ID PWD_ORYSJ Reviewed; 1206 AA.
AC Q2QTC2; Q0INT3;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 24-JAN-2024, entry version 109.
DE RecName: Full=Phosphoglucan, water dikinase, chloroplastic;
DE EC=2.7.9.5;
DE Flags: Precursor;
GN Name=GWD3; Synonyms=PWD; OrderedLocusNames=Os12g0297500, LOC_Os12g20150;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: Mediates the incorporation of phosphate into starch-like
CC phospho-alpha-glucan, mostly at the C-3 position of glucose units. May
CC be required for starch degradation, suggesting that the phosphate
CC content of starch regulates its degradability (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-6-phospho-alpha-D-glucosyl](n) + n ATP + n H2O =
CC [(1->4)-3,6-bisphospho-alpha-D-glucosyl](n) + n AMP + 2n H(+) + n
CC phosphate; Xref=Rhea:RHEA:10256, Rhea:RHEA-COMP:12983, Rhea:RHEA-
CC COMP:14598, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:134068, ChEBI:CHEBI:140561,
CC ChEBI:CHEBI:456215; EC=2.7.9.5;
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 during
CC starch mobilization in darkness. {ECO:0000250}.
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; DP000011; ABA97816.2; -; Genomic_DNA.
DR EMBL; AP008218; BAF29632.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT16806.1; -; Genomic_DNA.
DR RefSeq; XP_015620009.1; XM_015764523.1.
DR AlphaFoldDB; Q2QTC2; -.
DR SMR; Q2QTC2; -.
DR BioGRID; 821065; 1.
DR STRING; 39947.Q2QTC2; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR PaxDb; 39947-Q2QTC2; -.
DR EnsemblPlants; Os12t0297500-01; Os12t0297500-01; Os12g0297500.
DR GeneID; 4352028; -.
DR Gramene; Os12t0297500-01; Os12t0297500-01; Os12g0297500.
DR KEGG; osa:4352028; -.
DR eggNOG; ENOG502QS3J; Eukaryota.
DR HOGENOM; CLU_012115_0_0_1; -.
DR InParanoid; Q2QTC2; -.
DR OMA; WRLCEIS; -.
DR OrthoDB; 19923at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR ExpressionAtlas; Q2QTC2; baseline and differential.
DR Genevisible; Q2QTC2; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102217; F:6-phosphoglucan, water dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102219; F:phosphogluco-amylopectin water dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05818; CBM20_water_dikinase; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR034848; CBM20_water_dikinase.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR47453; PHOSPHOGLUCAN, WATER DIKINASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47453:SF1; PHOSPHOGLUCAN, WATER DIKINASE, CHLOROPLASTIC; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Chloroplast; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..1206
FT /note="Phosphoglucan, water dikinase, chloroplastic"
FT /id="PRO_0000240251"
FT DOMAIN 67..168
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 776
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1206 AA; 132895 MW; 92A1E4D4CFBD54B5 CRC64;
MTSLRPLETS LSIGGRPRRG LVLPPPGVGA GVLLRRGAMA LPGRRGFACR GRSAASAAER
TKEKKRRDSS KQPLVHLQVC LEHQVKFGEH VGIIGSTKEL GSWEEQVELE WTTNGWVCQL
KLPGETLVEF KFVIFLVGGK DKIWEDGNNR VVELPKDGKF DIVCHWNRTE EPLELLGTPK
FELVGEAEKN TGEDASASVT FAPEKVQDIS VVENGDPAPE AESSKFGGQW QGSKTVFMRS
NEHLNKEADR MWDTTGLDGI ALKLVEGDKA SRNWWRKLEV VRGILSESFD DQSRLGALVY
SAIYLKWIYT GQISCFEDGG HHRPNKHAEI SRQIFRELEM MYYGKTTSAK DVLVIRKIHP
FLPSFKSEFT ASVPLTRIRD IAHRNDIPHD LKQEIKHTIQ NKLHRNAGPE DLIATEVMLA
RITKTPGEYS ETFVEQFTIF YSELKDFFNA GSLFEQLESI KESLNESGLE VLSSFVETKR
SLDQVDHAED LDKNDTIQIL MTTLQSLSSL RSVLMKGLES GLRNDAPDNA IAMRQKWRLC
EISLEDYSFV LLSRFINTLE ALGGSASLAK DVARNTTLWD TTLDALVIGI NQVSFSGWKT
DECIAIGNEI LSWKQKGLSE SEGCEDGKYI WSLRLKATLD RARRLTEEYS EALLSIFPEK
VMVIGKALGI PDNSVRTYTE AEIRAGIVFQ VSKLCTVLQK AIREVLGSTG WDVLVPGVAH
GTLMRVERIL PGSLPSSVKE PVVLIVDKAD GDEEVKAAGD NIVGVILLQE LPHLSHLGVR
ARQENVVFVT CEYDDTVTDV YLLEGKYIRL EASSINVNLS IVSEKNDNAV STEPNSTGNP
FQQKLQNEFS LPSDIEMPLQ MSKQKSKSGV NGSFAALELS EASVESAGAK AAACRTLSVL
ASLSNKVYSD QGVPAAFRVP SGAVIPFGSM EDALKKSGSL ESFTSLLEKI ETAKVENGEV
DSLALELQAI ISHLSPPEET IIFLKRIFPQ DVRLIVRSSA NVEDLAGMSA AGLYDSIPNV
SLMDPCAFGA AVGKVWASLY TRRAILSRRA AGVYQRDATM AVLVQEILQP DLSFVLHTVC
PADHDPKVVQ AEVAPGLGET LASGTRGTPW RLSCNKFDGK VATLAFSNFS EEMVVHNSGP
ANGEVIRLTV DYSKKPLSVD TTFRKQFGQR LAAIGQYLEQ KFGSAQDVEG CLVGKDIFIV
QSRPQP
//
