FNTA_CANAX
ID FNTA_CANAX Reviewed; 306 AA.
AC Q9Y765;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha;
DE EC=2.5.1.58;
DE EC=2.5.1.59;
DE AltName: Full=CAAX farnesyltransferase subunit alpha;
DE AltName: Full=FTase-alpha;
DE AltName: Full=Ras proteins prenyltransferase subunit alpha;
DE AltName: Full=Type I protein geranyl-geranyltransferase subunit alpha;
DE Short=GGTase-I-alpha;
GN Name=RAM2;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10376828; DOI=10.1099/13500872-145-5-1123;
RA Mazur P., Register E., Bonfiglio C.A., Yuan X., Kurtz M.B.,
RA Williamson J.M., Kelly R.;
RT "Purification of geranylgeranyltransferase I from Candida albicans and
RT cloning of the CaRAM2 and CaCDC43 genes encoding its subunits.";
RL Microbiology 145:1123-1135(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT, AND
RP SUBUNIT.
RX PubMed=18713740; DOI=10.1074/jbc.m805330200;
RA Hast M.A., Beese L.S.;
RT "Structure of protein geranylgeranyltransferase-I from the human pathogen
RT Candida albicans complexed with a lipid substrate.";
RL J. Biol. Chem. 283:31933-31940(2008).
CC -!- FUNCTION: Essential subunit of both the farnesyltransferase and the
CC geranylgeranyltransferase complex. Contributes to the transfer of a
CC farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl
CC diphosphate to a cysteine at the fourth position from the C-terminus of
CC several proteins having the C-terminal sequence Cys-aliphatic-
CC aliphatic-X.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019,
CC ChEBI:CHEBI:175763; EC=2.5.1.58;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-geranylgeranyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC ChEBI:CHEBI:86021; EC=2.5.1.59;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P29703};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC {ECO:0000269|PubMed:18713740}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000305}.
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DR EMBL; AF110691; AAD32540.1; -; Genomic_DNA.
DR PDB; 3DRA; X-ray; 1.80 A; A=1-306.
DR PDB; 4YDO; X-ray; 3.00 A; A=1-305.
DR PDBsum; 3DRA; -.
DR PDBsum; 4YDO; -.
DR AlphaFoldDB; Q9Y765; -.
DR SMR; Q9Y765; -.
DR CGD; CAL0000180742; RAM2.
DR VEuPathDB; FungiDB:C1_09530W_A; -.
DR VEuPathDB; FungiDB:CAWG_00476; -.
DR PhylomeDB; Q9Y765; -.
DR BRENDA; 2.5.1.58; 1096.
DR BRENDA; 2.5.1.59; 1096.
DR EvolutionaryTrace; Q9Y765; -.
DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB.
DR GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; IDA:CGD.
DR GO; GO:0004660; F:protein farnesyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004661; F:protein geranylgeranyltransferase activity; ISS:UniProtKB.
DR GO; GO:0007323; P:peptide pheromone maturation; IEA:EnsemblFungi.
DR GO; GO:0018343; P:protein farnesylation; ISS:UniProtKB.
DR GO; GO:0018344; P:protein geranylgeranylation; IDA:CGD.
DR InterPro; IPR002088; Prenyl_trans_a.
DR Pfam; PF01239; PPTA; 4.
DR PROSITE; PS51147; PFTA; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Prenyltransferase; Repeat; Transferase.
FT CHAIN 1..306
FT /note="Protein
FT farnesyltransferase/geranylgeranyltransferase type-1
FT subunit alpha"
FT /id="PRO_0000119752"
FT REPEAT 48..82
FT /note="PFTA 1"
FT REPEAT 84..118
FT /note="PFTA 2"
FT REPEAT 125..159
FT /note="PFTA 3"
FT REPEAT 161..195
FT /note="PFTA 4"
FT REPEAT 201..235
FT /note="PFTA 5"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:4YDO"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:3DRA"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 199..215
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:3DRA"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:4YDO"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:3DRA"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 258..270
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:3DRA"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:3DRA"
SQ SEQUENCE 306 AA; 36601 MW; BC42924AC96DD920 CRC64;
MTDSKYDYSD ITPVDINTEE PQICQILYDE DYKQIMGLLL ALMKAEEYSE RALHITELGI
NELASHYTIW IYRFNILKNL PNRNLYDELD WCEEIALDNE KNYQIWNYRQ LIIGQIMELN
NNDFDPYREF PILEAMLSSD PKNHHVWSYR KWLVDTFDLH NDAKELSFVD KVIDTDLKNN
SAWSHRFFLL FSKKHLATDN TIDEELNYVK DKIVKCPQNP STWNYLLGIH ERFDRSITQL
EEFSLQFVDL EKDQVTSSFA LETLAKIYTQ QKKYNESRTV YDLLKSKYDP IRSNFWDYQI
SKLTSV
