GWD1_ARATH
ID GWD1_ARATH Reviewed; 1399 AA.
AC Q9SAC6; Q93VD0; Q940Z0; Q9FPP2; Q9SGX4;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Alpha-glucan water dikinase 1, chloroplastic {ECO:0000305};
DE EC=2.7.9.4 {ECO:0000269|PubMed:11487701};
DE AltName: Full=Protein starch excess 1 {ECO:0000303|PubMed:11487701};
DE AltName: Full=Protein starch-related R1 {ECO:0000303|PubMed:11487701};
DE Flags: Precursor;
GN Name=GWD1 {ECO:0000305};
GN Synonyms=R1 {ECO:0000303|PubMed:11487701},
GN SEX1 {ECO:0000303|PubMed:11487701};
GN OrderedLocusNames=At1g10760 {ECO:0000312|Araport:AT1G10760};
GN ORFNames=F20B24.19 {ECO:0000312|EMBL:AAF17665.1},
GN T16B5.10 {ECO:0000312|EMBL:AAD31337.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLY-1268.
RX PubMed=11487701; DOI=10.2307/3871327;
RA Yu T.-S., Kofler H., Haeusler R.E., Hille D., Fluegge U.-I., Zeeman S.C.,
RA Smith A.M., Kossmann J., Lloyd J., Ritte G., Steup M., Lue W.-L., Chen J.,
RA Weber A.;
RT "The Arabidopsis sex1 mutant is defective in the R1 protein, a general
RT regulator of starch degradation in plants, and not in the chloroplast
RT hexose transporter.";
RL Plant Cell 13:1907-1918(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1220-1399.
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-76, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-75, 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 alpha-glucan, mostly at the C-6 position of glucose units. Acts as an
CC overall regulator of starch mobilization. Required for starch
CC degradation, suggesting that the phosphate content of starch regulates
CC its degradability. {ECO:0000269|PubMed:11487701}.
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 Evidence={ECO:0000269|PubMed:11487701};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11669;
CC Evidence={ECO:0000269|PubMed:11487701};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P23538};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P23538}.
CC -!- INTERACTION:
CC Q9SAC6; Q17TI5: BRX; NbExp=3; IntAct=EBI-2355356, EBI-4426649;
CC Q9SAC6; Q8VYF7: WHY2; NbExp=3; IntAct=EBI-2355356, EBI-15219982;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:11487701}. Note=Starch granules.
CC {ECO:0000269|PubMed:11487701}.
CC -!- DEVELOPMENTAL STAGE: The level of protein does not vary in a circadian
CC rhythm and is stable throughout day and night (at protein level).
CC {ECO:0000269|PubMed:11487701}.
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.
CC {ECO:0000250|UniProtKB:P23538}.
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=AAD31337.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF17665.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK49609.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK96541.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF312027; AAG47821.1; -; mRNA.
DR EMBL; AC007354; AAD31337.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC009398; AAF17665.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28643.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58154.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58155.1; -; Genomic_DNA.
DR EMBL; AF372893; AAK49609.1; ALT_INIT; mRNA.
DR EMBL; AY052349; AAK96541.1; ALT_INIT; mRNA.
DR EMBL; AY057722; AAL15352.1; -; mRNA.
DR PIR; B86241; B86241.
DR RefSeq; NP_001318975.1; NM_001331926.1.
DR RefSeq; NP_001320611.1; NM_001331927.1.
DR RefSeq; NP_563877.1; NM_100952.4.
DR AlphaFoldDB; Q9SAC6; -.
DR SMR; Q9SAC6; -.
DR BioGRID; 22859; 8.
DR IntAct; Q9SAC6; 3.
DR MINT; Q9SAC6; -.
DR STRING; 3702.AT1G10760.1; -.
DR CAZy; CBM45; Carbohydrate-Binding Module Family 45.
DR iPTMnet; Q9SAC6; -.
DR PaxDb; Q9SAC6; -.
DR PRIDE; Q9SAC6; -.
DR ProteomicsDB; 247326; -.
DR EnsemblPlants; AT1G10760.1; AT1G10760.1; AT1G10760.
DR EnsemblPlants; AT1G10760.2; AT1G10760.2; AT1G10760.
DR EnsemblPlants; AT1G10760.3; AT1G10760.3; AT1G10760.
DR GeneID; 837619; -.
DR Gramene; AT1G10760.1; AT1G10760.1; AT1G10760.
DR Gramene; AT1G10760.2; AT1G10760.2; AT1G10760.
DR Gramene; AT1G10760.3; AT1G10760.3; AT1G10760.
DR KEGG; ath:AT1G10760; -.
DR Araport; AT1G10760; -.
DR TAIR; locus:2019953; AT1G10760.
DR eggNOG; ENOG502QQ6R; Eukaryota.
