KEGG   ENZYME: 2.8.3.8Help
Entry
EC 2.8.3.8                  Enzyme                                 

Name acetate CoA-transferase;
acetate coenzyme A-transferase;
butyryl CoA:acetate CoA transferase;
butyryl coenzyme A transferase;
succinyl-CoA:acetate CoA transferase
Class Transferases;
Transferring sulfur-containing groups;
CoA-transferases
BRITE hierarchy
Sysname acyl-CoA:acetate CoA-transferase
Reaction(IUBMB) acyl-CoA + acetate = a fatty acid anion + acetyl-CoA [RN:R00393]
Reaction(KEGG) R00393 > R01179 R01359 R07832
Show
Substrate acyl-CoA [CPD:C00040];
acetate [CPD:C00033]
Product fatty acid anion [CPD:C02403];
acetyl-CoA [CPD:C00024]
Comment Acts on butanoyl-CoA and pentanoyl-CoA.
Pathway PATH: ec00632  Benzoate degradation via CoA ligation
PATH: ec00640  Propanoate metabolism
PATH: ec00650  Butanoate metabolism
PATH: ec01100  Metabolic pathways
Orthology KO: K01034  acetate CoA-transferase alpha subunit
KO: K01035  acetate CoA-transferase beta subunit
Genes ECO: b2221(atoD) b2222(atoA)
ECJ: JW2215(atoD) JW2216(atoA)
ECD: ECDH10B_2379(atoD)
EBW: BWG_1995(atoD)
ECG: E2348C_2366(atoD)
ECC: c2764(atoD) c2765(atoA)
ECI: UTI89_C2503(atoD) UTI89_C2504(atoA)
ECP: ECP_2266
ECV: APECO1_4337(atoA) APECO1_4338(atoD)
ECX: EcHS_A2362(pcaI) EcHS_A2363
ECM: EcSMS35_2370(pcaI) EcSMS35_2371
ECL: EcolC_1429
ECQ: ECED1_2687(atoD)
ECT: ECIAI39_2359(atoD)
ECZ: ECS88_2370(atoD)
EUM: ECUMN_2559(atoD)
ELF: LF82_0188(atoD)
EBL: B21_02107(atoD)
EBD: ECBD_1438
EBR: ECB_02148(atoD)
EFE: EFER_0938(atoD)
SSN: SSON_2280(atoD) SSON_2281(atoA)
ECA: ECA1283(atoA) ECA1284(atoD)
PCT: PC1_1162
PWA: Pecwa_3169
PLU: plu3799(atoD) plu3800(atoA)
PAY: PAU_01019(atoA) PAU_01020(atoD)
CKO: CKO_00547 CKO_00548
EIC: NT01EI_2206
ETR: ETAE_2012(atoD)
DDA: Dd703_1374
HIN: HI0773(atoA) HI0774
HIT: NTHI0934(atoA) NTHI0935(atoD)
HIQ: CGSHiGG_07370
HSM: HSM_0807 HSM_0808
AAT: D11S_0077
ACI: ACIAD2514(atoA)
RPI: Rpic_4029
RPF: Rpic12D_4141
LCH: Lcho_2490
SFU: Sfum_2291
BJA: bll3461(pcaJ)
RPC: RPC_0637 RPC_0829 RPC_2003
NHA: Nham_0867 Nham_0868
MET: M446_1573
MNO: Mnod_2277
BID: Bind_3273
MSL: Msil_1855
RRU: Rru_A1382 Rru_A1383 Rru_A1472
BAH: BAMEG_2299(atoD)
BAI: BAA_2359(atoD)
BCA: BCE_2329(atoD)
BCZ: BCZK2074(atoD) BCZK2075(atoA)
BCR: BCAH187_A2403(atoD)
BCB: BCB4264_A2276(atoD)
BCU: BCAH820_2320(atoD)
BCG: BCG9842_B3047(atoD)
BCQ: BCQ_2229(atoD)
BCX: BCA_2376(atoD)
BCY: Bcer98_1683 Bcer98_1684
BTK: BT9727_2078(atoD) BT9727_2079(atoA)
BTL: BALH_2057 BALH_2058
BWE: BcerKBAB4_2113 BcerKBAB4_2114
BAY: RBAM_019560(yodS)
BPU: BPUM_0613(atoD) BPUM_0614(yodR)
BBE: BBR47_20940
SPY: SPy_0141(atoD.2) SPy_0142 SPy_1638(atoD.1) SPy_1639(atoA)
SPZ: M5005_Spy_0120(atoD.2) M5005_Spy_1345(atoD.1)
     M5005_Spy_1346(atoA)
SPM: spyM18_0137 spyM18_0138 spyM18_1646(atoD) spyM18_1647(atoA)
SPG: SpyM3_0109(atoD.2) SpyM3_0110 SpyM3_1379(atoD.1)
     SpyM3_1380(atoA)
SPS: SPs0111 SPs0112 SPs0482 SPs0483
SPH: MGAS10270_Spy0122(atoD2) MGAS10270_Spy0123
     MGAS10270_Spy1462(atoD1) MGAS10270_Spy1463(atoA)
SPI: MGAS10750_Spy0125(atoD2) MGAS10750_Spy1454(atoD1)
     MGAS10750_Spy1455(atoA)
SPJ: MGAS2096_Spy0124(atoD2) MGAS2096_Spy0125
     MGAS2096_Spy1366(atoD1) MGAS2096_Spy1367(atoA)
SPK: MGAS9429_Spy0122(atoD2) MGAS9429_Spy0123
     MGAS9429_Spy1340(atoD1) MGAS9429_Spy1341(atoA)
SPF: SpyM50115(atoD1) SpyM50116(atoA1) SpyM50446(atoD2)
SPA: M6_Spy0167 M6_Spy0168 M6_Spy1391 M6_Spy1392
SPB: M28_Spy0118(atoD.2) M28_Spy1386(atoD.1) M28_Spy1387(atoA)
SOZ: Spy49_0124(atoD.2) Spy49_1269(atoD1)
SEQ: SZO_05200
SEZ: Sez_1435 Sez_1436
SEU: SEQ_1626
SUB: SUB1395(atoD2)
SDS: SDEG_1701(atoD.1)
CDF: CD2677(ctfA) CD2678(ctfB)
CDC: CD196_2518(ctfA)
CDL: CDR20291_2565(ctfA)
CBO: CBO2847(ctfA) CBO2848(ctfB)
CBA: CLB_2790
CBH: CLC_2723
CBY: CLM_3218
CBL: CLK_2238
CBK: CLL_A0698 CLL_A2133
CBB: CLD_1723
CBI: CLJ_B3081
CBT: CLH_1917
CBF: CLI_2897
CBE: Cbei_2654 Cbei_3833
AOE: Clos_2361
TTE: TTE0720(atoD) TTE0721(atoA)
NTH: Nther_1910 Nther_2248
PGI: PG1066(ctfA) PG1075
PGN: PGN_1162
TLE: Tlet_1556
TME: Tmel_1136
TAF: THA_1442
FNO: Fnod_0212
PMO: Pmob_1075
KOL: Kole_0597
Taxonomy
Structures PDB: 1K6D  
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:4884054]
Vanderwinkel E, Furmanski P, Reeves HC, Ajl SJ.
Growth of Escherichia coli on fatty acids: requirement for coenzyme
A transferase activity.
Biochem. Biophys. Res. Commun. 33 (1968) 902-8.
Escherichia coli [GN:eco]
Reference
  Authors
  Title



