KEGG   ORTHOLOGY: K01648Help
Entry
K01648                      KO                                     

Name
ACLY
Definition
ATP citrate (pro-S)-lyase [EC:2.3.3.8]
Pathway
Citrate cycle (TCA cycle)
Carbon fixation pathways in prokaryotes
Brite
KEGG Orthology (KO) [BR:ko00001]
 Metabolism
  Carbohydrate metabolism
   00020 Citrate cycle (TCA cycle)
    K01648  ACLY; ATP citrate (pro-S)-lyase
  Energy metabolism
   00720 Carbon fixation pathways in prokaryotes
    K01648  ACLY; ATP citrate (pro-S)-lyase
Enzymes [BR:ko01000]
 2. Transferases
  2.3  Acyltransferases
   2.3.3  Acyl groups converted into alkyl groups on transfer
    2.3.3.8  ATP citrate synthase
     K01648  ACLY; ATP citrate (pro-S)-lyase
Exosome [BR:ko04147]
 Exosomal proteins
  Exosomal proteins of haemopoietic cells  (B-cell, T-cell, DC-cell, reticulocyte, and mast cell)
   K01648  ACLY; ATP citrate (pro-S)-lyase
  Exosomal proteins of bladder cancer cells
   K01648  ACLY; ATP citrate (pro-S)-lyase
  Exosomal proteins of melanoma cells
   K01648  ACLY; ATP citrate (pro-S)-lyase
BRITE hierarchy
Other DBs
RN: 
GO: 
Genes
HSA: 
47(ACLY)
PTR: 
454672(ACLY)
PPS: 
100981849(ACLY)
GGO: 
101132535(ACLY)
PON: 
100439535(ACLY)
NLE: 
100601132(ACLY)
MCC: 
708501(ACLY)
MCF: 
102139439(ACLY)
CSAB: 
103243859(ACLY)
RRO: 
104680455(ACLY)
RBB: 
CJC: 
100405725(ACLY)
SBQ: 
101051906(ACLY)
MMU: 
104112(Acly)
RNO: 
24159(Acly)
NGI: 
103735876(Acly)
HGL: 
101700349(Acly)
CCAN: 
109695762(Acly)
OCU: 
100346747(ACLY)
TUP: 
102487454(ACLY)
CFA: 
607852(ACLY)
AML: 
100467494(ACLY)
UMR: 
103672560(ACLY)
FCA: 
100422779(ACLY)
PTG: 
102954566(ACLY)
AJU: 
106972598(ACLY)
BTA: 
511135(ACLY)
BOM: 
102287054(ACLY)
BIU: 
109573634(ACLY)
PHD: 
102334260(ACLY)
CHX: 
102181894(ACLY)
OAS: 
654404(ACLY)
SSC: 
100125957(ACLY)
CFR: 
102508520(ACLY)
CDK: 
105090445(ACLY)
BACU: 
LVE: 
103077497(ACLY)
ECB: 
100053195(ACLY)
EPZ: 
103550376(ACLY)
EAI: 
106826361(ACLY)
MYB: 
102246873(ACLY)
MYD: 
102759921(ACLY)
HAI: 
109395729(ACLY)
RSS: 
PALE: 
102888049(ACLY)
LAV: 
100667233(ACLY)
MDO: 
100011977(ACLY)
SHR: 
100924578(ACLY)
OAA: 
GGA: 
395373(ACLY)
MGP: 
100544111(ACLY)
CJO: 
107325118(ACLY)
APLA: 
101793308(ACLY)
ACYG: 
106048017(ACLY)
TGU: 
100221719(ACLY)
GFR: 
102034815(ACLY)
FAB: 
101805819(ACLY)
PHI: 
102099293(ACLY)
PMAJ: 
107215114(ACLY)
CCW: 
104697755(ACLY)
FPG: 
101918381(ACLY)
FCH: 
102047351(ACLY)
CLV: 
102097494(ACLY)
AAM: 
106487628(ACLY)
ASN: 
102386616(ACLY)
AMJ: 
102572777(ACLY)
PSS: 
102444696(ACLY)
CMY: 
102930695(ACLY)
CPIC: 
101941763(ACLY)
ACS: 
100557175(acly)
PVT: 
110088988(ACLY)
PBI: 
103067911(ACLY)
GJA: 