DR HOGENOM; CLU_002399_1_0_1; -.
DR InParanoid; Q9SAC6; -.
DR OMA; IFVWIRF; -.
DR OrthoDB; 55520at2759; -.
DR PhylomeDB; Q9SAC6; -.
DR BioCyc; ARA:AT1G10760-MON; -.
DR BioCyc; MetaCyc:AT1G10760-MON; -.
DR BRENDA; 2.7.9.4; 399.
DR PRO; PR:Q9SAC6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SAC6; baseline and differential.
DR Genevisible; Q9SAC6; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0050521; F:alpha-glucan, water dikinase activity; IMP: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:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0102218; F:starch, H2O dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009631; P:cold acclimation; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009610; P:response to symbiotic fungus; IEP:TAIR.
DR GO; GO:0005983; P:starch catabolic process; IMP:TAIR.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Carbohydrate metabolism; Chloroplast; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..75
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 76..1399
FT /note="Alpha-glucan water dikinase 1, chloroplastic"
FT /id="PRO_0000023565"
FT REGION 265..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1004
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 76
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 1268
FT /note="G->E: In sex1-1; induces an excess of starch in
FT leaves after a long period of darkness."
FT /evidence="ECO:0000269|PubMed:11487701"
SQ SEQUENCE 1399 AA; 156582 MW; 1FE9285376B479EB CRC64;
MSNSVVHNLL NRGLIRPLNF EHQNKLNSSV YQTSTANPAL GKIGRSKLYG KGLKQAGRSL
VTETGGRPLS FVPRAVLAMD PQAAEKFSLD GNIDLLVEVT STTVREVNIQ IAYTSDTLFL
HWGAILDNKE NWVLPSRSPD RTQNFKNSAL RTPFVKSGGN SHLKLEIDDP AIHAIEFLIF
DESRNKWYKN NGQNFHINLP TERNVKQNVS VPEDLVQIQA YLRWERKGKQ MYNPEKEKEE
YEAARTELRE EMMRGASVED LRAKLLKKDN SNESPKSNGT SSSGREEKKK VSKQPERKKN
YNTDKIQRKG RDLTKLIYKH VADFVEPESK SSSEPRSLTT LEIYAKAKEE QETTPVFSKK
TFKLEGSAIL VFVTKLSGKT KIHVATDFKE PVTLHWALSQ KGGEWLDPPS DILPPNSLPV
RGAVDTKLTI TSTDLPSPVQ TFELEIEGDS YKGMPFVLNA GERWIKNNDS DFYVDFAKEE
KHVQKDYGDG KGTAKHLLDK IADLESEAQK SFMHRFNIAA DLVDEAKSAG QLGFAGILVW
MRFMATRQLV WNKNYNVKPR EISKAQDRLT DLLQDVYASY PEYRELLRMI MSTVGRGGEG
DVGQRIRDEI LVIQRKNDCK GGIMEEWHQK LHNNTSPDDV VICQALMDYI KSDFDLSVYW
KTLNDNGITK ERLLSYDRAI HSEPNFRGEQ KDGLLRDLGH YMRTLKAVHS GADLESAIQN
CMGYQDDGEG FMVGVQINPV SGLPSGYPDL LRFVLEHVEE KNVEPLLEGL LEARQELRPL
LLKSHDRLKD LLFLDLALDS TVRTAIERGY EQLNDAGPEK IMYFISLVLE NLALSSDDNE
DLIYCLKGWQ FALDMCKSKK DHWALYAKSV LDRSRLALAS KAERYLEILQ PSAEYLGSCL
GVDQSAVSIF TEEIIRAGSA AALSSLVNRL DPVLRKTANL GSWQVISPVE VVGYVIVVDE
LLTVQNKTYD RPTIIVANRV RGEEEIPDGA VAVLTPDMPD VLSHVSVRAR NGKICFATCF
DSGILSDLQG KDGKLLSLQP TSADVVYKEV NDSELSSPSS DNLEDAPPSI SLVKKQFAGR
YAISSEEFTS DLVGAKSRNI GYLKGKVPSW VGIPTSVALP FGVFEKVISE KANQAVNDKL
LVLKKTLDEG DQGALKEIRQ TLLGLVAPPE LVEELKSTMK SSDMPWPGDE GEQRWEQAWA
AIKKVWASKW NERAYFSTRK VKLDHDYLCM AVLVQEVINA DYAFVIHTTN PSSGDSSEIY
AEVVKGLGET LVGAYPGRSL SFICKKNNLD SPLVLGYPSK PIGLFIRRSI IFRSDSNGED
LEGYAGAGLY DSVPMDEEDQ VVLDYTTDPL ITDLSFQKKV LSDIARAGDA IEKLYGTAQD
IEGVIRDGKL YVVQTRPQV
