PGTB1_ARATH
ID PGTB1_ARATH Reviewed; 375 AA.
AC O80642; Q9FPP6;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Geranylgeranyl transferase type-1 subunit beta;
DE EC=2.5.1.59;
DE AltName: Full=Geranylgeranyl transferase type I subunit beta;
DE Short=AtGGT-IB;
DE Short=GGTase-I-beta;
GN Name=GGB; Synonyms=PGGT1B, PGGTI; OrderedLocusNames=At2g39550;
GN ORFNames=F12L6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RX PubMed=11500541; DOI=10.1104/pp.126.4.1416;
RA Caldelari D., Sternberg H., Rodriguez-Concepcion M., Gruissem W.,
RA Yalovsky S.;
RT "Efficient prenylation by a plant geranylgeranyltransferase-I requires a
RT functional CaaL box motif and a proximal polybasic domain.";
RL Plant Physiol. 126:1416-1429(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=16183844; DOI=10.1104/pp.105.065045;
RA Johnson C.D., Chary S.N., Chernoff E.A., Zeng Q., Running M.P.,
RA Crowell D.N.;
RT "Protein geranylgeranyltransferase I is involved in specific aspects of
RT abscisic acid and auxin signaling in Arabidopsis.";
RL Plant Physiol. 139:722-733(2005).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20565889; DOI=10.1186/1471-2229-10-118;
RA Andrews M., Huizinga D.H., Crowell D.N.;
RT "The CaaX specificities of Arabidopsis protein prenyltransferases explain
RT era1 and ggb phenotypes.";
RL BMC Plant Biol. 10:118-118(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC geranyl-geranyl pyrophosphate to a cysteine at the fourth position from
CC the C-terminus of proteins having the C-terminal sequence Cys-
CC aliphatic-aliphatic-X (CaaX). Seems to exclusively prenylate CaaX
CC substrates with leucine in the terminal position. The beta subunit is
CC responsible for peptide-binding. May negatively regulate abscisic acid
CC (ABA) signaling in guard cells and auxin-induced lateral root
CC initiation.
CC -!- FUNCTION: Negatively regulates ABA signaling in guard cells. in
CC negative regulation of auxin-induced lateral root initiation.
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=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P53610};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P53610};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P18898};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.8 uM for CVIM substrate {ECO:0000269|PubMed:11500541,
CC ECO:0000269|PubMed:20565889};
CC KM=3.5 uM for CVIQ substrate {ECO:0000269|PubMed:11500541,
CC ECO:0000269|PubMed:20565889};
CC KM=19.0 uM for CVII substrate {ECO:0000269|PubMed:11500541,
CC ECO:0000269|PubMed:20565889};
CC KM=17.2 uM for CVIL substrate {ECO:0000269|PubMed:11500541,
CC ECO:0000269|PubMed:20565889};
CC Note=kcat is 0.5 h(-1), 0.08 h(-1), 0.008 h(-1) and 0.012 h(-1) for
CC CVIL, CVII, CVIQ and CVIM substrates, respectively.;
CC pH dependence:
CC Optimum pH is 7.9-8.5 for CTIL substrate.
CC {ECO:0000269|PubMed:11500541, ECO:0000269|PubMed:20565889};
CC Temperature dependence:
CC Optimum temperature is 30-37 degrees Celsius for CTIL substrate.
CC {ECO:0000269|PubMed:11500541, ECO:0000269|PubMed:20565889};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:11500541}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have an enhanced response to abscisic
CC acid (ABA)-mediated stomatal closure and increased lateral root
CC formation in response to exogenous auxin.
CC {ECO:0000269|PubMed:16183844}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG40865.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF311225; AAG40865.1; ALT_FRAME; mRNA.
DR EMBL; AC004218; AAC27846.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09693.1; -; Genomic_DNA.
DR EMBL; BT002465; AAO00825.1; -; mRNA.
DR EMBL; BT008464; AAP37823.1; -; mRNA.
DR PIR; T00565; T00565.
DR RefSeq; NP_181487.1; NM_129513.4.
DR AlphaFoldDB; O80642; -.
DR SMR; O80642; -.
DR BioGRID; 3878; 5.
DR STRING; 3702.AT2G39550.1; -.
DR iPTMnet; O80642; -.
DR PaxDb; O80642; -.
DR PRIDE; O80642; -.
DR ProteomicsDB; 235010; -.
DR EnsemblPlants; AT2G39550.1; AT2G39550.1; AT2G39550.
DR GeneID; 818540; -.
DR Gramene; AT2G39550.1; AT2G39550.1; AT2G39550.
DR KEGG; ath:AT2G39550; -.
DR Araport; AT2G39550; -.
DR TAIR; locus:2039752; AT2G39550.
DR eggNOG; KOG0367; Eukaryota.
DR HOGENOM; CLU_028946_2_2_1; -.
DR InParanoid; O80642; -.
DR OMA; RWCLMRQ; -.
DR OrthoDB; 1042804at2759; -.
DR PhylomeDB; O80642; -.
DR BioCyc; ARA:AT2G39550-MON; -.
DR BioCyc; MetaCyc:AT2G39550-MON; -.
DR PRO; PR:O80642; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80642; baseline and differential.
DR Genevisible; O80642; AT.
DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; IBA:GO_Central.
DR GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; IMP:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; TAS:TAIR.
DR GO; GO:0018344; P:protein geranylgeranylation; IMP:TAIR.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR CDD; cd02895; GGTase-I; 1.
DR InterPro; IPR041960; GGTase_I_beta.
DR InterPro; IPR001330; PFTB_repeat.
DR InterPro; IPR045089; PGGT1B-like.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774; PTHR11774; 1.
DR Pfam; PF00432; Prenyltrans; 5.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 1: Evidence at protein level;
KW Acetylation; Magnesium; Metal-binding; Prenyltransferase;
KW Reference proteome; Repeat; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..375
FT /note="Geranylgeranyl transferase type-1 subunit beta"
FT /id="PRO_0000422982"
FT REPEAT 157..199
FT /note="PFTB 1"
FT /evidence="ECO:0000255"
FT REPEAT 206..247
FT /note="PFTB 2"
FT /evidence="ECO:0000255"
FT REPEAT 265..306
FT /note="PFTB 3"
FT /evidence="ECO:0000255"
FT REPEAT 313..354
FT /note="PFTB 4"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 232..234
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 285..288
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 294..297
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 85
FT /note="D -> Y (in Ref. 1; AAG40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="L -> S (in Ref. 1; AAG40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="L -> F (in Ref. 1; AAG40865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 41472 MW; 4D7919F3F3A695DF CRC64;
MSETAVSIDS DRSKSEEEDE EEYSPPVQSS PSANFEKDRH LMYLEMMYEL LPYHYQSQEI
NRLTLAHFII SGLHFLGARD RVDKDVVAKW VLSFQAFPTN RVSLKDGEFY GFFGSRSSQF
PIDENGDLKH NGSHLASTYC ALAILKVIGH DLSTIDSKSL LISMINLQQD DGSFMPIHIG
GETDLRFVYC AAAICYMLDS WSGMDKESAK NYILNCQSYD GGFGLIPGSE SHGGATYCAI
ASLRLMGYIG VDLLSNDSSS SIIDPSLLLN WCLQRQANDG GFQGRTNKPS DTCYAFWIGA
VLKLIGGDAL IDKMALRKFL MSCQSKYGGF SKFPGQLPDL YHSYYGYTAF SLLEEQGLSP
LCPELGLPLL AAPGI
