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
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)
CJC: 
100405725(ACLY)
MMU: 
104112(Acly)
RNO: 
24159(Acly)
NGI: 
103735876(Acly)
HGL: 
101700349(Acly)
OCU: 
100346747(ACLY)
TUP: 
102487454(ACLY)
CFA: 
607852(ACLY)
AML: 
100467494(ACLY)
UMR: 
103672560(ACLY)
FCA: 
100422779(ACLY)
PTG: 
102954566(ACLY)
BTA: 
511135(ACLY)
BOM: 
102287054(ACLY)
PHD: 
102334260(ACLY)
CHX: 
102181894(ACLY)
OAS: 
654404(ACLY)
SSC: 
100125957(ACLY)
CFR: 
102508520(ACLY)
BACU: 
LVE: 
103077497(ACLY)
ECB: 
100053195(ACLY)
MYB: 
102246873(ACLY)
MYD: 
102759921(ACLY)
PALE: 
102888049(ACLY)
MDO: 
100011977(ACLY)
SHR: 
100924578(ACLY)
OAA: 
GGA: 
395373(ACLY)
MGP: 
100544111(ACLY)
APLA: 
101793308(ACLY)
TGU: 
100221719(ACLY)
FAB: 
101805819(ACLY)
PHI: 
102099293(ACLY)
FPG: 
101918381(ACLY)
FCH: 
102047351(ACLY)
CLV: 
102097494(ACLY)
ASN: 
102386616(ACLY)
AMJ: 
102572777(ACLY)
PSS: 
102444696(ACLY)
CMY: 
102930695(ACLY)
ACS: 
100557175(acly)
PBI: 
103067911(ACLY)
XLA: 
XTR: 
493390(acly)
DRE: 
436922(aclya)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102364563(ACLY)
CMK: 
103185738(acly)
BFO: 
CIN: 
445783(acl)
SPU: 
587157(ACLY)
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
MDE: 
AGA: 
AAG: 
CQU: 
AME: 
550686(ATPCL)
NVI: 
TCA: 
BMOR: 
API: 
100165099(Atpcl)
PHU: 
ISC: 
CEL: 
CBR: 
BMY: 
LOA: 
TSP: 
HRO: 
LGI: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
AT1G09430(ACLA-3) AT1G10670(ACLA-1) AT1G60810(ACLA-2) AT3G06650(ACLB-1) AT5G49460(ACLB-2)
ALY: 
CRB: 
EUS: 
BRP: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
MTR: 
CAM: 
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
CSV: 
CMO: 
RCU: 
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: 
SOT: 
OSA: 
DOSA: 
Os01t0300200-01(Os01g0300200) Os11t0693800-01(Os11g0693800) Os11t0696200-01(Os11g0696200) Os12t0566300-01(Os12g0566300)
OBR: 
BDI: 
SBI: 
SORBI_05g027180(SORBIDRAFT_05g027180) SORBI_08g018480(SORBIDRAFT_08g018480)
ZMA: 
100273868(cl718_1(752)) 100282948(pco080711) 100381760(pco065117) 103635086 103643046 103650092
SITA: 
PDA: 
MUS: 
ATR: 
s00003p00077760(AMTR_s00003p00077760) s00045p00030700(AMTR_s00045p00030700) s00096p00027570(AMTR_s00096p00027570)
SMO: 
PPP: 
CRE: 
VCN: 
CSL: 
CVR: 
CME: 
GSL: 
CCP: 
YLI: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
ELA: 
SSL: 
BFU: 
MBE: 
ANI: 
AFM: 
AOR: 
AOR_1_352144(AO090023000205) AOR_1_354144(AO090023000206)
ANG: 
ANI_1_76094(An11g00510) ANI_1_78094(An11g00530)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
TMS: 
PPL: 
DSQ: 
PCO: 
SHS: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MPR: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT115583(AGABI1DRAFT_115583)
ABV: 
AGABI2DRAFT194501(AGABI2DRAFT_194501)
CPUT: 
SLA: 
UMA: 
PFP: 
PGR: 
MLR: 
WSE: 
MBR: 
DDI: 
DPP: 
DFA: 
ACAN: 
TGO: 
PTI: 
PIF: 
NGD: 
TDN: 
SUA: 
SKU: 
SULR: 
NSA: 
NIS: 
SUN: 
NAM: 
CTE: 
CPC: 
CCH: 
CPH: 
CPB: 
CLI: 
PVI: 
PLT: 
PPH: 
PAA: 
CTS: 
SUL: 
SAF: 
PMX: 
TAM: 
DTE: 
NDE: 
NIDE0834(aclB) NIDE0835(aclA)
MHI: 
 » 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

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