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Protein

Alpha-glucan water dikinase, chloroplastic

Gene

R1

Organism
Solanum tuberosum (Potato)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates the incorporation of phosphate into starch-like alpha-glucan, mostly at the C-6 position of glucose units. Acts as an overall regulator of starch mobilization. Required for starch degradation, suggesting that the phosphate content of starch regulates its degradability. More active on alpha-1,6 branched amylopectin.3 Publications

Catalytic activityi

ATP + alpha-glucan + H2O = AMP + phospho-alpha-glucan + phosphate.1 Publication
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.1 Publication

Cofactori

Mg2+1 Publication

Kineticsi

  1. KM=0.23 µM for ATP2 Publications
  2. KM=1.7 µM for amylopectin2 Publications

    pH dependencei

    Optimum pH is 7.2 Publications

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1069 – 10691Tele-phosphohistidine intermediate2 Publications

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.9.4. 5757.
    SABIO-RKQ9AWA5.

    Protein family/group databases

    CAZyiCBM45. Carbohydrate-Binding Module Family 45.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-glucan water dikinase, chloroplastic (EC:2.7.13.3, EC:2.7.9.4)
    Alternative name(s):
    Starch-related R1 protein
    Gene namesi
    Name:R1
    OrganismiSolanum tuberosum (Potato)
    Taxonomic identifieri4113 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
    Proteomesi
    • UP000011115 Componenti: Unassembled WGS sequence

    Subcellular locationi

    • Plastidchloroplast 2 Publications

    • Note: Starch granules. Binds to starch granules isolated from either illuminated or darkened leaves. However, binding to darkened leaves is more effective, suggesting that depending upon the metabolic state of the cells, the starch granule surface changes and thereby affects its binding.

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1069 – 10691H → A: Loss of activity, no autophosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 7777Chloroplast2 PublicationsAdd
    BLAST
    Chaini78 – 14641387Alpha-glucan water dikinase, chloroplasticPRO_0000023567Add
    BLAST

    Proteomic databases

    ProMEXiQ9AWA5.

    Expressioni

    Tissue specificityi

    Expressed in leaves.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi4113.PGSC0003DMT400019845.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9AWA5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The N-terminal domain contains the alpha-glucan binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the ATP binding site.

    Sequence similaritiesi

    Belongs to the PEP-utilizing enzyme family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiENOG410IHGM. Eukaryota.
    ENOG410XUE8. LUCA.
    InParanoidiQ9AWA5.
    KOiK08244.

