GWD1_SOLTU
ID GWD1_SOLTU Reviewed; 1464 AA.
AC Q9AWA5; O82061;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Alpha-glucan water dikinase, chloroplastic;
DE EC=2.7.13.3;
DE EC=2.7.9.4;
DE AltName: Full=Starch-related R1 protein;
DE Flags: Precursor;
GN Name=R1;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 78-91, FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Desiree;
RX PubMed=9592398; DOI=10.1038/nbt0598-473;
RA Lorberth R., Ritte G., Willmitzer L., Kossmann J.;
RT "Inhibition of a starch-granule-bound protein leads to modified starch and
RT repression of cold sweetening.";
RL Nat. Biotechnol. 16:473-477(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Prevalent;
RX PubMed=11841813; DOI=10.1016/s0008-6215(01)00326-3;
RA Viksoe-Nielsen A., Chen P.-H.J., Larsson H., Blennow A., Moeller B.L.;
RT "Production of highly phosphorylated glycopolymers by expression of R1 in
RT Escherichia coli.";
RL Carbohydr. Res. 337:327-333(2002).
RN [3]
RP PROTEIN SEQUENCE OF 78-86; 394-405; 614-622; 797-805; 1121-1130 AND
RP 1132-1140, ACTIVE SITE HIS-1069, AND ENZYME MECHANISM.
RX PubMed=15361065; DOI=10.1042/bj20041119;
RA Mikkelsen R., Blennow A.;
RT "Functional domain organization of the potato alpha-glucan, water dikinase
RT (GWD): evidence for separate site catalysis as revealed by limited
RT proteolysis and deletion mutants.";
RL Biochem. J. 385:355-361(2005).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=10758490; DOI=10.1046/j.1365-313x.2000.00683.x;
RA Ritte G., Lorberth R., Steup M.;
RT "Reversible binding of the starch-related R1 protein to the surface of
RT transitory starch granules.";
RL Plant J. 21:387-391(2000).
RN [5]
RP ENZYME ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12011472; DOI=10.1073/pnas.062053099;
RA Ritte G., Lloyd J.R., Eckermann N., Rottmann A., Kossmann J., Steup M.;
RT "The starch-related R1 protein is an alpha-glucan, water dikinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7166-7171(2002).
RN [6]
RP FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE HIS-1069, AND
RP MUTAGENESIS OF HIS-1069.
RX PubMed=14525539; DOI=10.1042/bj20030999;
RA Mikkelsen R., Baunsgaard L., Blennow A.;
RT "Functional characterization of alpha-glucan, water dikinase, the starch
RT phosphorylating enzyme.";
RL Biochem. J. 377:525-532(2004).
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. More active on alpha-1,6 branched amylopectin.
CC {ECO:0000269|PubMed:11841813, ECO:0000269|PubMed:14525539,
CC ECO:0000269|PubMed:9592398}.
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:12011472};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:12011472};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12011472};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 uM for ATP {ECO:0000269|PubMed:12011472,
CC ECO:0000269|PubMed:14525539};
CC KM=1.7 uM for amylopectin {ECO:0000269|PubMed:12011472,
CC ECO:0000269|PubMed:14525539};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:12011472,
CC ECO:0000269|PubMed:14525539};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:12011472, ECO:0000269|PubMed:14525539};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14525539}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10758490, ECO:0000269|PubMed:9592398}. Note=Starch
CC granules. Binds to starch granules isolated from either illuminated or
CC darkened leaves. However, binding to darkened leaves is more effective,
CC suggesting that depending upon the metabolic state of the cells, the
CC starch granule surface changes and thereby affects its binding.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:9592398}.
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 -!- 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.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR EMBL; Y09533; CAA70725.1; -; mRNA.
DR EMBL; AY027522; AAK11735.1; -; mRNA.
DR PIR; T07050; T07050.
DR AlphaFoldDB; Q9AWA5; -.
DR SMR; Q9AWA5; -.
DR STRING; 4113.PGSC0003DMT400019845; -.
DR CAZy; CBM45; Carbohydrate-Binding Module Family 45.
DR PRIDE; Q9AWA5; -.
DR ProMEX; Q9AWA5; -.
DR KEGG; ag:CAA70725; -.
DR eggNOG; ENOG502QQ6R; Eukaryota.
DR InParanoid; Q9AWA5; -.
DR BRENDA; 2.7.9.4; 5757.
DR SABIO-RK; Q9AWA5; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q9AWA5; baseline.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0102218; F:starch, H2O dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; 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 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Chloroplast;
KW Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..77
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:15361065,
FT ECO:0000269|PubMed:9592398"
FT CHAIN 78..1464
FT /note="Alpha-glucan water dikinase, chloroplastic"
FT /id="PRO_0000023567"
FT ACT_SITE 1069
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000269|PubMed:14525539,
FT ECO:0000269|PubMed:15361065"
FT MUTAGEN 1069
FT /note="H->A: Loss of activity, no autophosphorylation."
