX: KOX_19465
KOE: A225_2763
EAE: EAE_20470
EAR: CCG29786
KQV: B8P98_15225(pcaF)
KLW: DA718_15530(pcaF)
CYO: CD187_14230(pcaF)
CPOT: FOB25_01975(pcaF)
EBT: EBL_c16650(paaJ)
RAO: DSD31_14125(pcaF)
RTG: NCTC13098_04015(paaJ_3)
REE: electrica_02710(paaJ)
KIE: NCTC12125_01344(paaJ)
LEI: C2U54_17495(pcaF)
LEH: C3F35_22350(pcaF)
LEE: DVA44_10910(pcaF)
LER: GNG29_12035(pcaF)
LEA: GNG26_12275(pcaF)
LEW: DAI21_16085(pcaF)
BUF: D8682_03060(pcaF)
BAGE: BADSM9389_21450(pcaF)
YRE: HEC60_05185(pcaF)
SGOE: A8O29_012285(pcaF)
EBF: D782_2323
EBU: CUC76_03660(pcaF)
SMAR: SM39_2563(paaJ)
SMAC: SMDB11_2355(paaJ)
SMW: SMWW4_v1c31030(paaJ)
SPE: Spro_3081
SPLY: Q5A_016025(paaJ)
SMAF: D781_2889
SERF: L085_13115
SERM: CLM71_15005(pcaF)
SQU: E4343_00615(pcaF)
SFJ: SAMEA4384070_3131(paaJ)
SOF: NCTC11214_03713(paaJ)
SURI: J0X03_08535(pcaF)
SRHZ: FO014_18875(pcaF)
XBO: XBJ1_0118(paaJ)
XBV: XBW1_0155(paaJ)
XNE: XNC1_4626(paaJ)
XNM: XNC2_4467(paaJ)
XDO: XDD1_3927(paaJ)
XBU: HGO23_00615(pcaF)
PSI: S70_09380
PSX: DR96_1306(pcaF)
PRG: RB151_002340(paaJ)
PALA: CO695_03810(pcaF)
PHEI: NCTC12003_00246(paaJ)
PRQ: CYG50_15075(pcaF)
PRJ: NCTC6933_00251(paaJ)
PVC: G3341_00960(pcaF)
HPAR: AL518_19650(pcaF)
PGH: FH974_15970(pcaF)
PSCQ: KHQ08_01180(pcaF)
PALG: HFP57_16235(pcaF)
ASZ: ASN_1367(paaE)
ATO: CIW82_05220(pcaF)
 » show all
Reference
1  [PMID:20660314]
  Authors
Teufel R, Mascaraque V, Ismail W, Voss M, Perera J, Eisenreich W, Haehnel W, Fuchs G
  Title
Bacterial phenylalanine and phenylacetate catabolic pathway revealed.
  Journal
Proc Natl Acad Sci U S A 107:14390-5 (2010)
DOI:10.1073/pnas.1005399107
  Sequence
[eco:b1397]
Other DBs
ExplorEnz - The Enzyme Database: 2.3.1.223
IUBMB Enzyme Nomenclature: 2.3.1.223
ExPASy - ENZYME nomenclature database: 2.3.1.223
BRENDA, the Enzyme Database: 2.3.1.223

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