SGGP_ARATH
ID SGGP_ARATH Reviewed; 244 AA.
AC Q9ZVJ5; Q93ZP4;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein Sgpp;
DE EC=3.1.3.-;
DE AltName: Full=Subclass I phosphosugar phosphatase;
DE Short=AtSgpp;
GN Name=SGPP; OrderedLocusNames=At2g38740; ORFNames=T6A23.6;
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=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 [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, INDUCTION, AND FUNCTION.
RX PubMed=23179445; DOI=10.1007/s00425-012-1809-5;
RA Caparros-Martin J.A., McCarthy-Suarez I., Culianez-Macia F.A.;
RT "HAD hydrolase function unveiled by substrate screening: enzymatic
RT characterization of Arabidopsis thaliana subclass I phosphosugar
RT phosphatase AtSgpp.";
RL Planta 237:943-954(2013).
CC -!- FUNCTION: Acts as a phosphosugar phosphatase on a broad range of sugar
CC phosphate substrates with preferential activity on D-ribose-5-
CC phosphate, 2-deoxy-D-ribose-5-phosphate, 2-deoxy-D-glucose-6-phosphate,
CC and D-mannose-6-phosphate and with a lower activity on D-fructose-1-
CC phosphate, D-glucose-6-phosphate, DL-glycerol-3-phosphate, and D-
CC fructose-6-phosphate. {ECO:0000269|PubMed:23179445}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.6 mM for D-Ribose-5-phosphate {ECO:0000269|PubMed:23179445};
CC KM=4.5 mM for 2-Deoxy-D-ribose-5-phosphate
CC {ECO:0000269|PubMed:23179445};
CC KM=4.6 mM for 2-Deoxy-D-glucose-6-phosphate
CC {ECO:0000269|PubMed:23179445};
CC KM=4.9 mM for D-Mannose-6-phosphate {ECO:0000269|PubMed:23179445};
CC KM=6.9 mM for D-Fructose-1-phosphate {ECO:0000269|PubMed:23179445};
CC KM=7.1 mM for D-Glucose-6-phosphate {ECO:0000269|PubMed:23179445};
CC KM=7.3 mM for DL-Glycerol-3-phosphate {ECO:0000269|PubMed:23179445};
CC KM=7.7 mM for D-Fructose-6-phosphate {ECO:0000269|PubMed:23179445};
CC Vmax=552 nmol/sec/mg enzyme toward D-Ribose-5-phosphate
CC {ECO:0000269|PubMed:23179445};
CC Vmax=476 nmol/sec/mg enzyme toward 2-Deoxy-D-ribose-5-phosphate
CC {ECO:0000269|PubMed:23179445};
CC Vmax=472 nmol/sec/mg enzyme toward 2-Deoxy-D-glucose-6-phosphate
CC {ECO:0000269|PubMed:23179445};
CC Vmax=464 nmol/sec/mg enzyme toward D-Mannose-6-phosphate
CC {ECO:0000269|PubMed:23179445};
CC Vmax=368 nmol/sec/mg enzyme toward D-Fructose-1-phosphate
CC {ECO:0000269|PubMed:23179445};
CC Vmax=348 nmol/sec/mg enzyme toward D-Glucose-6-phosphate
CC {ECO:0000269|PubMed:23179445};
CC Vmax=332 nmol/sec/mg enzyme toward DL-Glycerol-3-phosphate
CC {ECO:0000269|PubMed:23179445};
CC Vmax=276 nmol/sec/mg enzyme toward D-Fructose-6-phosphate
CC {ECO:0000269|PubMed:23179445};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:23179445};
CC -!- TISSUE SPECIFICITY: Ubiquitous with highest expression in flowers.
CC {ECO:0000269|PubMed:23179445}.
CC -!- INDUCTION: Induced by NaCl and sorbitol. {ECO:0000269|PubMed:23179445}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. DOG/GPP
CC family. {ECO:0000305}.
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DR EMBL; AC005499; AAC67344.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09579.1; -; Genomic_DNA.
DR EMBL; AY056406; AAL08262.1; -; mRNA.
DR EMBL; AY081707; AAL87360.1; -; mRNA.
DR EMBL; AY088003; AAM65549.1; -; mRNA.
DR PIR; G84808; G84808.
DR RefSeq; NP_565895.1; NM_129431.2.
DR AlphaFoldDB; Q9ZVJ5; -.
DR SMR; Q9ZVJ5; -.
DR STRING; 3702.AT2G38740.1; -.
DR PaxDb; Q9ZVJ5; -.
DR PRIDE; Q9ZVJ5; -.
DR ProteomicsDB; 228245; -.
DR EnsemblPlants; AT2G38740.1; AT2G38740.1; AT2G38740.
DR GeneID; 818456; -.
DR Gramene; AT2G38740.1; AT2G38740.1; AT2G38740.
DR KEGG; ath:AT2G38740; -.
DR Araport; AT2G38740; -.
DR TAIR; locus:2064133; AT2G38740.
DR eggNOG; KOG2914; Eukaryota.
DR HOGENOM; CLU_045011_7_0_1; -.
DR InParanoid; Q9ZVJ5; -.
DR OMA; YHGRRPM; -.
DR OrthoDB; 747123at2759; -.
DR PhylomeDB; Q9ZVJ5; -.
DR BRENDA; 3.1.3.23; 399.
DR PRO; PR:Q9ZVJ5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVJ5; baseline and differential.
DR Genevisible; Q9ZVJ5; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050308; F:sugar-phosphatase activity; IDA:CACAO.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
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 PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..244
FT /note="Haloacid dehalogenase-like hydrolase domain-
FT containing protein Sgpp"
FT /id="PRO_0000424319"
FT ACT_SITE 28
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 30
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 244 AA; 26732 MW; F05F9368F45C67AB CRC64;
MNGFSDLNPS ESKPSLSQLA PLEAILFDVD GTLCDSDPIH LIAFQELLQE IGFNNGVPID
EKFFVENIAG KHNSEIALLL FPDDVSRGLK FCDEKEALYR KIVAEKIKPL DGLIKLTKWI
EDRGLKRAAV TNAPKENAEL MISKLGLTDF FQAVILGSEC EFPKPHPGPY LKALEVLNVS
KEHTLVFEDS ISGIKAGVAA GMPVIGLTTG NPASLLMQAK PAFLIENYAD PKLWAVLEEL
DNKS
