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Geranylgeranyl transferase type-1 subunit beta (EC 2.5.1.59) (Geranylgeranyl transferase type I subunit beta) (AtGGT-IB) (GGTase-I-beta)

 PGT1_ARATH              Reviewed;         375 AA.
O80642; Q9FPP6;
24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 107.
RecName: Full=Geranylgeranyl transferase type-1 subunit beta;
EC=2.5.1.59;
AltName: Full=Geranylgeranyl transferase type I subunit beta;
Short=AtGGT-IB;
Short=GGTase-I-beta;
Name=GGB; Synonyms=PGGT1B, PGGTI; OrderedLocusNames=At2g39550;
ORFNames=F12L6;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
AND TISSUE SPECIFICITY.
PubMed=11500541; DOI=10.1104/pp.126.4.1416;
Caldelari D., Sternberg H., Rodriguez-Concepcion M., Gruissem W.,
Yalovsky S.;
"Efficient prenylation by a plant geranylgeranyltransferase-I requires
a functional CaaL box motif and a proximal polybasic domain.";
Plant Physiol. 126:1416-1429(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia, and cv. Wassilewskija;
PubMed=16183844; DOI=10.1104/pp.105.065045;
Johnson C.D., Chary S.N., Chernoff E.A., Zeng Q., Running M.P.,
Crowell D.N.;
"Protein geranylgeranyltransferase I is involved in specific aspects
of abscisic acid and auxin signaling in Arabidopsis.";
Plant Physiol. 139:722-733(2005).
[6]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=20565889; DOI=10.1186/1471-2229-10-118;
Andrews M., Huizinga D.H., Crowell D.N.;
"The CaaX specificities of Arabidopsis protein prenyltransferases
explain era1 and ggb phenotypes.";
BMC Plant Biol. 10:118-118(2010).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
geranyl-geranyl pyrophosphate to a cysteine at the fourth position
from the C-terminus of proteins having the C-terminal sequence
Cys-aliphatic-aliphatic-X (CaaX). Seems to exclusively prenylate
CaaX substrates with leucine in the terminal position. The beta
subunit is responsible for peptide-binding. May negatively
regulate abscisic acid (ABA) signaling in guard cells and auxin-
induced lateral root initiation.
-!- FUNCTION: Negatively regulates ABA signaling in guard cells. in
negative regulation of auxin-induced lateral root initiation.
-!- CATALYTIC ACTIVITY: Geranylgeranyl diphosphate + protein-cysteine
= S-geranylgeranyl-protein + diphosphate.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5.8 uM for CVIM substrate {ECO:0000269|PubMed:11500541,
ECO:0000269|PubMed:20565889};
KM=3.5 uM for CVIQ substrate {ECO:0000269|PubMed:11500541,
ECO:0000269|PubMed:20565889};
KM=19.0 uM for CVII substrate {ECO:0000269|PubMed:11500541,
ECO:0000269|PubMed:20565889};
KM=17.2 uM for CVIL substrate {ECO:0000269|PubMed:11500541,
ECO:0000269|PubMed:20565889};
Note=Kcat is 0.5 h(-1), 0.08 h(-1), 0.008 h(-1) and 0.012 h(-1)
for CVIL, CVII, CVIQ and CVIM substrates, respectively.;
pH dependence:
Optimum pH is 7.9-8.5 for CTIL substrate.
{ECO:0000269|PubMed:11500541, ECO:0000269|PubMed:20565889};
Temperature dependence:
Optimum temperature is 30-37 degrees Celsius for CTIL substrate.
{ECO:0000269|PubMed:11500541, ECO:0000269|PubMed:20565889};
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
siliques. {ECO:0000269|PubMed:11500541}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but mutant plants have an enhanced response to
abscisic acid (ABA)-mediated stomatal closure and increased
lateral root formation in response to exogenous auxin.
{ECO:0000269|PubMed:16183844}.
-!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG40865.1; Type=Frameshift; Positions=106; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF311225; AAG40865.1; ALT_FRAME; mRNA.
EMBL; AC004218; AAC27846.1; -; Genomic_DNA.
EMBL; CP002685; AEC09693.1; -; Genomic_DNA.
EMBL; BT002465; AAO00825.1; -; mRNA.
EMBL; BT008464; AAP37823.1; -; mRNA.
PIR; T00565; T00565.
RefSeq; NP_181487.1; NM_129513.4.
UniGene; At.16938; -.
ProteinModelPortal; O80642; -.
SMR; O80642; -.
BioGrid; 3878; 5.
STRING; 3702.AT2G39550.1; -.
iPTMnet; O80642; -.
PaxDb; O80642; -.
EnsemblPlants; AT2G39550.1; AT2G39550.1; AT2G39550.
GeneID; 818540; -.
Gramene; AT2G39550.1; AT2G39550.1; AT2G39550.
KEGG; ath:AT2G39550; -.
Araport; AT2G39550; -.
TAIR; locus:2039752; AT2G39550.
eggNOG; KOG0367; Eukaryota.
eggNOG; COG5029; LUCA.
HOGENOM; HOG000180333; -.
InParanoid; O80642; -.
KO; K11713; -.
OMA; LDDWSGM; -.
OrthoDB; EOG09360DVA; -.
PhylomeDB; O80642; -.
BioCyc; ARA:AT2G39550-MONOMER; -.
BioCyc; MetaCyc:AT2G39550-MONOMER; -.
PRO; PR:O80642; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; O80642; baseline and differential.
Genevisible; O80642; AT.
GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; IMP:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; TAS:TAIR.
GO; GO:0018344; P:protein geranylgeranylation; IMP:TAIR.
GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
GO; GO:0009733; P:response to auxin; IMP:TAIR.
GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
InterPro; IPR001330; PFTB_repeat.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
Pfam; PF00432; Prenyltrans; 5.
SUPFAM; SSF48239; SSF48239; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Metal-binding; Prenyltransferase;
Reference proteome; Repeat; Transferase; Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 375 Geranylgeranyl transferase type-1 subunit
beta.
/FTId=PRO_0000422982.
REPEAT 157 199 PFTB 1. {ECO:0000255}.
REPEAT 206 247 PFTB 2. {ECO:0000255}.
REPEAT 265 306 PFTB 3. {ECO:0000255}.
REPEAT 313 354 PFTB 4. {ECO:0000255}.
REGION 232 234 Geranylgeranyl diphosphate binding.
{ECO:0000250|UniProtKB:P53610}.
REGION 285 288 Geranylgeranyl diphosphate binding.
{ECO:0000250|UniProtKB:P53610}.
REGION 294 297 Geranylgeranyl diphosphate binding.
{ECO:0000250|UniProtKB:P53610}.
METAL 291 291 Zinc; catalytic.
{ECO:0000250|UniProtKB:P53610}.
METAL 293 293 Zinc; catalytic.
{ECO:0000250|UniProtKB:P53610}.
METAL 342 342 Zinc; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:P53610}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
CONFLICT 85 85 D -> Y (in Ref. 1; AAG40865).
{ECO:0000305}.
CONFLICT 358 358 L -> S (in Ref. 1; AAG40865).
{ECO:0000305}.
CONFLICT 369 369 L -> F (in Ref. 1; AAG40865).
{ECO:0000305}.
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


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