PWD_ARATH
ID PWD_ARATH Reviewed; 1196 AA.
AC Q6ZY51; O81504; O81505; Q5XMK9; Q84TI8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Phosphoglucan, water dikinase, chloroplastic;
DE EC=2.7.9.5;
DE Flags: Precursor;
GN Name=GWD3; Synonyms=OK1, PWD; OrderedLocusNames=At5g26570;
GN ORFNames=F9D12.1, F9D12.19;
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, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, INDUCTION, TISSUE SPECIFICITY, AND AUTOPHOSPHORYLATION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=15686522; DOI=10.1111/j.1365-313x.2004.02322.x;
RA Baunsgaard L., Luetken H., Mikkelsen R., Glaring M.A., Pham T.T.,
RA Blennow A.;
RT "A novel isoform of glucan, water dikinase phosphorylates pre-
RT phosphorylated alpha-glucans and is involved in starch degradation in
RT Arabidopsis.";
RL Plant J. 41:595-605(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND ACTIVE SITE HIS-759.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=15618411; DOI=10.1104/pp.104.055954;
RA Koetting O., Pusch K., Tiessen A., Geigenberger P., Steup M., Ritte G.;
RT "Identification of a novel enzyme required for starch metabolism in
RT Arabidopsis leaves. The phosphoglucan, water dikinase.";
RL Plant Physiol. 137:242-252(2005).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-1196.
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-55, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-54, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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: Mediates the incorporation of phosphate into starch-like
CC phospho-alpha-glucan, mostly at the C-3 position of glucose units.
CC Required for starch degradation, suggesting that the phosphate content
CC of starch regulates its degradability. {ECO:0000269|PubMed:15618411,
CC ECO:0000269|PubMed:15686522}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-6-phospho-alpha-D-glucosyl](n) + n ATP + n H2O =
CC [(1->4)-3,6-bisphospho-alpha-D-glucosyl](n) + n AMP + 2n H(+) + n
CC phosphate; Xref=Rhea:RHEA:10256, Rhea:RHEA-COMP:12983, Rhea:RHEA-
CC COMP:14598, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:134068, ChEBI:CHEBI:140561,
CC ChEBI:CHEBI:456215; EC=2.7.9.5;
CC Evidence={ECO:0000269|PubMed:15618411, ECO:0000269|PubMed:15686522};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15618411, ECO:0000269|PubMed:15686522}. Note=Starch
CC granules during starch mobilization in darkness.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q6ZY51-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: In all starch containing tissues (e.g. roots,
CC leaves, stems, inflorescence and siliques).
CC {ECO:0000269|PubMed:15686522}.
CC -!- INDUCTION: Circadian regulation. Induced during light phase and
CC repressed during dark phase. {ECO:0000269|PubMed:15686522}.
CC -!- DOMAIN: The N-terminal domain contains the alpha-glucan binding site,
CC the central domain the pyrophosphate/phosphate carrier histidine, and
CC the C-terminal domain the ATP binding site. {ECO:0000250}.
CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated by a
CC phosphocarrier histidine residue located on the surface of the central
CC domain. The two first partial reactions are catalyzed at an active site
CC located on the C-terminal domain, and the third partial reaction is
CC catalyzed at an active site located on the N-terminal domain. For
CC catalytic turnover, the central domain swivels from the concave surface
CC of the C-terminal domain to that of the N-terminal domain (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC26245.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC26246.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY747068; AAU93516.1; -; mRNA.
DR EMBL; AJ635427; CAG25776.1; -; mRNA.
DR EMBL; AF077407; AAC26245.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF077407; AAC26246.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93555.1; -; Genomic_DNA.
DR EMBL; BT005745; AAO64153.1; -; mRNA.
DR PIR; T01856; T01856.
DR PIR; T01857; T01857.
DR RefSeq; NP_198009.3; NM_122538.5. [Q6ZY51-1]
DR AlphaFoldDB; Q6ZY51; -.
DR SMR; Q6ZY51; -.
DR BioGRID; 17981; 1.
DR STRING; 3702.AT5G26570.1; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR iPTMnet; Q6ZY51; -.
DR PaxDb; Q6ZY51; -.
DR PRIDE; Q6ZY51; -.
DR ProteomicsDB; 226130; -. [Q6ZY51-1]
DR EnsemblPlants; AT5G26570.1; AT5G26570.1; AT5G26570. [Q6ZY51-1]
DR GeneID; 832706; -.
DR Gramene; AT5G26570.1; AT5G26570.1; AT5G26570. [Q6ZY51-1]
DR KEGG; ath:AT5G26570; -.
DR Araport; AT5G26570; -.
DR TAIR; locus:2151089; AT5G26570.