    Family and domain databases

    Gene3Di3.30.1490.20. 2 hits.
    3.30.470.20. 1 hit.
    InterProiIPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR002192. PPDK_PEP-bd.
    [Graphical view]
    PfamiPF01326. PPDK_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9AWA5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSNSLGNNLL YQGFLTSTVL EHKSRISPPC VGGNSLFQQQ VISKSPLSTE
    60 70 80 90 100
    FRGNRLKVQK KKIPMEKKRA FSSSPHAVLT TDTSSELAEK FSLGGNIELQ
    110 120 130 140 150
    VDVRPPTSGD VSFVDFQVTN GSDKLFLHWG AVKFGKETWS LPNDRPDGTK
    160 170 180 190 200
    VYKNKALRTP FVKSGSNSIL RLEIRDTAIE AIEFLIYDEA HDKWIKNNGG
    210 220 230 240 250
    NFRVKLSRKE IRGPDVSVPE ELVQIQSYLR WERKGKQNYP PEKEKEEYEA
    260 270 280 290 300
    ARTVLQEEIA RGASIQDIRA RLTKTNDKSQ SKEEPLHVTK SDIPDDLAQA
    310 320 330 340 350
    QAYIRWEKAG KPNYPPEKQI EELEEARREL QLELEKGITL DELRKTITKG
    360 370 380 390 400
    EIKTKVEKHL KRSSFAVERI QRKKRDFGHL INKYTSSPAV QVQKVLEEPP
    410 420 430 440 450
    ALSKIKLYAK EKEEQIDDPI LNKKIFKVDD GELLVLVAKS SGKTKVHLAT
    460 470 480 490 500
    DLNQPITLHW ALSKSPGEWM VPPSSILPPG SIILDKAAET PFSASSSDGL
    510 520 530 540 550
    TSKVQSLDIV IEDGNFVGMP FVLLSGEKWI KNQGSDFYVG FSAASKLALK
    560 570 580 590 600
    AAGDGSGTAK SLLDKIADME SEAQKSFMHR FNIAADLIED ATSAGELGFA
    610 620 630 640 650
    GILVWMRFMA TRQLIWNKNY NVKPREISKA QDRLTDLLQN AFTSHPQYRE
    660 670 680 690 700
    ILRMIMSTVG RGGEGDVGQR IRDEILVIQR NNDCKGGMMQ EWHQKLHNNT
    710 720 730 740 750
    SPDDVVICQA LIDYIKSDFD LGVYWKTLNE NGITKERLLS YDRAIHSEPN
    760 770 780 790 800
    FRGDQKGGLL RDLGHYMRTL KAVHSGADLE SAIANCMGYK TEGEGFMVGV
    810 820 830 840 850
    QINPVSGLPS GFQDLLHFVL DHVEDKNVET LLERLLEARE ELRPLLLKPN
    860 870 880 890 900
    NRLKDLLFLD IALDSTVRTA VERGYEELNN ANPEKIMYFI SLVLENLALS
    910 920 930 940 950
    VDDNEDLVYC LKGWNQALSM SNGGDNHWAL FAKAVLDRTR LALASKAEWY
    960 970 980 990 1000
    HHLLQPSAEY LGSILGVDQW ALNIFTEEII RAGSAASLSS LLNRLDPVLR
    1010 1020 1030 1040 1050
    KTANLGSWQI ISPVEAVGYV VVVDELLSVQ NEIYEKPTIL VAKSVKGEEE
    1060 1070 1080 1090 1100
    IPDGAVALIT PDMPDVLSHV SVRARNGKVC FATCFDPNIL ADLQAKEGRI
    1110 1120 1130 1140 1150
    LLLKPTPSDI IYSEVNEIEL QSSSNLVEAE TSATLRLVKK QFGGCYAISA
    1160 1170 1180 1190 1200
    DEFTSEMVGA KSRNIAYLKG KVPSSVGIPT SVALPFGVFE KVLSDDINQG
    1210 1220 1230 1240 1250
    VAKELQILMK KLSEGDFSAL GEIRTTVLDL SAPAQLVKEL KEKMQGSGMP
    1260 1270 1280 1290 1300
    WPGDEGPKRW EQAWMAIKKV WASKWNERAY FSTRKVKLDH DYLCMAVLVQ
    1310 1320 1330 1340 1350
    EIINADYAFV IHTTNPSSGD DSEIYAEVVR GLGETLVGAY PGRALSFICK
    1360 1370 1380 1390 1400
    KKDLNSPQVL GYPSKPIGLF IKRSIIFRSD SNGEDLEGYA GAGLYDSVPM
    1410 1420 1430 1440 1450
    DEEEKVVIDY SSDPLITDGN FRQTILSNIA RAGHAIEELY GSPQDIEGVV
    1460
    RDGKIYVVQT RPQM
    Length:1,464
    Mass (Da):163,237
    Last modified:January 4, 2005 - v2
    Checksum:i62B0FE0FE298EE24
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661E → G (PubMed:11841813).Curated
    Sequence conflicti68 – 681K → N (PubMed:11841813).Curated
    Sequence conflicti86 – 861E → Q in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti86 – 861E → Q AA sequence (PubMed:15361065).Curated
    Sequence conflicti94 – 941G → E in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti198 – 1981N → I in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti203 – 2042RV → HI in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti240 – 2401P → T in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti254 – 2541V → E in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti292 – 2921D → N in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti346 – 3461T → K in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti353 – 3531K → E in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti379 – 3791H → Q in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti385 – 3851T → P in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti400 – 4001P → A in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti400 – 4001Missing AA sequence (PubMed:15361065).Curated
    Sequence conflicti438 – 4381A → S in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti540 – 5401G → D in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti547 – 5471L → S in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti588 – 5881I → M in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti681 – 6811N → K in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti690 – 6901Q → E in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti768 – 7681R → K in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti1129 – 11291A → V in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti1129 – 11291A → V AA sequence (PubMed:15361065).Curated
    Sequence conflicti1209 – 12091M → T in AAK11735 (PubMed:11841813).Curated
    Sequence conflicti1256 – 12561G → V in AAK11735 (PubMed:11841813).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y09533 mRNA. Translation: CAA70725.1.
    AY027522 mRNA. Translation: AAK11735.1.
    PIRiT07050.
    UniGeneiStu.2125.

