ID   GWD1_CITRE              Reviewed;        1475 AA.
AC   Q8LPT9;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Alpha-glucan water dikinase, chloroplastic;
DE            EC=2.7.9.4;
DE   AltName: Full=Starch-related protein R1;
DE   Flags: Precursor;
GN   Name=R1;
OS   Citrus reticulata (Tangerine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=85571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   PubMed=12721844; DOI=10.1007/s00425-002-0963-6;
RA   Li C.Y., Weiss D., Goldschmidt E.E.;
RT   "Effects of carbohydrate starvation on gene expression in citrus root.";
RL   Planta 217:11-20(2003).
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 (By similarity). {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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Note=Starch granules.
CC   -!- INDUCTION: Down-regulated upon carbohydrate starvation.
CC       {ECO:0000269|PubMed:12721844}.
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 N-terminal domain (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR   EMBL; AY094062; AAM18228.1; -; mRNA.
DR   AlphaFoldDB; Q8LPT9; -.
DR   CAZy; CBM45; Carbohydrate-Binding Module Family 45.
DR   PRIDE; Q8LPT9; -.
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: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; -; 2.
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; Chloroplast; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Plastid; Transferase; Transit peptide.
FT   TRANSIT         1..85
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           86..1475
FT                   /note="Alpha-glucan water dikinase, chloroplastic"
FT                   /id="PRO_0000023566"
FT   ACT_SITE        1077
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1475 AA;  164767 MW;  0EC3073D8143D23A CRC64;
     MSNSIGRNVL HQSLLCSTVF EHQSNRHSSG IPANSLFQAV SINQPAGASA ARKSPLSTKF
     YGTSLNARPK MAMGRHRPVL ITPRAVLAVD SASELAGKFN LEGNVELQIT VGAPTPGSLT
     QVNIEISYSS NSLLLHWGAI RDKKEKWVLP SRPPDGTKIL KNRALRTPFV SSGSKSLVKL
     EIDDPAIEAV EFLILDEAQN KWFKNNGANF HVKLPSERSL IQNVSVPEDL VQTQAYLRWE
     RKGKQIYTPE QEKEEYEAAR TELLEEIVRG TSVEDLRAKL TNKNDRQEIK ESSSHGTKNA
     IPDDLVQIQS YIRWERAGKP NYSADQQLRE FEEARKELQS ELEKGISLDE IWKKITKGEI
     QTKVSDQLKT KKYFRTERIQ RKQRDFMQIL NKHVAEPTEK KNISVEPKAL TPVELFVGAT
     EEQEGDSILN KKIYKLAGKE LLVLVHKPGG KTKIHLATDG KEPLILHWAL SKKAGEWLAP
     PPSVLPAGSV LLSGSVETTF TTSSLADLPY QVQSIEIEIE EEGYVGMPSV LQSGGNWIKN
     KGSDFYVDFS YESKQVQQDF GDGKGTAKAL LEKIAGLEIE AQKSFMHRFN IAADLIQEAK
     EAGELGFAGI LVWMRFMATR QLIWNKNYNV KPREISKAQD RLTDLLQNVY ISNPEYREIV
     RMILSTVGRG GEGDVGQRIR DEILVIQRNN NCKGGMMEEW HQKLHNNTSP DDVIICQALI
     DYIKSDFDIS AYWKTLNDNG ITKERLLSYD RAIHSEPNFR RDQKDGLLRD LGNYMRTLKA
     VHSGADLESA ITNCLGYRSE GQGFMVGVQI NPIPNLPSGF PELLQFVSEH VEDRNVEALL
     EGLLEARQEI RPLLCKHNDR LKDLLFLDIA LESSVRTAIE KGYEELNEAG PEKIMYFVSL
     ILENLALSLD DNEDLIYCLK GWSNALSMSK SKSDNWALFA KSVLDRTRLA LAGKADWYQK
     VLQPSAEYLG TLLSVDKWAV DIFTEEMIRA GSAAALSLLL NRLDPVLRKT ASLGSWQVIS
     PVEVFGYVAV VDELLAVQDK SYDQPTILLA RRVKGEEEIP HGTVAVLTAD MPDVLSHVSV
     RARNCKVCFA TCFDPNILAD LQSNEGKMLH LKPTSADIAY SVVEGSELQD SSSANLKEED
     GPSSSVALVK KQFAGRYAIT SDEFTGELVG AKSRNIAYLK GKVPSWIGIP TSVALPFGVF
     EKVLSDDINQ AVAEKLQILK QKLGEEDHSA LREIRETVLQ MKAPNQLVQE LKTEMKSSGM
     PWPGDEGEQR WEQAWMAIKK VWASKWNERA FFSTRRVKLD HEYLCMAVLV QEIINADYAF
     VIHTTNPSSG DSSEIYAEVV KGLGETLVGA YPGRALSFVC KKNDLKSPRV LGYPSKPIGL
     FIRRSIIFRS DSNGEDLEGY AGAGLYDSVP MDEAEKVVLD YSSDHLITDG HFQQSILSSI
     ARAGCEIEEL FGSAQDIEGV VRDGKIYVVQ TRPQM