KEGG   ENZYME: 2.5.1.60Help
Entry
EC 2.5.1.60                 Enzyme                                 

Name
protein geranylgeranyltransferase type II;
GGTaseII;
Rab geranylgeranyltransferase;
RabGGTase;
geranylgeranyl-diphosphate,geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
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 I (EC 2.5.1.59), constitutes the protein prenyltransferase family of enzymes. Attaches geranylgeranyl groups to two C-terminal cysteines in Ras-related GTPases of a single family, the Rab family (Ypt/Sec4 in lower eukaryotes) that terminate in XXCC, XCXC and CCXX motifs. Reaction is entirely dependent on the Rab substrate being bound to Rab escort protein (REP). Post-translational modification with the geranylgeranyl moiety is essential for Rab GTPases to be able to control the processes of membrane docking and fusion [5].
History
EC 2.5.1.60 created 2003
Orthology
K05956  
geranylgeranyl transferase type-2 subunit beta
K14050  
geranylgeranyl transferase type-2 subunit alpha
Genes
HSA: 
5875(RABGGTA) 5876(RABGGTB)
PTR: 
100614714(RABGGTB) 452815(RABGGTA)
PPS: 
100978858(RABGGTA) 100987085(RABGGTB)
GGO: 
101140684(RABGGTB) 101152486(RABGGTA)
PON: 
100174130(RABGGTA) 100440764(RABGGTB)
MCC: 
705421(RABGGTB) 714521
MCF: 
102119899(RABGGTA) 102126317(RABGGTB)
MMU: 
19352(Rabggtb) 56187(Rabggta)
RNO: 
25533(Rabggtb) 58983(Rabggta)
CGE: 
100757505(Rabggta) 100762868(Rabggtb)
HGL: 
101709927(Rabggtb) 101722509(Rabggta)
TUP: 
102474188(RABGGTB) 102501477(RABGGTA)
CFA: 
608407(RABGGTA) 612683(RABGGTB)
AML: 
FCA: 
101082319(RABGGTA) 101090281(RABGGTB)
PTG: 
102962034(RABGGTB) 102963179(RABGGTA)
BTA: 
516619(RABGGTA) 533276(RABGGTB)
BOM: 
102264837(RABGGTA) 102288371(RABGGTB)
PHD: 
102338947(RABGGTB) 102339491(RABGGTA) 102343581
CHX: 
102183383(RABGGTB) 102187051(RABGGTA)
SSC: 
100049679(RABGGTA) 733698
CFR: 
102505171(RABGGTB) 102523014(RABGGTA)
BACU: 
102998347(RABGGTA) 103019854(RABGGTB)
LVE: 
103078134(RABGGTB) 103078888(RABGGTA)
ECB: 
100051161(RABGGTA) 100067295(RABGGTB)
MYB: 
102250484(RABGGTA) 102252699(RABGGTB)
MYD: 
102752362(RABGGTA) 102758789(RABGGTB)
PALE: 
102891613(RABGGTA) 102893188(RABGGTB)
MDO: 
100030822(RABGGTA) 100616945(RABGGTB)
SHR: 
100915544(RABGGTA) 100927615(RABGGTB)
OAA: 
GGA: 
424723(RABGGTB)
MGP: 
TGU: 
100220901(RABGGTB)
FAB: 
PHI: 
APLA: 
101796884(RABGGTB)
FPG: 
101919112(RABGGTB)
FCH: 
102055652(RABGGTB)
CLV: 
ASN: 
102374627(RABGGTA) 102384192(RABGGTB)
AMJ: 
102575873(RABGGTB) 102576818(RABGGTA)
PSS: 
102463096(RABGGTB)
CMY: 
102944402(RABGGTA) 102944974(RABGGTB)
ACS: 
PBI: 
XLA: 
446590(rabggta) 734339(rabggtb)
XTR: 
100127877(rabggtb) 448385(rabggta)
DRE: 
406386(rabggtb) 767725(rabggta)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102354536(RABGGTB) 102355599(RABGGTA)
CMK: 
103174735(rabggtb)
BFO: 
CIN: 
SPU: 
100887959 588843(rabggtb)
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
726822(betaggt-II) 726983
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CELE_B0280.1(ggtb-1) CELE_M57.2(M57.2)
CBR: 
BMY: 
LOA: 
TSP: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
AT3G12070(RGTB2) AT4G24490(RGTA1) AT5G12210(RGTB1)
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