107116244(ACLY)
XLA: 
495086(acly.S) 495316
XTR: 
493390(acly)
NPR: 
108788936(ACLY)
DRE: 
436922(aclya)
SRX: 
SANH: 
SGH: 
IPU: 
TRU: 
TNG: 
LCO: 
NCC: 
MZE: 
OLA: 
XMA: 
CSEM: 
LCF: 
HCQ: 
BPEC: 
SASA: 
ELS: 
105013338(acly)
SFM: 
LCM: 
102364563(ACLY)
CMK: 
103185738(acly)
BFO: 
CIN: 
445783(acl)
SPU: 
587157(ACLY)
SKO: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
Dsimw501_GD25577(Dsim_GD25577)
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
MDE: 
AGA: 
AAG: 
CQU: 
AME: 
550686(ATPCL)
BIM: 
BTER: 
SOC: 
AEC: 
ACEP: 
PBAR: 
HST: 
CFO: 
LHU: 
PGC: 
NVI: 
TCA: 
DPA: 
NVL: 
BMOR: 
DPL: 
PXY: 
API: 
100165099(Atpcl)
DNX: 
PHU: 
DPX: 
ISC: 
TUT: 
CEL: 
CELE_B0365.1(acly-2) CELE_D1005.1(acly-1)
CBR: 
NAI: 
BMY: 
LOA: 
TSP: 
HRO: 
LGI: 
CRG: 
OBI: 
LAK: 
SMM: 
SHX: 
OVI: 
NVE: 
ADF: 
HMG: 
TAD: 
AQU: 
ATH: 
AT1G09430(ACLA-3) AT1G10670(ACLA-1) AT1G60810(ACLA-2) AT3G06650(ACLB-1) AT5G49460(ACLB-2)
ALY: 
CRB: 
EUS: 
BRP: 
BNA: 
BOE: 
THJ: 
CIT: 
CIC: 
TCC: 
GRA: 
GHI: 
EGR: 
GMX: 
PVU: 
VRA: 
VAR: 
CCAJ: 
MTR: 
CAM: 
ADU: 
AIP: 
LJA: 
Lj0g3v0068209.1(Lj0g3v0068209.1) Lj1g3v4804050.1(Lj1g3v4804050.1) Lj1g3v4804050.2(Lj1g3v4804050.2) Lj2g3v1415070.1(Lj2g3v1415070.1) Lj2g3v1415070.2(Lj2g3v1415070.2) Lj3g3v0937850.1(Lj3g3v0937850.1) Lj4g3v2265020.1(Lj4g3v2265020.1) Lj4g3v2266260.1(Lj4g3v2266260.1) Lj6g3v1915820.1(Lj6g3v1915820.1) Lj6g3v1915820.2(Lj6g3v1915820.2) Lj6g3v1915830.1(Lj6g3v1915830.1)
LANG: 
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
ZJU: 
CSV: 
CMO: 
RCU: 
JCU: 
POP: 
POPTR_0005s00670g POPTR_0008s10480g(POPTRDRAFT_656642) POPTR_0008s19320g(POPTRDRAFT_832869) POPTR_0010s05260g(POPTRDRAFT_658317) POPTR_0010s15590g(POPTRDRAFT_723928) POPTR_0013s00580g(POPTRDRAFT_823560)
VVI: 
SLY: 
SPEN: 
SOT: 
CANN: 
NTA: 
INI: 
SIND: 
BVG: 
NNU: 
OSA: 
4325777(ACLB-1) 4352549(ACLA-3) 9272295
DOSA: 
Os01t0300200-01(Os01g0300200) Os11t0693800-01(Os11g0693800) Os11t0696200-01(Os11g0696200) Os12t0566300-01(Os12g0566300)
OBR: 
BDI: 
ATS: 
SBI: 
ZMA: 
100273868(cl718_1(752)) 100282948(pco080711) 100381760(pco065117) 103635086
SITA: 
PDA: 
EGU: 
MUS: 
ATR: 
SMO: 
PPP: 
CRE: 
VCN: 
CSL: 
CVR: 
APRO: 
CME: 
GSL: 
CCP: 
YLI: 
NCR: 
NTE: 
NEUTE1DRAFT117451(NEUTE1DRAFT_117451) NEUTE1DRAFT123184(NEUTE1DRAFT_123184)
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
FPU: 
FVR: 
FOX: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
VDA: 
CFJ: 
ELA: 
PFY: 
SSL: 
BFU: 
MBE: 
PSCO: 
GLZ: 
ANI: 
AFM: 
AOR: 
AOR_1_352144(AO090023000205) AOR_1_354144(AO090023000206)
ANG: 
ANI_1_76094(An11g00510) ANI_1_78094(An11g00530)
AFV: 
ACT: 
NFI: 
PCS: 
PDP: 
CIM: 
CPW: 
