KEGG   ENZYME: 2.1.1.100Help
Entry
EC 2.1.1.100                Enzyme                                 

Name
protein-S-isoprenylcysteine O-methyltransferase;
farnesyl cysteine C-terminal methyltransferase;
farnesyl-protein carboxymethyltransferase;
protein C-terminal farnesylcysteine O-methyltransferase;
farnesylated protein C-terminal O-methyltransferase;
isoprenylated protein methyltransferase;
prenylated protein methyltransferase;
protein S-farnesylcysteine C-terminal methyltransferase;
S-farnesylcysteine methyltransferase;
prenylcysteine carboxylmethyltransferase [misleading];
prenylcysteine carboxymethyltransferase [misleading];
prenylcysteine methyltransferase
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:protein-C-terminal-S-farnesyl-L-cysteine O-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine = S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester [RN:R04496]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:C00019];
protein C-terminal S-farnesyl-L-cysteine [CPD:C04506]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
protein C-terminal S-farnesyl-L-cysteine methyl ester [CPD:C04748]
Comment
C-terminal S-geranylgeranylcysteine and S-geranylcysteine residues are also methylated, but more slowly.
History
EC 2.1.1.100 created 1992 (EC 2.1.1.24 created 1972, modified 1983, modified 1989, part incorporated 1992)
Pathway
Terpenoid backbone biosynthesis
Orthology
K00587  
protein-S-isoprenylcysteine O-methyltransferase
Genes
HSA: 
23463(ICMT)
PTR: 
469782(ICMT)
PPS: 
100978940(ICMT)
GGO: 
101151352(ICMT)
PON: 
100456656(ICMT)
NLE: 
100583818(ICMT)
MCF: 
102143064(ICMT)
CJC: 
100407809(ICMT)
MMU: 
57295(Icmt)
RNO: 
170818(Icmt)
CGE: 
100765763(Icmt)
NGI: 
103725122(Icmt)
HGL: 
101708049(Icmt)
OCU: 
100354959(ICMT)
TUP: 
102481076(ICMT)
CFA: 
489628(ICMT)
AML: 
UMR: 
103666895(ICMT)
FCA: 
101093374(ICMT)
PTG: 
102972150(ICMT)
BTA: 
785548(ICMT)
BOM: 
102284128(ICMT)
PHD: 
CHX: 
102181140(ICMT)
OAS: 
101117687(ICMT)
SSC: 
100514410(ICMT)
CFR: 
BACU: 
102998274(ICMT)
LVE: 
103075548(ICMT)
ECB: 
100059680(ICMT)
MYB: 
102243859(ICMT)
PALE: 
102888174(ICMT)
MDO: 
100026574(ICMT)
SHR: 
100922116(ICMT)
OAA: 
100082737(ICMT)
GGA: 
419373(ICMT)
APLA: 
101796351(ICMT)
TGU: 
100226385(ICMT)
FAB: 
101807717(ICMT)
PHI: 
102099231(ICMT)
FPG: 
101917928(ICMT)
FCH: 
102051478(ICMT)
CLV: 
102091468(ICMT)
ASN: 
102370476(ICMT)
AMJ: 
102558543(ICMT)
PSS: 
102445166(ICMT)
CMY: 
102930965(ICMT)
PBI: 
103060255(ICMT)
XLA: 
397717(icmt)
XTR: 
100127802(icmt)
DRE: 
550281(icmt)
TRU: 
MZE: 
OLA: 
XMA: 
CMK: 
103181416(icmt)
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
MDE: 
AGA: 
AAG: 
CQU: 
AME: 
726380(GB19279)
NVI: 
100120654(Icmt)
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CELE_F21F3.3(F21F3.3) CELE_M01E11.1(M01E11.1)
CBR: 
BMY: 
LOA: 
TSP: 
HRO: 
LGI: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
AT5G08335(ATSTE14B) AT5G23320(STE14A)
ALY: 
CRB: 
EUS: 
BRP: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
CAM: 
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
CSV: 
CMO: 
RCU: 
POP: 
POPTR_0005s09180g(POPTRDRAFT_801032) POPTR_0007s07350g(POPTRDRAFT_802771)
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os04t0602900-01(Os04g0602900)
OBR: 
BDI: 
SBI: 
SORBI_01g048060(SORBIDRAFT_01g048060)
ZMA: 
100284671(pco145633) 100285803
SITA: 
PDA: 
MUS: 
ATR: 
s00019p00236540(AMTR_s00019p00236540)
SMO: 
PPP: 
CRE: 
VCN: 
OLU: 
OTA: 
BPG: 
MIS: 
MPP: 
CSL: 
CVR: 
CME: 
CCP: 
SCE: 
YDR410C(STE14)
AGO: 
ERC: 
KLA: 
LTH: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0A12100(NCAS0A12100)
NDI: 
NDAI_0A04160(NDAI0A04160)
TPF: 
TPHA_0E02030(TPHA0E02030)
TBL: 
TBLA_0A06820(TBLA0A06820)
TDL: 
TDEL_0A03740(TDEL0A03740)
KAF: 
KAFR_0E03400(KAFR0E03400)
PPA: 
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CaO19.7766(STE141)
CTP: 
COT: 
CDU: 
CTEN: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
ELA: 
MBE: 
ANI: 
AFM: 
AOR: 
AOR_1_1448054(AO090011000860)
ANG: 
ANI_1_1694104(An12g03660)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
TMS: 
PPL: 
DSQ: 
SHS: 
PSQ: 
FME: 
GTR: 
LBC: 
MRR: 
CCI: 
SCM: 
SLA: 
PFP: 
MGL: 
PGR: 
MLR: 
WSE: 
MBR: 
DDI: 
DDB_G0272799(icmA-1) DDB_G0273995(icmA-2)
DPP: 
EHI: 
EHI_006100(83.t00023)
EDI: 
ACAN: 
PTM: 
PTI: 
TPS: 
PIF: 
EHX: 
GTT: 
TBR: 
TCR: 
LMA: 
LIF: 
LDO: 
LMI: 
LBZ: 
NGR: 
TVA: 
GLA: 
XCC: 
XCB: 
XCV: 
XOO: 
XOM: 
ABA: 
 » show all
Taxonomy
Reference
1  [PMID:3290900]
  Authors
Clarke S, Vogel JP, Deschenes RJ, Stock J.
  Title
Posttranslational modification of the Ha-ras oncogene protein: evidence for a third class of protein carboxyl methyltransferases.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 4643-7.
Reference
2  [PMID:2753892]
  Authors
Ota IM, Clarke S.
  Title
Enzymatic methylation of 23-29-kDa bovine retinal rod outer segment membrane proteins. Evidence for methyl ester formation at carboxyl-terminal cysteinyl residues.
  Journal
J. Biol. Chem. 264 (1989) 12879-84.
Reference
3  [PMID:2398053]
  Authors
Stephenson RC, Clarke S.
  Title
Identification of a C-terminal protein carboxyl methyltransferase in rat liver membranes utilizing a synthetic farnesyl cysteine-containing peptide substrate.
  Journal
J. Biol. Chem. 265 (1990) 16248-54.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
130731-20-3

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