DR eggNOG; ENOG502QS3J; Eukaryota.
DR HOGENOM; CLU_012115_0_0_1; -.
DR InParanoid; Q6ZY51; -.
DR OMA; DKVYSDQ; -.
DR PhylomeDB; Q6ZY51; -.
DR BioCyc; ARA:AT5G26570-MON; -.
DR BioCyc; MetaCyc:AT5G26570-MON; -.
DR BRENDA; 2.7.9.4; 399.
DR BRENDA; 2.7.9.5; 399.
DR PRO; PR:Q6ZY51; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6ZY51; baseline and differential.
DR Genevisible; Q6ZY51; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0102217; F:6-phosphoglucan, water dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019200; F:carbohydrate kinase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051752; F:phosphoglucan, water dikinase activity; IDA:TAIR.
DR GO; GO:0102219; F:phosphogluco-amylopectin water dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0005983; P:starch catabolic process; TAS:TAIR.
DR GO; GO:0005982; P:starch metabolic process; IMP:TAIR.
DR CDD; cd05818; CBM20_water_dikinase; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR034848; CBM20_water_dikinase.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Carbohydrate metabolism;
KW Chloroplast; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 55..1196
FT /note="Phosphoglucan, water dikinase, chloroplastic"
FT /id="PRO_0000240250"
FT DOMAIN 66..166
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 174..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 759
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000305|PubMed:15618411"
FT MOD_RES 55
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 52
FT /note="C -> R (in Ref. 1; AAU93516)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="Y -> C (in Ref. 1; AAU93516)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="K -> R (in Ref. 5; AAO64153)"
FT /evidence="ECO:0000305"
FT CONFLICT 1109
FT /note="I -> V (in Ref. 5; AAO64153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1196 AA; 131323 MW; 98A320AC0484532B CRC64;
MESIGSHCCS SPFTFITRNS SSSLPRLVNI THRVNLSHQS HRLRNSNSRL TCTATSSSTI
EEQRKKKDGS GTKVRLNVRL DHQVNFGDHV AMFGSAKEIG SWKKKSPLNW SENGWVCELE
LDGGQVLEYK FVIVKNDGSL SWESGDNRVL KVPNSGNFSV VCHWDATRET LDLPQEVGND
DDVGDGGHER DNHDVGDDRV VGSENGAQLQ KSTLGGQWQG KDASFMRSND HGNREVGRNW
DTSGLEGTAL KMVEGDRNSK NWWRKLEMVR EVIVGSVERE ERLKALIYSA IYLKWINTGQ
IPCFEDGGHH RPNRHAEISR LIFRELEHIC SKKDATPEEV LVARKIHPCL PSFKAEFTAA
VPLTRIRDIA HRNDIPHDLK QEIKHTIQNK LHRNAGPEDL IATEAMLQRI TETPGKYSGD
FVEQFKIFHN ELKDFFNAGS LTEQLDSMKI SMDDRGLSAL NLFFECKKRL DTSGESSNVL
ELIKTMHSLA SLRETIIKEL NSGLRNDAPD TAIAMRQKWR LCEIGLEDYF FVLLSRFLNA
LETMGGADQL AKDVGSRNVA SWNDPLDALV LGVHQVGLSG WKQEECLAIG NELLAWRERD
LLEKEGEEDG KTIWAMRLKA TLDRARRLTA EYSDLLLQIF PPNVEILGKA LGIPENSVKT
YTEAEIRAGI IFQISKLCTV LLKAVRNSLG SEGWDVVVPG STSGTLVQVE SIVPGSLPAT
SGGPIILLVN KADGDEEVSA ANGNIAGVML LQELPHLSHL GVRARQEKIV FVTCDDDDKV
ADIRRLVGKF VRLEASPSHV NLILSTEGRS RTSKSSATKK TDKNSLSKKK TDKKSLSIDD
EESKPGSSSS NSLLYSSKDI PSGGIIALAD ADVPTSGSKS AACGLLASLA EASSKVHSEH
GVPASFKVPT GVVIPFGSME LALKQNNSEE KFASLLEKLE TARPEGGELD DICDQIHEVM
KTLQVPKETI NSISKAFLKD ARLIVRSSAN VEDLAGMSAA GLYESIPNVS PSDPLVFSDS
VCQVWASLYT RRAVLSRRAA GVSQREASMA VLVQEMLSPD LSFVLHTVSP ADPDSNLVEA
EIAPGLGETL ASGTRGTPWR LASGKLDGIV QTLAFANFSE ELLVSGTGPA DGKYVRLTVD
YSKKRLTVDS VFRQQLGQRL GSVGFFLERN FGCAQDVEGC LVGEDVYIVQ SRPQPL