  Journal
  Organism
2  [PMID:11741862]
Kaschabek SR, Kuhn B, Muller D, Schmidt E, Reineke W.
Degradation of aromatics and chloroaromatics by Pseudomonas sp.
strain B13: purification and characterization of
3-oxoadipate:succinyl-coenzyme A (CoA) transferase and
3-oxoadipyl-CoA thiolase.
J. Bacteriol. 184 (2002) 207-15.
Pseudomonas sp.
Reference
  Authors
  Title



  Journal
  Organism
3  [PMID:11741863]
Gobel M, Kassel-Cati K, Schmidt E, Reineke W.
Degradation of aromatics and chloroaromatics by Pseudomonas sp.
strain B13: cloning, characterization, and analysis of sequences
encoding 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and
3-oxoadipyl-CoA thiolase.
J. Bacteriol. 184 (2002) 216-23.
Pseudomonas sp.
Other DBs ExplorEnz - The Enzyme Database: 2.8.3.8
IUBMB Enzyme Nomenclature: 2.8.3.8
ExPASy - ENZYME nomenclature database: 2.8.3.8
UM-BBD (Biocatalysis/Biodegradation Database): 2.8.3.8
BRENDA, the Enzyme Database: 2.8.3.8
CAS: 37278-35-6

DBGET integrated database retrieval system