PBL: 
PBN: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
TMS: 
PPL: 
TVS: 
DSQ: 
PCO: 
SHS: 
HIR: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MPR: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT115583(AGABI1DRAFT_115583)
ABV: 
AGABI2DRAFT194501(AGABI2DRAFT_194501)
CPUT: 
SLA: 
WSE: 
WIC: 
UMA: 
PFP: 
PGR: 
MLR: 
MBR: 
SRE: 
DDI: 
DPP: 
DFA: 
ACAN: 
TGO: 
SMIN: 
v1.2.003200.t1(symbB.v1.2.003200.t1) v1.2.026551.t1(symbB.v1.2.026551.t1) v1.2.028198.t1(symbB.v1.2.028198.t1) v1.2.028199.t1(symbB.v1.2.028199.t1) v1.2.030373.t1(symbB.v1.2.030373.t1) v1.2.036589.t1(symbB.v1.2.036589.t1) v1.2.036589.t2(symbB.v1.2.036589.t2)
PTI: 
FCY: 
AAF: 
NGD: 
PIF: 
PSOJ: 
SPAR: 
 » show all
TaxonomyKoalaUniProt
Reference
  Authors
Beckner ME, Fellows-Mayle W, Zhang Z, Agostino NR, Kant JA, Day BW, Pollack IF
  Title
Identification of ATP citrate lyase as a positive regulator of glycolytic function in glioblastomas.
  Journal
Int J Cancer 126:2282-95 (2010)
DOI:10.1002/ijc.24918

KEGG   ORTHOLOGY: K15230Help
Entry
K15230                      KO                                     

Name
aclA
Definition
ATP-citrate lyase alpha-subunit [EC:2.3.3.8]
Pathway
Citrate cycle (TCA cycle)
Carbon fixation pathways in prokaryotes
Carbon metabolism
Module
M00173  
Reductive citrate cycle (Arnon-Buchanan cycle)
Brite
KEGG Orthology (KO) [BR:ko00001]
 Metabolism
  Overview
   01200 Carbon metabolism
    K15230  aclA; ATP-citrate lyase alpha-subunit
  Carbohydrate metabolism
   00020 Citrate cycle (TCA cycle)
    K15230  aclA; ATP-citrate lyase alpha-subunit
  Energy metabolism
   00720 Carbon fixation pathways in prokaryotes
    K15230  aclA; ATP-citrate lyase alpha-subunit
KEGG modules [BR:ko00002]
 Pathway module
  Energy metabolism
   Carbon fixation
    M00173  Reductive citrate cycle (Arnon-Buchanan cycle)
     K15230  aclA; ATP-citrate lyase alpha-subunit
Enzymes [BR:ko01000]
 2. Transferases
  2.3  Acyltransferases
   2.3.3  Acyl groups converted into alkyl groups on transfer
    2.3.3.8  ATP citrate synthase
     K15230  aclA; ATP-citrate lyase alpha-subunit
BRITE hierarchy
Other DBs
RN: 
GO: 
Genes
TDN: 
SUA: 
SKU: 
SULR: 
SMUL: 
SMUL_0067(aclB)
NSA: 
NIS: 
SUN: 
SLH: 
NAM: 
CTE: 
CPC: 
CLZ: 
CCH: 
CPH: 
CPB: 
CLI: 
PVI: 
PLT: 
PPH: 
PAA: 
PROC: 
PRS: 
PROS: 
CTS: 
SUL: 
SAF: 
PMX: 
TAM: 
DTE: 
NDE: 
NIDE0835(aclA)
NMV: 
NIO: 
NJA: 
NSJP_1800(aclA)
MHI: 
 » show all
TaxonomyKoalaUniProt
Reference
  Authors
Aoshima M, Ishii M, Igarashi Y
  Title
A novel enzyme, citryl-CoA lyase, catalysing the second step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK-6.