    Genome annotation databases

    KEGGiag:CAA70725.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y09533 mRNA. Translation: CAA70725.1.
    AY027522 mRNA. Translation: AAK11735.1.
    PIRiT07050.
    UniGeneiStu.2125.

    3D structure databases

    ProteinModelPortaliQ9AWA5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi4113.PGSC0003DMT400019845.

    Protein family/group databases

    CAZyiCBM45. Carbohydrate-Binding Module Family 45.

    Proteomic databases

    ProMEXiQ9AWA5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:CAA70725.

    Phylogenomic databases

    eggNOGiENOG410IHGM. Eukaryota.
    ENOG410XUE8. LUCA.
    InParanoidiQ9AWA5.
    KOiK08244.

    Enzyme and pathway databases

    BRENDAi2.7.9.4. 5757.
    SABIO-RKQ9AWA5.

    Family and domain databases

    Gene3Di3.30.1490.20. 2 hits.
    3.30.470.20. 1 hit.
    InterProiIPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR002192. PPDK_PEP-bd.
    [Graphical view]
    PfamiPF01326. PPDK_N. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Inhibition of a starch-granule-bound protein leads to modified starch and repression of cold sweetening."
      Lorberth R., Ritte G., Willmitzer L., Kossmann J.
      Nat. Biotechnol. 16:473-477(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 78-91, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: cv. Desiree.
    2. "Production of highly phosphorylated glycopolymers by expression of R1 in Escherichia coli."
      Viksoe-Nielsen A., Chen P.-H.J., Larsson H., Blennow A., Moeller B.L.
      Carbohydr. Res. 337:327-333(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Strain: cv. Prevalent.
    3. "Functional domain organization of the potato alpha-glucan, water dikinase (GWD): evidence for separate site catalysis as revealed by limited proteolysis and deletion mutants."
      Mikkelsen R., Blennow A.
      Biochem. J. 385:355-361(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 78-86; 394-405; 614-622; 797-805; 1121-1130 AND 1132-1140, ACTIVE SITE HIS-1069, ENZYME MECHANISM.
    4. "Reversible binding of the starch-related R1 protein to the surface of transitory starch granules."
      Ritte G., Lorberth R., Steup M.
      Plant J. 21:387-391(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    5. Cited for: ENZYME ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Functional characterization of alpha-glucan, water dikinase, the starch phosphorylating enzyme."
      Mikkelsen R., Baunsgaard L., Blennow A.
      Biochem. J. 377:525-532(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE HIS-1069, MUTAGENESIS OF HIS-1069.

    Entry informationi

    Entry nameiGWD1_SOLTU
    AccessioniPrimary (citable) accession number: Q9AWA5
    Secondary accession number(s): O82061
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: January 4, 2005
    Last modified: April 13, 2016
    This is version 72 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the C-terminal domain, and the third partial reaction is catalyzed at an active site located on the N-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the C-terminal domain to that of the N-terminal domain.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.