KEGG   ENZYME: 2.5.1.58Help
Entry
EC 2.5.1.58                 Enzyme                                 

Name
protein farnesyltransferase;
FTase
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
farnesyl-diphosphate:protein-cysteine farnesyltransferase
Reaction(IUBMB)
farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate [RN:R09844]
Reaction(KEGG)
Substrate
farnesyl diphosphate [CPD:C00448];
protein-cysteine [CPD:C20119]
Product
S-farnesyl protein [CPD:C20120];
diphosphate [CPD:C00013]
Comment
This enzyme, along with protein geranylgeranyltransferase types I (EC 2.5.1.59) and II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 of an isoprenyl 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 serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, gamma-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction. A zinc metalloenzyme that requires Mg2+ for activity.
History
EC 2.5.1.58 created 2003
Pathway
ec00900  Terpenoid backbone biosynthesis
ec01130  Biosynthesis of antibiotics
Orthology
K05954  protein farnesyltransferase subunit beta
K05955  protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Genes
HSA: 2339(FNTA) 2342(FNTB)
PTR: 452971(FNTB) 472929(FNTA)
PPS: 100991890(FNTB) 103786897(FNTA)
GGO: 101147861(FNTA) 101150420(FNTB)
PON: 100436184(FNTB) 100448439(FNTA)
NLE: 100603548(FNTB) 100605797(FNTA)
MCC: 708129(FNTB) 712681(FNTA)
MCF: 101865967(FNTB) 101866500(FNTA)
CSAB: 103215701(FNTA) 103229180(FNTB)
RRO: 104668310(FNTA) 104678437(FNTB)
RBB: 108542421(FNTB)
CJC: 100392598(FNTB) 100401677(FNTA)
SBQ: 101053282(FNTB) 104649982(FNTA)
MMU: 110606(Fntb) 14272(Fnta)
RNO: 25318(Fnta) 64511(Fntb)
CGE: 100752221(Fntb) 100752295(Fnta)
NGI: 103749278(Fntb)
HGL: 101703640(Fnta) 101703774(Fntb)
CCAN: 109691132(Fntb) 109699820(Fnta)
OCU: 100341143 100343931(FNTB) 100347188(FNTA)
TUP: 102479775(FNTB) 102494685(FNTA)
CFA: 475566(FNTA) 490735(FNTB)
AML: 100467230(FNTA) 100474526
UMR: 103674342 103677044(FNTA)
ORO: 101376890(FNTA) 101383702(FNTB) 101383786
FCA: 101088759(FNTB) 101097062(FNTA)
PTG: 102957564(FNTA) 102966415(FNTB)
AJU: 106971334(FNTB) 106990022(FNTA)
BTA: 281169(FNTA) 327686(FNTB)
BOM: 102272299(FNTA) 102287965(FNTB)
BIU: 109553498(FNTA) 109565251(FNTB)
PHD: 102330315(FNTB) 102332237(FNTA)
CHX: 102189488(FNTB) 102191016(FNTA)
OAS: 100302086(FNTA) 101110335(FNTB)
SSC: 100512293(FNTB) 100627556(FNTA)
CFR: 102511020(FNTA) 102522965(FNTB)
CDK: 105086183 105094300(FNTA)
BACU: 102999003(FNTB) 103014092(FNTA)
LVE: 103074104(FNTB) 103085981(FNTA)
OOR: 101277224(FNTB) 101288631(FNTA)
ECB: 100052486(FNTB) 100053704(FNTA)
EPZ: 103541355(FNTA) 103550215(FNTB)
EAI: 106828969(FNTA) 106844888(FNTB)
MYB: 102255519(FNTA) 102261986(FNTB)
MYD: 102751880(FNTB) 102770189(FNTA)
HAI: 109382065 109386282(FNTA)
RSS: 109442237 109448276(FNTB) 109452851(FNTA)
PALE: 102881721(FNTB) 102890666(FNTA)
LAV: 100655632(FNTB) 100669104(FNTA)
MDO: 100027938(FNTB) 100617990(FNTA)
SHR: 100916157(FNTB) 100924354(FNTA)
OAA: 100078580(FNTA)
GGA: 100857683(FNTB) 427299(FNTA)
MGP: 100544213(FNTA) 100548337
APLA: 101793836(FNTA)
ACYG: 106040419(FNTA)
TGU: 100222812(FNTA) 100223864
GFR: 102031891(FNTA) 102043195(FNTB)
FAB: 101810421(FNTB) 101814503(FNTA)
PHI: 102102894(FNTB) 102111175(FNTA)
PMAJ: 107198168(FNTA) 107205595
CCAE: 111940897(FNTA) 111945042
CCW: 104689741(FNTA) 104693013
FPG: 101913248(FNTA) 101920206(FNTB)
FCH: 102046284(FNTA) 102052180 102059349(FNTB)
EGZ: 104126429(FNTA)
ASN: 102382443(FNTA) 102385137
AMJ: 102564152(FNTA) 102574457(FNTB)
PSS: 102452430(FNTA) 102459340
CMY: 102937672(FNTB) 102940529
CPIC: 101934158(FNTA) 101938834(FNTB)
ACS: 100559827 100561851(fnta)
PVT: 110083168(FNTA) 110085642
PBI: 103049019 103051193(FNTA)
GJA: 107120943(FNTA) 107121947
XLA: 100137632(fnta.S) 108699724(fntb.S) 447605(fntb.L)
XTR: 100144648(fnta) 550012(fntb)
NPR: 108796770 108804918(FNTA)
DRE: 323500(fntb) 555882(fnta)