  Journal
Mol Microbiol 52:763-70 (2004)
DOI:10.1111/j.1365-2958.2004.04010.x

KEGG   ORTHOLOGY: K15231Help
Entry
K15231                      KO                                     

Name
aclB
Definition
ATP-citrate lyase beta-subunit [EC:2.3.3.8]
Pathway
Citrate cycle (TCA cycle)
Carbon fixation pathways in prokaryotes
Carbon metabolism
Module
M00173  
Reductive citrate cycle (Arnon-Buchanan cycle)
Brite
KEGG Orthology (KO) [BR:ko00001]
 Metabolism
  Overview
   01200 Carbon metabolism
    K15231  aclB; ATP-citrate lyase beta-subunit
  Carbohydrate metabolism
   00020 Citrate cycle (TCA cycle)
    K15231  aclB; ATP-citrate lyase beta-subunit
  Energy metabolism
   00720 Carbon fixation pathways in prokaryotes
    K15231  aclB; ATP-citrate lyase beta-subunit
KEGG modules [BR:ko00002]
 Pathway module
  Energy metabolism
   Carbon fixation
    M00173  Reductive citrate cycle (Arnon-Buchanan cycle)
     K15231  aclB; ATP-citrate lyase beta-subunit
Enzymes [BR:ko01000]
 2. Transferases
  2.3  Acyltransferases
   2.3.3  Acyl groups converted into alkyl groups on transfer
    2.3.3.8  ATP citrate synthase
     K15231  aclB; ATP-citrate lyase beta-subunit
BRITE hierarchy
Other DBs
RN: 
GO: 
Genes
TDN: 
SUA: 
SKU: 
SULR: 
SMUL: 
SMUL_0066(aclA)
NSA: 
NIS: 
SUN: 
SLH: 
NAM: 
CTE: 
CPC: 
CLZ: 
CCH: 
CPH: 
CPB: 
CLI: 
PVI: 
PLT: 
PPH: 
PAA: 
PROC: 
PRS: 
PROS: 
CTS: 
SUL: 
SAF: 
PMX: 
TAM: 
DTE: 
NDE: 
NIDE0834(aclB)
NMV: 
NIO: 
NJA: 
NSJP_1799(aclB)
MHI: 
LOKI: 
 » show all
TaxonomyKoalaUniProt
Reference
  Authors
Aoshima M, Ishii M, Igarashi Y
  Title
A novel enzyme, citryl-CoA lyase, catalysing the second step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK-6.
  Journal
Mol Microbiol 52:763-70 (2004)
DOI:10.1111/j.1365-2958.2004.04010.x

KEGG   ENZYME: 2.3.3.8Help
Entry
EC 2.3.3.8                  Enzyme                                 

Name
ATP citrate synthase;
ATP-citric lyase;
ATP:citrate oxaloacetate-lyase [(pro-S)-CH2COO-->acetyl-CoA] (ATP-dephosphorylating);
acetyl-CoA:oxaloacetate acetyltransferase (isomerizing;
ADP-phosphorylating);
adenosine triphosphate citrate lyase;
citrate cleavage enzyme;
citrate-ATP lyase;
citric cleavage enzyme;
ATP citrate (pro-S)-lyase
Class
Transferases;
Acyltransferases;
Acyl groups converted into alkyl groups on transfer
BRITE hierarchy
Sysname
acetyl-CoA:oxaloacetate C-acetyltransferase [(pro-S)-carboxymethyl-forming, ADP-phosphorylating]
Reaction(IUBMB)
ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA [RN:R00352]
Reaction(KEGG)
Substrate
ADP [CPD:C00008];
phosphate [CPD:C00009];
acetyl-CoA [CPD:C00024];
oxaloacetate [CPD:C00036]
Product
ATP [CPD:C00002];
citrate [CPD:C00158];
CoA [CPD:C00010]
Comment
The enzyme can be dissociated into components, two of which are identical with EC 4.1.3.34 (citryl-CoA lyase) and EC 6.2.1.18 (citrate---CoA ligase).
