KEGG   ENZYME: 2.5.1.59Help
Entry
EC 2.5.1.59                 Enzyme                                 

Name
protein geranylgeranyltransferase type I;
GGTase-I;
GGTaseI
Class
Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
BRITE hierarchy
Sysname
geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
Reaction(IUBMB)
geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Substrate
geranylgeranyl diphosphate [CPD:C00353];
protein-cysteine [CPD:C20119]
Product
S-geranylgeranyl-protein;
diphosphate [CPD:C00013]
Comment
This enzyme, along with protein farnesyltransferase (EC 2.5.1.58) and protein geranylgeranyltransferase type II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 atom of the geranylgeranyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Known targets of this enzyme include most gamma-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. A zinc metalloenzyme. The Zn2+ is required for peptide, but not for isoprenoid, substrate binding.
History
EC 2.5.1.59 created 2003
Orthology
K05955  
protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
K11713  
geranylgeranyl transferase type-1 subunit beta
Genes
HSA: 
2339(FNTA) 5229(PGGT1B)
PTR: 
471600(PGGT1B) 472929(FNTA)
PPS: 
100989189(PGGT1B)
GGO: 
101146731(PGGT1B) 101147861(FNTA)
PON: 
100436505(PGGT1B) 100448439(FNTA)
MCC: 
MCF: 
MMU: 
14272(Fnta) 225467(Pggt1b)
RNO: 
25318(Fnta) 81746(Pggt1b)
CGE: 
100752295(Fnta) 100759155(Pggt1b)
HGL: 
101703640(Fnta) 101723510(Pggt1b)
TUP: 
102483233(PGGT1B) 102494685(FNTA)
CFA: 
475566(FNTA) 481440(PGGT1B)
AML: 
FCA: 
101089829(PGGT1B) 101097062(FNTA)
PTG: 
102951684(PGGT1B) 102957564(FNTA)
BTA: 
281169(FNTA) 509322(PGGT1B)
BOM: 
102271879(PGGT1B) 102272299(FNTA)
PHD: 
102324598(PGGT1B) 102332237(FNTA)
CHX: 
102183603(PGGT1B) 102191016(FNTA)
OAS: 
100302086(FNTA) 101123045(PGGT1B)
SSC: 
CFR: 
102511020(FNTA) 102511063(PGGT1B)
BACU: 
103004097(PGGT1B) 103014092(FNTA)
LVE: 
103085770(PGGT1B) 103085981(FNTA)
ECB: 
100053704(FNTA) 100064254(PGGT1B)
MYB: 
102242187(PGGT1B) 102255519(FNTA)
MYD: 
102770189(FNTA) 102773769(PGGT1B)
PALE: 
102883059(PGGT1B) 102890666(FNTA)
MDO: 
100016343(PGGT1B) 100617990(FNTA)
SHR: 
100924354(FNTA) 100928606(PGGT1B)
OAA: 
100076094(PGGT1B) 100078580(FNTA)
GGA: 
427299(FNTA) 770633(PGGT1B)
MGP: 
TGU: 
FAB: 
101807115(PGGT1B)
PHI: 
APLA: 
101792505(PGGT1B) 101793836(FNTA)
FPG: 
101913248(FNTA) 101914299(PGGT1B)
FCH: 
CLV: 
102094236(PGGT1B) 102098098(FNTA)
ASN: 
102378457(PGGT1B) 102382443(FNTA)
AMJ: 
PSS: 
102445929(PGGT1B) 102452430(FNTA)
CMY: 
ACS: 
PBI: 
XLA: 
100137632(fnta) 734580(pggt1b)
XTR: 
100144648(fnta) 493499(pggt1b)
DRE: 
555882(fnta) 570808(pggt1b)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102349666(FNTA) 102359482(PGGT1B)
CMK: 
103181137(pggt1b) 103191504(fnta)
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
412933(betaggt-I) 551732(GB10315)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CELE_R02D3.5(fnta-1) CELE_Y48E1B.3(Y48E1B.3)