FT /evidence="ECO:0000269|PubMed:14525539"
FT CONFLICT 66
FT /note="E -> G (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="K -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="E -> Q (in Ref. 2; AAK11735 and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="G -> E (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="N -> I (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 203..204
FT /note="RV -> HI (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="P -> T (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="V -> E (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="D -> N (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="T -> K (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="K -> E (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="H -> Q (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="T -> P (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="P -> A (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="A -> S (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="G -> D (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="L -> S (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="I -> M (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="N -> K (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="Q -> E (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 768
FT /note="R -> K (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1129
FT /note="A -> V (in Ref. 2; AAK11735 and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1209
FT /note="M -> T (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1256
FT /note="G -> V (in Ref. 2; AAK11735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1464 AA; 163237 MW; 62B0FE0FE298EE24 CRC64;
MSNSLGNNLL YQGFLTSTVL EHKSRISPPC VGGNSLFQQQ VISKSPLSTE FRGNRLKVQK
KKIPMEKKRA FSSSPHAVLT TDTSSELAEK FSLGGNIELQ VDVRPPTSGD VSFVDFQVTN
GSDKLFLHWG AVKFGKETWS LPNDRPDGTK VYKNKALRTP FVKSGSNSIL RLEIRDTAIE
AIEFLIYDEA HDKWIKNNGG NFRVKLSRKE IRGPDVSVPE ELVQIQSYLR WERKGKQNYP
PEKEKEEYEA ARTVLQEEIA RGASIQDIRA RLTKTNDKSQ SKEEPLHVTK SDIPDDLAQA
QAYIRWEKAG KPNYPPEKQI EELEEARREL QLELEKGITL DELRKTITKG EIKTKVEKHL
KRSSFAVERI QRKKRDFGHL INKYTSSPAV QVQKVLEEPP ALSKIKLYAK EKEEQIDDPI
LNKKIFKVDD GELLVLVAKS SGKTKVHLAT DLNQPITLHW ALSKSPGEWM VPPSSILPPG
SIILDKAAET PFSASSSDGL TSKVQSLDIV IEDGNFVGMP FVLLSGEKWI KNQGSDFYVG
FSAASKLALK AAGDGSGTAK SLLDKIADME SEAQKSFMHR FNIAADLIED ATSAGELGFA
GILVWMRFMA TRQLIWNKNY NVKPREISKA QDRLTDLLQN AFTSHPQYRE ILRMIMSTVG
RGGEGDVGQR IRDEILVIQR NNDCKGGMMQ EWHQKLHNNT SPDDVVICQA LIDYIKSDFD
LGVYWKTLNE NGITKERLLS YDRAIHSEPN FRGDQKGGLL RDLGHYMRTL KAVHSGADLE
SAIANCMGYK TEGEGFMVGV QINPVSGLPS GFQDLLHFVL DHVEDKNVET LLERLLEARE
ELRPLLLKPN NRLKDLLFLD IALDSTVRTA VERGYEELNN ANPEKIMYFI SLVLENLALS
VDDNEDLVYC LKGWNQALSM SNGGDNHWAL FAKAVLDRTR LALASKAEWY HHLLQPSAEY
LGSILGVDQW ALNIFTEEII RAGSAASLSS LLNRLDPVLR KTANLGSWQI ISPVEAVGYV
VVVDELLSVQ NEIYEKPTIL VAKSVKGEEE IPDGAVALIT PDMPDVLSHV SVRARNGKVC
FATCFDPNIL ADLQAKEGRI LLLKPTPSDI IYSEVNEIEL QSSSNLVEAE TSATLRLVKK
QFGGCYAISA DEFTSEMVGA KSRNIAYLKG KVPSSVGIPT SVALPFGVFE KVLSDDINQG
VAKELQILMK KLSEGDFSAL GEIRTTVLDL SAPAQLVKEL KEKMQGSGMP WPGDEGPKRW
EQAWMAIKKV WASKWNERAY FSTRKVKLDH DYLCMAVLVQ EIINADYAFV IHTTNPSSGD
DSEIYAEVVR GLGETLVGAY PGRALSFICK KKDLNSPQVL GYPSKPIGLF IKRSIIFRSD
SNGEDLEGYA GAGLYDSVPM DEEEKVVIDY SSDPLITDGN FRQTILSNIA RAGHAIEELY
GSPQDIEGVV RDGKIYVVQT RPQM