History
EC 2.3.3.8 created 1965 as EC 4.1.3.8, modified 1986, transferred 2002 to EC 2.3.3.8
Pathway
Citrate cycle (TCA cycle)
Carbon fixation pathways in prokaryotes
Metabolic pathways
Biosynthesis of secondary metabolites
Microbial metabolism in diverse environments
Biosynthesis of antibiotics
Orthology
K01648  
ATP citrate (pro-S)-lyase
K15230  
ATP-citrate lyase alpha-subunit
K15231  
ATP-citrate lyase beta-subunit
Genes
HSA: 
47(ACLY)
PTR: 
454672(ACLY)
PPS: 
100981849(ACLY)
GGO: 
101132535(ACLY)
PON: 
100439535(ACLY)
NLE: 
100601132(ACLY)
MCC: 
708501(ACLY)
MCF: 
102139439(ACLY)
CSAB: 
103243859(ACLY)
RRO: 
104680455(ACLY)
RBB: 
CJC: 
100405725(ACLY)
SBQ: 
101051906(ACLY)
MMU: 
104112(Acly)
RNO: 
24159(Acly)
NGI: 
103735876(Acly)
HGL: 
101700349(Acly)
CCAN: 
109695762(Acly)
OCU: 
100346747(ACLY)
TUP: 
102487454(ACLY)
CFA: 
607852(ACLY)
AML: 
100467494(ACLY)
UMR: 
103672560(ACLY)
FCA: 
100422779(ACLY)
PTG: 
102954566(ACLY)
AJU: 
106972598(ACLY)
BTA: 
511135(ACLY)
BOM: 
102287054(ACLY)
BIU: 
109573634(ACLY)
PHD: 
102334260(ACLY)
CHX: 
102181894(ACLY)
OAS: 
654404(ACLY)
SSC: 
100125957(ACLY)
CFR: 
102508520(ACLY)
CDK: 
105090445(ACLY)
BACU: 
LVE: 
103077497(ACLY)
ECB: 
100053195(ACLY)
EPZ: 
103550376(ACLY)
EAI: 
106826361(ACLY)
MYB: 
102246873(ACLY)
MYD: 
102759921(ACLY)
HAI: 
109395729(ACLY)
RSS: 
PALE: 
102888049(ACLY)
LAV: 
100667233(ACLY)
MDO: 
100011977(ACLY)
SHR: 
100924578(ACLY)
OAA: 
GGA: 
395373(ACLY)
MGP: 
100544111(ACLY)
CJO: 
107325118(ACLY)
APLA: 
101793308(ACLY)
ACYG: 
106048017(ACLY)
TGU: 
100221719(ACLY)
GFR: 
102034815(ACLY)
FAB: 
101805819(ACLY)
PHI: 
102099293(ACLY)
PMAJ: 
107215114(ACLY)
CCW: 
104697755(ACLY)
FPG: 
101918381(ACLY)
FCH: 
102047351(ACLY)
CLV: 
102097494(ACLY)
AAM: 
106487628(ACLY)
ASN: 
102386616(ACLY)
AMJ: 
102572777(ACLY)
PSS: 
102444696(ACLY)
CMY: 
102930695(ACLY)
CPIC: 
101941763(ACLY)
ACS: 
100557175(acly)
PVT: 
110088988(ACLY)
PBI: 
103067911(ACLY)
GJA: 
107116244(ACLY)
XLA: 
495086(acly.S) 495316
XTR: 
493390(acly)
NPR: 
108788936(ACLY)
DRE: 
436922(aclya)
SRX: 
SANH: 
SGH: 
IPU: 
TRU: 
TNG: 
LCO: 
NCC: 
MZE: 
OLA: 
XMA: 
CSEM: 
LCF: 
HCQ: 
BPEC: 
SASA: 
ELS: 
105013338(acly)
SFM: 
LCM: 
102364563(ACLY)
CMK: 
103185738(acly)
BFO: 
CIN: 
445783(acl)
SPU: 
587157(ACLY)
SKO: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
