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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)DescriptionActionsGraphical viewLength
    Active sitei1069Tele-phosphohistidine intermediate2 Publications1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi1069H → A: Loss of activity, no autophosphorylation. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 77Chloroplast2 PublicationsAdd BLAST77
    ChainiPRO_000002356778 – 1464Alpha-glucan water dikinase, chloroplasticAdd BLAST1387

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti66E → G (PubMed:11841813).Curated1
    Sequence conflicti68K → N (PubMed:11841813).Curated1
    Sequence conflicti86E → Q in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti86E → Q AA sequence (PubMed:15361065).Curated1
    Sequence conflicti94G → E in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti198N → I in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti203 – 204RV → HI in AAK11735 (PubMed:11841813).Curated2
    Sequence conflicti240P → T in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti254V → E in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti292D → N in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti346T → K in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti353K → E in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti379H → Q in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti385T → P in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti400P → A in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti400Missing AA sequence (PubMed:15361065).Curated1
    Sequence conflicti438A → S in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti540G → D in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti547L → S in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti588I → M in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti681N → K in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti690Q → E in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti768R → K in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti1129A → V in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti1129A → V AA sequence (PubMed:15361065).Curated1
    Sequence conflicti1209M → T in AAK11735 (PubMed:11841813).Curated1
    Sequence conflicti1256G → V in AAK11735 (PubMed:11841813).Curated1

    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...

    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.