ID   GWD2_ARATH              Reviewed;        1278 AA.
AC   Q9STV0; Q84W86;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 3.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Alpha-glucan water dikinase 2;
DE            EC=2.7.9.4;
DE   Flags: Precursor;
GN   Name=GWD2; OrderedLocusNames=At4g24450; ORFNames=T22A6.280;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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).
CC   -!- FUNCTION: Mediates the incorporation of phosphate into alpha-glucan,
CC       mostly at the C-6 position of glucose units. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + n ATP + n H2O = [(1->4)-6-
CC         phospho-alpha-D-glucosyl](n) + n AMP + 2n H(+) + n phosphate;
CC         Xref=Rhea:RHEA:11668, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:12983,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:134068,
CC         ChEBI:CHEBI:456215; EC=2.7.9.4;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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 B-terminal domain (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB45080.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79355.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL078637; CAB45080.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161561; CAB79355.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84906.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM67023.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM67024.1; -; Genomic_DNA.
DR   EMBL; BT004118; AAO42141.1; -; mRNA.
DR   PIR; T09908; T09908.
DR   RefSeq; NP_001328878.1; NM_001341673.1.
DR   RefSeq; NP_001328879.1; NM_001341674.1.
DR   RefSeq; NP_194176.3; NM_118578.5.
DR   AlphaFoldDB; Q9STV0; -.
DR   STRING; 3702.AT4G24450.1; -.
DR   CAZy; CBM45; Carbohydrate-Binding Module Family 45.
DR   PaxDb; Q9STV0; -.
DR   PRIDE; Q9STV0; -.
DR   ProteomicsDB; 247276; -.
DR   EnsemblPlants; AT4G24450.1; AT4G24450.1; AT4G24450.
DR   EnsemblPlants; AT4G24450.2; AT4G24450.2; AT4G24450.
DR   EnsemblPlants; AT4G24450.3; AT4G24450.3; AT4G24450.
DR   GeneID; 828547; -.
DR   Gramene; AT4G24450.1; AT4G24450.1; AT4G24450.
DR   Gramene; AT4G24450.2; AT4G24450.2; AT4G24450.
DR   Gramene; AT4G24450.3; AT4G24450.3; AT4G24450.
DR   KEGG; ath:AT4G24450; -.
DR   Araport; AT4G24450; -.
DR   TAIR; locus:2136027; AT4G24450.
DR   eggNOG; ENOG502QSQR; Eukaryota.
DR   HOGENOM; CLU_002399_1_0_1; -.
DR   InParanoid; Q9STV0; -.
DR   OMA; SFHVRNY; -.
DR   OrthoDB; 55520at2759; -.
DR   BioCyc; ARA:AT4G24450-MON; -.
DR   BRENDA; 2.7.9.4; 399.
DR   PRO; PR:Q9STV0; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9STV0; baseline and differential.
DR   Genevisible; Q9STV0; AT.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0102216; F:maltodextrin water dikinase; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0102218; F:starch, H2O dikinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   Pfam; PF01326; PPDK_N; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Signal; Transferase.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..1278
FT                   /note="Alpha-glucan water dikinase 2"
FT                   /id="PRO_0000240249"
FT   ACT_SITE        886
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        103
FT                   /note="S -> N (in Ref. 3; AAO42141)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="R -> G (in Ref. 3; AAO42141)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        630
FT                   /note="Q -> R (in Ref. 3; AAO42141)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1278 AA;  144812 MW;  C62746575CFCFA00 CRC64;
     MATSKSQQFQ LIEGMELQIT VTGLPNGSSV RAEFHLKNCT RAWILHWGCI YQGNNHWYIP
     SEHSSKQGAL QTTFVKSGDA YVVILELRDP RVRAIEFVLK DGSHNRWLRQ HNGNFRVEIP
     WNDLHAHHRI PKTLIERRAH KIWDRKGRPQ SSAREQQIDY DNAVRELHAE LARGISLDEL
     QANSTVPVEK EETSEPHHTM IQSYRRKHDV QKWLQKYTEP INRSGSVKSS ALAELSKRSV
     GQENLVSQKS FHVRNYEITV LQRDVKGDCR LWIATNMAGP TVLHWGVAKS SAGEWLIPPP
     DVLPEKSKFV HGACQTQFTD MSSREHSYQF IDINLKRGGF VGIQFVIWSG GYWVNNNGAN
     FVVNLKSADS TSGKLDVDEK YVLKWLLDEI SEREKEAERS LMHRFNIATE LTERCKDEGE
     GGCIGIMVWM RFMATRHLTW NKNYNVKPRE ISEALERFTN LMEKIYLQQP NKREIVRLTM
     ALVGRGGQGD VGQRIRDEIL VIQRNNHCKS GMMEEWHQKL HNNSSADDVI ICEALLNYVR
     SDFRIDAYWQ TLQTNGLTKE RLASYDRPIV SEPRFRSDSK EGLIRDLTMY LKTLKAVHSG
     ADLESAIDTF LSPSKGHHVF AVNGLSPKLQ DLLNLVKRLV REENTEPLIE KLVDARIQLH
     PALRAPRTRA KDLLFLDIAL ESCFKTTIEK RLISLNFNNP PEIIYVICVV LENLCLSIVN
     NEEIIFCTKD WYRVSEAYRP HDVQWALQTK AVLDRLQLVL ADRCQHYFTI IQPTAKYLGQ
     LLRVDKHGID VFTEEVIRAG PGAVLSTLVN RFDPSLRKIA NLGCWQVISS ADAYGFVVCV
     NELIVVQNKF YSKPTVIIAS KVTGEEEIPA GVVAVLTPSM IDVLSHVSIR ARNSKICFAT
     CFDQNVLSNL KSKEGRAISI HTKSTGLVIS DGNNSDVSVR HIFISSVPRG VISKGKKFCG
     HYVISSKEFT DERVGSKSYN IKFLRERVPS WIKIPTSAAL PFGTFENILS DDSNKDVARR
     ISVLKDSLNR GDLTKLKSIQ EAILQMSAPM ALRNELITKL RSERMPYLGD ESGWNRSWVA
     IKKVWASKWN ERAYVSCKKN KLDHDAVCMA VLIQEVICGD YAFVIHTNNP VSGDSSEIYT
     EIVKGLGETL VGAYPGRAMS FITKKTNLKS PTVISYPSKR IGLYSKPSII FRSDSNNEDL
     EGNAGAGLYD SVIMDEAEEV VVDYSREPLI MDKSFRVRLF SAIAEAGNVI ESIYGCPQDI
     EGVVKGGHIY IVQARPQV