Dsimw501_GD25577(Dsim_GD25577)
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
MDE: 
AGA: 
AAG: 
CQU: 
AME: 
550686(ATPCL)
BIM: 
BTER: 
SOC: 
AEC: 
ACEP: 
PBAR: 
HST: 
CFO: 
LHU: 
PGC: 
NVI: 
TCA: 
DPA: 
NVL: 
BMOR: 
DPL: 
PXY: 
API: 
100165099(Atpcl)
DNX: 
PHU: 
DPX: 
ISC: 
TUT: 
CEL: 
CELE_B0365.1(acly-2) CELE_D1005.1(acly-1)
CBR: 
NAI: 
BMY: 
LOA: 
TSP: 
HRO: 
LGI: 
CRG: 
OBI: 
LAK: 
SMM: 
SHX: 
OVI: 
NVE: 
ADF: 
HMG: 
TAD: 
AQU: 
ATH: 
AT1G09430(ACLA-3) AT1G10670(ACLA-1) AT1G60810(ACLA-2) AT3G06650(ACLB-1) AT5G49460(ACLB-2)
ALY: 
CRB: 
EUS: 
BRP: 
BNA: 
BOE: 
THJ: 
CIT: 
CIC: 
TCC: 
GRA: 
GHI: 
EGR: 
GMX: 
PVU: 
VRA: 
VAR: 
CCAJ: 
MTR: 
CAM: 
ADU: 
AIP: 
LJA: 
Lj0g3v0068209.1(Lj0g3v0068209.1) Lj1g3v4804050.1(Lj1g3v4804050.1) Lj1g3v4804050.2(Lj1g3v4804050.2) Lj2g3v1415070.1(Lj2g3v1415070.1) Lj2g3v1415070.2(Lj2g3v1415070.2) Lj3g3v0937850.1(Lj3g3v0937850.1) Lj4g3v2265020.1(Lj4g3v2265020.1) Lj4g3v2266260.1(Lj4g3v2266260.1) Lj6g3v1915820.1(Lj6g3v1915820.1) Lj6g3v1915820.2(Lj6g3v1915820.2) Lj6g3v1915830.1(Lj6g3v1915830.1)
LANG: 
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
ZJU: 
CSV: 
CMO: 
RCU: 
JCU: 
POP: 
POPTR_0005s00670g POPTR_0008s10480g(POPTRDRAFT_656642) POPTR_0008s19320g(POPTRDRAFT_832869) POPTR_0010s05260g(POPTRDRAFT_658317) POPTR_0010s15590g(POPTRDRAFT_723928) POPTR_0013s00580g(POPTRDRAFT_823560)
VVI: 
SLY: 
SPEN: 
SOT: 
CANN: 
NTA: 
INI: 
SIND: 
BVG: 
NNU: 
OSA: 
4325777(ACLB-1) 4352549(ACLA-3) 9272295
DOSA: 
Os01t0300200-01(Os01g0300200) Os11t0693800-01(Os11g0693800) Os11t0696200-01(Os11g0696200) Os12t0566300-01(Os12g0566300)
OBR: 
BDI: 
ATS: 
SBI: 
ZMA: 
100273868(cl718_1(752)) 100282948(pco080711) 100381760(pco065117) 103635086
SITA: 
PDA: 
EGU: 
MUS: 
ATR: 
SMO: 
PPP: 
CRE: 
VCN: 
CSL: 
CVR: 
APRO: 
CME: 
GSL: 
CCP: 
YLI: 
NCR: 
NTE: 
NEUTE1DRAFT117451(NEUTE1DRAFT_117451) NEUTE1DRAFT123184(NEUTE1DRAFT_123184)
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
FPU: 
FVR: 
FOX: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
VDA: 
CFJ: 
ELA: 
PFY: 
SSL: 
BFU: 
MBE: 
PSCO: 
GLZ: 
ANI: 
AFM: 
AOR: 
AOR_1_352144(AO090023000205) AOR_1_354144(AO090023000206)
ANG: 
ANI_1_76094(An11g00510) ANI_1_78094(An11g00530)
AFV: 
ACT: 
NFI: 
PCS: 
PDP: 
CIM: 
CPW: 
PBL: 
PBN: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
TMS: 