MTR: 
CAM: 
FVE: 
PPER: 
CSV: 
RCU: 
POP: 
POPTR_0006s24150g(POPTRDRAFT_561627) POPTR_0013s01400g(POPTRDRAFT_806754)
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os03t0193700-00(Os03g0193700) Os06t0677500-01(Os06g0677500) Os08t0512300-01(Os08g0512300) Os11t0523500-00(Os11g0523500)
OBR: 
BDI: 
SBI: 
SORBI_07g027520(SORBIDRAFT_07g027520) SORBI_10g027180(SORBIDRAFT_10g027180)
ZMA: 
SITA: 
ATR: 
s00033p00228890(AMTR_s00033p00228890) s00050p00182520(AMTR_s00050p00182520)
SMO: 
PPP: 
CRE: 
VCN: 
OLU: 
BPG: 
MIS: 
MPP: 
CSL: 
CVR: 
CME: 
GSL: 
CCP: 
SCE: 
YJL031C(BET4) YPR176C(BET2)
AGO: 
ERC: 
KLA: 
LTH: 
PPA: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0A15160(NCAS0A15160) NCAS_0F02080(NCAS0F02080)
NDI: 
NDAI_0C03710(NDAI0C03710) NDAI_0J00320(NDAI0J00320)
TPF: 
TPHA_0I03230(TPHA0I03230) TPHA_0N00960(TPHA0N00960)
TBL: 
TBLA_0D03430(TBLA0D03430) TBLA_0E00790(TBLA0E00790)
TDL: 
TDEL_0E03830(TDEL0E03830) TDEL_0H00380(TDEL0H00380)
KAF: 
KAFR_0B00380(KAFR0B00380) KAFR_0J01090(KAFR0J01090)
DHA: 
PIC: 
PICST_32799(BET4) PICST_37880(BET2.2)
PGU: 
SPAA: 
LEL: 
CAL: 
CaO19.1039(BET4) CaO19.7563(BET2) CaO19.8641(BET4)
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_2054154(AO090003001153) AOR_1_248174(AO090005000132)
ANG: 
ANI_1_148114(An13g01040) ANI_1_1942184(An04g06090)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
ZTR: 
PFJ: 
BCOM: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
PPL: 
LBC: 
MPR: 
CCI: 
SCM: 
UMA: 
MGL: 
PGR: 
ECU: 
EIN: 
EHE: 
NCE: 
MBR: 
DDI: 
DDB_G0269570(rabggta) DDB_G0290671(rabggtb)
DPP: 
DFA: 
DFA_00234(rabggta) DFA_05375(rabggtb)
EHI: 
EHI_023180(25.t00001) EHI_025110(505.t00003)
EDI: 
ACAN: 
PFA: 
PFD: 
PFH: 
PYO: 
PCB: 
PBE: 
PKN: 
PVX: 
PCY: 
TAN: 
TPV: 
BBO: 
BBOV_I004600(19.m02085) BBOV_III009610(17.m07834) BBOV_IV001440(21.m02925)
BEQ: 
CPV: 
CHO: 
TGO: 
TET: 
PTM: 
PTI: 
TPS: 
PIF: 
NGD: 
EHX: 
GTT: 
TBR: 
Tb927.4.690(Tb04.5E12.1040)
TCR: 
LMA: 
LIF: 
LDO: 
LMI: 
LBZ: 
NGR: 
TVA: 
GLA: 
RBA: 
PSL: 
PLM: 
PBS: 
CMR: 
 » 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:9677305]
  Authors
Wilson AL, Erdman RA, Castellano F, Maltese WA.
  Title
Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases.
  Journal
Biochem. J. 333 ( Pt 3) (1998) 497-504.
  Organism
Homo sapiens
Reference
3  [PMID:10745007]
  Authors
Zhang H, Seabra MC, Deisenhofer J.
  Title
Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution.
  Journal
Structure. Fold. Des. 8 (2000) 241-51.
  Organism
Rattus norvegicus
  Sequence
[rno:58983 25533]
Reference
4  [PMID:11591706]
  Authors
Thoma NH, Niculae A, Goody RS, Alexandrov K.
  Title
Double prenylation by RabGGTase can proceed without dissociation of the mono-prenylated intermediate.
  Journal
J. Biol. Chem. 276 (2001) 48631-6.
  Organism
Rattus norvegicus
Reference
5  [PMID:12071695]
  Authors
Rak A, Niculae A, Kalinin A, Thoma NH, Sidorovitch V, Goody RS, Alexandrov K.
  Title
In vitro assembly, purification, and crystallization of the rab geranylgeranyl transferase:substrate complex.
  Journal
Protein. Expr. Purif. 25 (2002) 23-30.
  Organism
Homo sapiens
Reference
6
  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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