CBR: 
BMY: 
LOA: 
TSP: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
AT2G39550(PGGT-I) AT3G59380(FTA)
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
MTR: 
CAM: 
FVE: 
PPER: 
CSV: 
RCU: 
POP: 
POPTR_0007s02070g(POPTRDRAFT_562248) POPTR_0008s05460g(POPTRDRAFT_832541) POPTR_0010s21300g
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os01t0150100-01(Os01g0150100) Os09t0514400-01(Os09g0514400)
OBR: 
BDI: 
SBI: 
SORBI_02g029780(SORBIDRAFT_02g029780) SORBI_03g006060(SORBIDRAFT_03g006060)
ZMA: 
SITA: 
ATR: 
s00012p00169450(AMTR_s00012p00169450) s00066p00082970(AMTR_s00066p00082970)
SMO: 
PPP: 
CRE: 
VCN: 
MIS: 
MPP: 
CSL: 
CVR: 
CME: 
GSL: 
CCP: 
SCE: 
YGL155W(CDC43) YKL019W(RAM2)
AGO: 
ERC: 
KLA: 
LTH: 
PPA: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0D00730(NCAS0D00730) NCAS_0H03470(NCAS0H03470)
NDI: 
NDAI_0C00210(NDAI0C00210) NDAI_0H03430(NDAI0H03430)
TPF: 
TPHA_0G00890(TPHA0G00890) TPHA_0N01840(TPHA0N01840)
TBL: 
TBLA_0A00700(TBLA0A00700) TBLA_0B06120(TBLA0B06120)
TDL: 
TDEL_0B07560(TDEL0B07560) TDEL_0G02420(TDEL0G02420)
KAF: 
KAFR_0B04650(KAFR0B04650) KAFR_0C03850(KAFR0C03850)
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CaO19.12280(RAM2) CaO19.1803(CDC43) CaO19.4817(RAM2)
CTP: 
COT: 
CDU: 
CTEN: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
ELA: 
SSL: 
BFU: 
MBE: 
ANI: 
AFM: 
AOR: 
AOR_1_1370144(AO090023000791)
ANG: 
ANI_1_462184(An04g02210)
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: 
DSQ: 
SHS: 
PCO: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MPR: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT100190(AGABI1DRAFT_100190) AGABI1DRAFT115274(AGABI1DRAFT_115274)
ABV: 
AGABI2DRAFT194236(AGABI2DRAFT_194236) AGABI2DRAFT72409(AGABI2DRAFT_72409)
CPUT: 
SLA: 
UMA: 
PFP: 
MGL: 
PGR: 
MLR: 
WSE: 
MBR: 
DDI: 
DPP: 
DFA: 
EHI: 
EHI_074760(288.t00007) EHI_077230(40.t00014)
EDI: 
ACAN: 
TAN: 
BBO: 
BBOV_III002550(17.m07246)
BEQ: 
CPV: 
CHO: 
TET: 
PTM: 
PTI: 
TPS: 
PIF: 
NGD: 
EHX: 
GTT: 
TBR: 
Tb927.3.4490(Tb03.26J7.830)
TCR: 
LMA: 
LIF: 
LDO: 
LMI: 
LBZ: 
NGR: 
TVA: 
GLA: 
 » show all
Taxonomy
Reference
1  [PMID:8621375]
  Authors
Casey PJ, Seabra MC.
  Title
Protein prenyltransferases.
  Journal
J. Biol. Chem. 271 (1996) 5289-92.
  Organism
Homo sapiens, Rattus norvegicus, Saccharomyces cerevisiae
Reference
2  [PMID:9003382]
  Authors
Zhang FL, Casey PJ.
  Title
Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I.
  Journal
Biochem. J. 320 ( Pt 3) (1996) 925-32.
  Organism
Homo sapiens, Rattus norvegicus
Reference
3
  Authors
Gibbs, R.A.
  Title
Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis.
  Journal
In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A Mechanistic Reference, vol. 1, Academic Press, San Diego, CA, 1998, p. 31-118.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
135371-29-8

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