PPL: 
TVS: 
DSQ: 
PCO: 
SHS: 
HIR: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MPR: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT115583(AGABI1DRAFT_115583)
ABV: 
AGABI2DRAFT194501(AGABI2DRAFT_194501)
CPUT: 
SLA: 
WSE: 
WIC: 
UMA: 
PFP: 
PGR: 
MLR: 
MBR: 
SRE: 
DDI: 
DPP: 
DFA: 
ACAN: 
TGO: 
SMIN: 
v1.2.003200.t1(symbB.v1.2.003200.t1) v1.2.026551.t1(symbB.v1.2.026551.t1) v1.2.028198.t1(symbB.v1.2.028198.t1) v1.2.028199.t1(symbB.v1.2.028199.t1) v1.2.030373.t1(symbB.v1.2.030373.t1) v1.2.036589.t1(symbB.v1.2.036589.t1) v1.2.036589.t2(symbB.v1.2.036589.t2)
PTI: 
FCY: 
AAF: 
NGD: 
PIF: 
PSOJ: 
SPAR: 
TDN: 
SUA: 
SKU: 
SULR: 
SMUL: 
SMUL_0066(aclA) SMUL_0067(aclB)
NSA: 
NIS: 
SUN: 
SLH: 
NAM: 
CTE: 
CPC: 
CLZ: 
CCH: 
CPH: 
CPB: 
CLI: 
PVI: 
PLT: 
PPH: 
PAA: 
PROC: 
PRS: 
PROS: 
CTS: 
SUL: 
SAF: 
PMX: 
TAM: 
DTE: 
NDE: 
NIDE0834(aclB) NIDE0835(aclA)
NMV: 
NIO: 
NJA: 
NSJP_1799(aclB) NSJP_1800(aclA)
MHI: 
LOKI: 
 » show all
Taxonomy
Reference
1  [PMID:6749502]
  Authors
Lill U, Schreil A, Eggerer H.
  Title
Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase.
  Journal
Eur. J. Biochem. 125 (1982) 645-50.
Reference
2
  Authors
Srere, P.A. and Lipmann, F.
  Title
An enzymatic reaction between citrate, adenosine triphosphate and coenzyme A.
  Journal
J. Am. Chem. Soc. 75 (1953) 4874.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9027-95-6

KEGG   REACTION: R00352Help
Entry
R00352                      Reaction                               

Name
acetyl-CoA:oxaloacetate C-acetyltransferase [(pro-S)-carboxymethyl-forming, ADP-phosphorylating]
Definition
ATP + Citrate + CoA <=> ADP + Orthophosphate + Acetyl-CoA + Oxaloacetate
Equation
Comment
multi-step reaction (see R01322+R00354)
Reaction class
C00002_C00008
C00010_C00024
C00036_C00158
Enzyme
Pathway
Citrate cycle (TCA cycle)
Carbon fixation pathways in prokaryotes
Metabolic pathways
Biosynthesis of secondary metabolites
Microbial metabolism in diverse environments
Biosynthesis of antibiotics
Carbon metabolism
Module
M00173  
Reductive citrate cycle (Arnon-Buchanan cycle)
Orthology
K01648  
ATP citrate (pro-S)-lyase [EC:2.3.3.8]
K15230  
ATP-citrate lyase alpha-subunit [EC:2.3.3.8]
K15231  
ATP-citrate lyase beta-subunit [EC:2.3.3.8]
Other DBs
RHEA: 

DBGET integrated database retrieval system