IPU: 108257588 108268629(fnta)
AMEX: 103026998(fnta) 103033540
TRU: 101076206(fnta) 101079983
NCC: 104942305(fnta) 104949856
MZE: 101468735(fnta) 101479885
OLA: 101160126 101160920(fnta)
XMA: 102234643(fnta) 102235994
PRET: 103457641 103471041(fnta)
NFU: 107377823 107381432(fnta)
KMR: 108228747(fnta) 108233508
CSEM: 103381205 103391301(fnta)
LCF: 108878782(fnta) 108887265
SDU: 111216443 111226657(fnta)
HCQ: 109515791(fnta) 109523733
BPEC: 110159349 110166430(fnta)
MALB: 109957583(fnta) 109962295
ELS: 105006791(fnta) 105024336
SFM: 108919508 108938728(fnta)
LCM: 102349666(FNTA) 102350945(FNTB)
CMK: 103175221 103191504(fnta)
CIN: 445680(fta)
DME: Dmel_CG17565(CG17565) Dmel_CG2976(Fnta)
DSI: Dsimw501_GD19096(Dsim_GD19096) Dsimw501_GD22689(Dsim_GD22689)
NVI: 100123894
BMOR: 692501(Fnta) 692537(Fntb)
API: 100166879 100167417(Fnta)
CEL: CELE_F23B12.6(fntb-1) CELE_R02D3.5(fnta-1)
CBR: CBG01666 CBG04611(Cbr-tag-114)
ADF: 107335525
ATH: AT3G59380(FTA) AT5G40280(ERA1)
GMX: 100306703(GMERA1B) 100790130 100811502 100814543(GMERA1A)
LJA: Lj0g3v0089459.1(Lj0g3v0089459.1) Lj2g3v1014160.1(Lj2g3v1014160.1)
SLY: 544036(FTA) 544037(FTB)
NTA: 107777651 107798306 107814428(Ntalpha) 107827532(NtbetaF)
DOSA: Os09t0514400-01(Os09g0514400)
ATS: 109744376(LOC109744376) 109773598(LOC109773598) 109778677(LOC109778677)
ZMA: 100272584(pco074498b) 100273635
SCE: YDL090C(RAM1) YKL019W(RAM2)
KMX: KLMA_20389(RAM1) KLMA_60145(RAM2)
NCS: NCAS_0B05820(NCAS0B05820) NCAS_0H03470(NCAS0H03470)
NDI: NDAI_0B03130(NDAI0B03130) NDAI_0C00210(NDAI0C00210)
TPF: TPHA_0C03780(TPHA0C03780) TPHA_0N01840(TPHA0N01840)
TBL: TBLA_0A00700(TBLA0A00700) TBLA_0B09490(TBLA0B09490)
TDL: TDEL_0B07560(TDEL0B07560) TDEL_0G02960(TDEL0G02960)
KAF: KAFR_0A06950(KAFR0A06950) KAFR_0C03850(KAFR0C03850)
PIC: PICST_55783(RAM2) PICST_82404(RAM1)
SLB: AWJ20_185(RAM2) AWJ20_887(RAM1)
NTE: NEUTE1DRAFT144524(NEUTE1DRAFT_144524) NEUTE1DRAFT88206(NEUTE1DRAFT_88206)
ANG: ANI_1_1988184(An04g06620) ANI_1_462184(An04g02210)
CIM: CIMG_05727 CIMG_12864(CIMG00563)
PBL: PAAG_07086 PAAG_11163(PAAG_00717) PAAG_11164
SPO: SPAC17G6.04c(cpp1) SPAPB1A10.04c(cwp1)
ABP: AGABI1DRAFT115274(AGABI1DRAFT_115274) AGABI1DRAFT61805(AGABI1DRAFT_61805)
ABV: AGABI2DRAFT194236(AGABI2DRAFT_194236) AGABI2DRAFT210804(AGABI2DRAFT_210804)
DDI: DDB_G0270948(fntB) DDB_G0283053(fntA)
DFA: DFA_05584(fntA) DFA_10414(fntB)
EHI: EHI_006190(83.t00031) EHI_074760(288.t00007)
PYO: PY17X_0903000(PY02409)
TPV: TP02_0810
BBO: BBOV_III002550(17.m07246) BBOV_III004550(17.m07408)
CPV: cgd6_2510
SMIN: v1.2.028464.t1(symbB.v1.2.028464.t1)
 » show all
Taxonomy
Reference
1  [PMID:7756316]
  Authors
Furfine ES, Leban JJ, Landavazo A, Moomaw JF, Casey PJ.
  Title
Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release.
  Journal
Biochemistry 34:6857-62 (1995)
Reference
2  [PMID:8621375]
  Authors
Casey PJ, Seabra MC.
  Title
Protein prenyltransferases.
  Journal
J Biol Chem 271:5289-92 (1996)
DOI:10.1074/jbc.271.10.5289
Reference
3  [PMID:9657673]
  Authors
Long SB, Casey PJ, Beese LS.
  Title
Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate.
  Journal
Biochemistry 37:9612-8 (1998)
DOI:10.1021/bi980708e
  Sequence
[rno:25318 64511]
Reference
4  [PMID:11591144]
  Authors
Micali E, Chehade KA, Isaacs RJ, Andres DA, Spielmann HP.
  Title
Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups.
  Journal
Biochemistry 40:12254-65 (2001)
DOI:10.1021/bi011133f
Reference
5  [PMID:12374986]
  Authors
Long SB, Casey PJ, Beese LS.
  Title
Reaction path of protein farnesyltransferase at atomic resolution.
  Journal
Nature 419:645-50 (2002)
DOI:10.1038/nature00986
  Sequence
[rno:25318 64511]
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: 2.5.1.58
IUBMB Enzyme Nomenclature: 2.5.1.58
ExPASy - ENZYME nomenclature database: 2.5.1.58
BRENDA, the Enzyme Database: 2.5.1.58
CAS: 131384-38-8

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