GDPD6_ARATH
ID GDPD6_ARATH Reviewed; 372 AA.
AC Q9SD81;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Glycerophosphodiester phosphodiesterase GDPD6 {ECO:0000305};
DE EC=3.1.4.46 {ECO:0000250|UniProtKB:Q9SGA2};
DE AltName: Full=Glycerophosphodiester phosphodiesterase 6 {ECO:0000303|PubMed:21323773};
DE Short=ATGDPD6 {ECO:0000303|PubMed:21323773};
DE Flags: Precursor;
GN Name=GDPD6 {ECO:0000303|PubMed:21323773};
GN OrderedLocusNames=At5g08030 {ECO:0000312|Araport:AT5G08030};
GN ORFNames=F13G24.230 {ECO:0000312|EMBL:CAB62615.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21323773; DOI=10.1111/j.1365-313x.2011.04538.x;
RA Cheng Y., Zhou W., El Sheery N.I., Peters C., Li M., Wang X., Huang J.;
RT "Characterization of the Arabidopsis glycerophosphodiester
RT phosphodiesterase (GDPD) family reveals a role of the plastid-localized
RT AtGDPD1 in maintaining cellular phosphate homeostasis under phosphate
RT starvation.";
RL Plant J. 66:781-795(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-
CC glycerol 3-phosphate; Xref=Rhea:RHEA:12969, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:83408; EC=3.1.4.46;
CC Evidence={ECO:0000250|UniProtKB:Q9SGA2};
CC -!- TISSUE SPECIFICITY: Expressed in flowers and siliques.
CC {ECO:0000269|PubMed:21323773}.
CC -!- INDUCTION: By phosphate starvation. {ECO:0000269|PubMed:21323773}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; AL133421; CAB62615.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91236.1; -; Genomic_DNA.
DR EMBL; BT023450; AAY56441.1; -; mRNA.
DR PIR; T45628; T45628.
DR RefSeq; NP_196420.1; NM_120885.4.
DR AlphaFoldDB; Q9SD81; -.
DR SMR; Q9SD81; -.
DR STRING; 3702.AT5G08030.1; -.
DR PaxDb; Q9SD81; -.
DR PRIDE; Q9SD81; -.
DR ProteomicsDB; 247119; -.
DR EnsemblPlants; AT5G08030.1; AT5G08030.1; AT5G08030.
DR GeneID; 830697; -.
DR Gramene; AT5G08030.1; AT5G08030.1; AT5G08030.
DR KEGG; ath:AT5G08030; -.
DR Araport; AT5G08030; -.
DR TAIR; locus:2142823; AT5G08030.
DR eggNOG; KOG2258; Eukaryota.
DR HOGENOM; CLU_030226_4_1_1; -.
DR InParanoid; Q9SD81; -.
DR PhylomeDB; Q9SD81; -.
DR PRO; PR:Q9SD81; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SD81; baseline and differential.
DR Genevisible; Q9SD81; AT.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS51704; GP_PDE; 1.
PE 2: Evidence at transcript level;
KW Glycerol metabolism; Glycoprotein; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..372
FT /note="Glycerophosphodiester phosphodiesterase GDPD6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430613"
FT DOMAIN 44..362
FT /note="GP-PDE"
FT /evidence="ECO:0000255"
FT REGION 32..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 372 AA; 42882 MW; D189363733C223D3 CRC64;
MAFKYLLPLL LLSLLVANCA SRPLYRLPSE AKHATKKPLQ TSRPYNLAHR GSNGELPEET
APAYMRAIEE GADFIETDIL SSKDGVLICH HDVNLDDTTD VADHKEFADR KRTYEVQGMN
MTGFFTVDFT LKELKTLGAK QRYPFRDQQY NGKFPIITFD EYISIALDAP RVVGIYPEIK
NPVFMNQQVK WADGKKFEDK FVETLKKYGY KGSYLSEDWL KQPIFIQSFA ATSLVYISNM
TDSPKLFLID DVTILTEDTN KTYAEITSDA YLDYIKPYVI GIGPWKDTIV PVNNNRLMTP
TDLVARAHSR NLQVHPYTYR NENQFLHLEF NQDPYLEYDY WLNKIGVDGL FTDFTGSLHN
YQELKSPLPQ QQ
