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) R00352
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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).
Pathway ec00020  Citrate cycle (TCA cycle)
ec00720  Reductive carboxylate cycle (CO2 fixation)
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology K01648  ATP citrate (pro-S)-lyase
Genes HSA: 47(ACLY)
PTR: 454672(ACLY)
MCC: 708501(ACLY)
MMU: 104112(Acly)
RNO: 24159(Acly)
CFA: 607852(ACLY)
BTA: 511135(ACLY)
SSC: 100125957(ACL)
ECB: 100053195(ACLY)
MDO: 100011977
GGA: 395373(ACLY)
XLA: 495086(acly) 495316
XTR: 493390(acly)
DRE: 436922(aclya)
BFO: BRAFLDRAFT_98927
CIN: 445783(acl)
SPU: 587157
DME: Dmel_CG8322(ATPCL)
DPO: Dpse_GA20986
DAN: Dana_GF13329
DER: Dere_GG22311
DPE: Dper_GL20648
DSE: Dsec_GM20101
DSI: Dsim_GD25577
DWI: Dwil_GK10643
DYA: Dyak_GE14108
DGR: Dgri_GH19829
DMO: Dmoj_GI20417
DVI: Dvir_GJ20089
AGA: AgaP_AGAP010156
AAG: AaeL_AAEL004297
CQU: CpipJ_CPIJ000859
AME: 550686(ATPCL)
NVI: 100119651(NV13576)
TCA: 656728
API: 100165099(Atpcl)
PHU: Phum_PHUM337470
ISC: IscW_ISCW009919
CEL: B0365.1 D1005.1
CBR: CBG09435 CBG24512
BMY: Bm1_26245
SMM: Smp_127730
NVE: NEMVE_v1g211386
TAD: TRIADDRAFT_22398
ATH: AT1G09430(ACLA-3) AT1G10670(ACLA-1) AT1G60810(ACLA-2)
     AT3G06650(ACLB-1) AT5G49460(ACLB-2)
POP: POPTR_656642 POPTR_658317 POPTR_827990 POPTR_832869
RCU: RCOM_0529250 RCOM_1000580 RCOM_1436330
VVI: 100240939 100255189 100267071
OSA: 4325777(Os01g0300200) 4351176(Os11g0696200)
     4352549(Os12g0566300)
SBI: SORBI_05g027180 SORBI_08g018480
ZMA: 100273868 100282948(pco080711) 100381760
PPP: PHYPADRAFT_174431 PHYPADRAFT_179458 PHYPADRAFT_183136
     PHYPADRAFT_208338
CRE: CHLREDRAFT_186611(ACLB1) CHLREDRAFT_196544(ACLA1)
CME: CMB118C CMB128C
YLI: YALI0D24431g YALI0E34793g
NCR: NCU06783 NCU06785
PAN: PODANSg6774 PODANSg6775
MGR: MGG_06719(MG06719.4) MGG_06720(MG06720.4)
FGR: FG06039.1
SSL: SS1G_02378 SS1G_02379
BFU: BC1G_05989 BC1G_05991
ANI: AN2435.2 AN2436.2
AFM: AFUA_6G10650 AFUA_6G10660
NFI: NFIA_056420 NFIA_056430
AOR: AO090023000205 AO090023000206
ANG: An11g00510 An11g00530
AFV: AFLA_106350
ACT: ACLA_084380 ACLA_084390
PCS: Pc21g20480 Pc21g20490
CIM: CIMG_09690 CIMG_09691
URE: UREG_04629 UREG_04630
PNO: SNOG_06832 SNOG_06833
TML: GSTUM_00005662001 GSTUM_00005664001
SPO: SPAC22A12.16 SPBC1703.07
CNE: CNJ00800
CNB: CNBJ2710
PPL: POSPLDRAFT_106430
LBC: LACBIDRAFT_299612
MPR: MPER_02281
CCI: CC1G_09654
UMA: UM01005.1
MBR: MONBRDRAFT_35919
DDI: DDB_G0278341 DDB_G0278345(acly)
TGO: TGME49_023840
PTI: PHATRDRAFT_54477(ACL)
TDN: Suden_0570 Suden_0571
NIS: NIS_0652 NIS_0653
SUN: SUN_0541 SUN_0542
NAM: NAMH_0713 NAMH_0714
CTE: CT1088 CT1089
CPC: Cpar_1008 Cpar_1009
CCH: Cag_0796 Cag_0797
CPH: Cpha266_1306 Cpha266_1307
CPB: Cphamn1_1350 Cphamn1_1351
CLI: Clim_1231 Clim_1232
PVI: Cvib_0866 Cvib_0867
PLT: Plut_1061 Plut_1062
PPH: Ppha_1392 Ppha_1393
PAA: Paes_1089 Paes_1090
CTS: Ctha_2552 Ctha_2553
SUL: SYO3AOP1_1055 SYO3AOP1_1056
SAF: SULAZ_0527 SULAZ_0528
PMX: PERMA_1714 PERMA_1715
NDE: NIDE0834(aclB) NIDE0835(aclA)
Taxonomy
Reference
  Authors
  Title

  Journal
  Organism
 1  [PMID:6749502]
Lill U, Schreil A, Eggerer H.
Isolation of enzymically active fragments formed by limited
proteolysis of ATP citrate lyase.
Eur. J. Biochem. 125 (1982) 645-50.
Rattus norvegicus [GN:rno]
Reference
  Authors
  Title

  Journal
 2
Srere, P.A. and Lipmann, F.
An enzymatic reaction between citrate, adenosine triphosphate and
coenzyme A.
J. Am. Chem. Soc. 75 (1953) 4874.
Other DBs ExplorEnz - The Enzyme Database: 2.3.3.8
IUBMB Enzyme Nomenclature: 2.3.3.8
ExPASy - ENZYME nomenclature database: 2.3.3.8
BRENDA, the Enzyme Database: 2.3.3.8
CAS: 9027-95-6
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