GPP2_ARATH
ID GPP2_ARATH Reviewed; 240 AA.
AC Q8VZP1; Q9FKM6;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=(DL)-glycerol-3-phosphatase 2;
DE EC=3.1.3.21;
DE AltName: Full=Glycerol-1-phosphatase 2;
DE AltName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein GPP2;
GN Name=GPP2; Synonyms=GS1; OrderedLocusNames=At5g57440;
GN ORFNames=MSF19, MUA2.2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND FUNCTION.
RX PubMed=17136424; DOI=10.1007/s11103-006-9104-0;
RA Caparros-Martin J.A., Reiland S., Koechert K., Cutanda M.C.,
RA Culianez-Macia F.A.;
RT "Arabidopsis thaliana AtGppl and AtGpp2: two novel low molecular weight
RT phosphatases involved in plant glycerol metabolism.";
RL Plant Mol. Biol. 63:505-517(2007).
CC -!- FUNCTION: Acts as a glycerol-3-phosphatase with higher
CC stereospecificity for L-glycerol-3-phosphate than DL-glycerol-3-
CC phosphate. {ECO:0000269|PubMed:17136424}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 1-phosphate = glycerol + phosphate;
CC Xref=Rhea:RHEA:46084, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57685; EC=3.1.3.21;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 3-phosphate = glycerol + phosphate;
CC Xref=Rhea:RHEA:66372, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57597; EC=3.1.3.21;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.5 mM for DL-glycerol-3-phosphate {ECO:0000269|PubMed:17136424};
CC Vmax=23 nmol/min/mg enzyme toward DL-glycerol-3-phosphate
CC {ECO:0000269|PubMed:17136424};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:17136424};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:17136424}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with highest expression in siliques.
CC Mainly restricted to the meristem of immature flower and vascular
CC elements of the root, shoot, leave, siliqua and developing embryo (at
CC the protein level). {ECO:0000269|PubMed:17136424}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. DOG/GPP
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08780.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB011482; BAB08780.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED96902.1; -; Genomic_DNA.
DR EMBL; AY063967; AAL36323.1; -; mRNA.
DR EMBL; AY114031; AAM45079.1; -; mRNA.
DR EMBL; AY084531; AAM61099.1; -; mRNA.
DR RefSeq; NP_568858.1; NM_125126.3.
DR AlphaFoldDB; Q8VZP1; -.
DR SMR; Q8VZP1; -.
DR BioGRID; 21093; 1.
DR STRING; 3702.AT5G57440.1; -.
DR PaxDb; Q8VZP1; -.
DR PRIDE; Q8VZP1; -.
DR ProteomicsDB; 220777; -.
DR EnsemblPlants; AT5G57440.1; AT5G57440.1; AT5G57440.
DR GeneID; 835849; -.
DR Gramene; AT5G57440.1; AT5G57440.1; AT5G57440.
DR KEGG; ath:AT5G57440; -.
DR Araport; AT5G57440; -.
DR TAIR; locus:2174567; AT5G57440.
DR eggNOG; KOG2914; Eukaryota.
DR HOGENOM; CLU_045011_13_0_1; -.
DR InParanoid; Q8VZP1; -.
DR OMA; HTLDDSW; -.
DR OrthoDB; 1510544at2759; -.
DR PhylomeDB; Q8VZP1; -.
DR BioCyc; ARA:AT5G57440-MON; -.
DR PRO; PR:Q8VZP1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VZP1; baseline and differential.
DR Genevisible; Q8VZP1; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000121; F:glycerol-1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0043136; F:glycerol-3-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0050308; F:sugar-phosphatase activity; IDA:TAIR.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006114; P:glycerol biosynthetic process; IMP:UniProtKB.
DR CDD; cd07529; HAD_AtGPP-like; 1.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR045228; Gpp1/Gpp2-like.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..240
FT /note="(DL)-glycerol-3-phosphatase 2"
FT /id="PRO_0000424318"
FT ACT_SITE 20
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 22
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 240 AA; 26780 MW; 25ECC3407BF349BD CRC64;
MSNPAAVTAG RGSITHVIFD MDGLLLDTEK FYTEVQEIIL ARFNKKFDWS LKAKMMGRKA
IEAARIFVEE SGISDSLSAE DFLVERESML QDLFPTSELM PGASRLIKHL HVKNIPICIA
TGTHTRHYDL KTQRHRELFS LMHHVVRGDD PEVKQGKPAP DGFLAAARRF KDGPVDSQKV
LVFEDAPSGV LAAKNAGMNV VMVPDPRLDI SHQDVADQII TSLVDFKPEE WGLPPFEDSN
