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GLGL4_ORYSJ
ID   GLGL4_ORYSJ             Reviewed;         509 AA.
AC   Q0D7I3; Q8GRM4;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit 4, chloroplastic/amyloplastic {ECO:0000305};
DE            Short=OsAGPL4 {ECO:0000303|PubMed:17406793};
DE            Short=OsAPL4 {ECO:0000303|PubMed:15821022};
DE            EC=2.7.7.27 {ECO:0000305|PubMed:17406793};
DE   AltName: Full=ADP-glucose pyrophosphorylase AGPL4 {ECO:0000305};
DE   AltName: Full=ADP-glucose synthase AGPL4 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=AGPL4 {ECO:0000303|PubMed:17406793};
GN   Synonyms=APL4 {ECO:0000303|PubMed:15821022};
GN   OrderedLocusNames=Os07g0243200 {ECO:0000312|EMBL:BAF21190.1},
GN   LOC_Os07g13980 {ECO:0000305};
GN   ORFNames=OJ1341_A08.119 {ECO:0000312|EMBL:BAD30207.1},
GN   P0418E08.141 {ECO:0000312|EMBL:BAC16096.1};
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=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   [2]
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   [3]
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [5]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=15821022; DOI=10.1093/pcp/pci101;
RA   Akihiro T., Mizuno K., Fujimura T.;
RT   "Gene expression of ADP-glucose pyrophosphorylase and starch contents in
RT   rice cultured cells are cooperatively regulated by sucrose and ABA.";
RL   Plant Cell Physiol. 46:937-946(2005).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=17406793; DOI=10.1007/s11103-007-9153-z;
RA   Lee S.K., Hwang S.K., Han M., Eom J.S., Kang H.G., Han Y., Choi S.B.,
RA   Cho M.H., Bhoo S.H., An G., Hahn T.R., Okita T.W., Jeon J.S.;
RT   "Identification of the ADP-glucose pyrophosphorylase isoforms essential for
RT   starch synthesis in the leaf and seed endosperm of rice (Oryza sativa
RT   L.).";
RL   Plant Mol. Biol. 65:531-546(2007).
CC   -!- FUNCTION: Involved in synthesis of starch. Catalyzes the synthesis of
CC       ADP-glucose, a molecule that serves as an activated glycosyl donor for
CC       alpha-1,4-glucan synthesis. Essential for starch synthesis in leaf
CC       chloroplasts. {ECO:0000305|PubMed:17406793}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose
CC         + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498,
CC         ChEBI:CHEBI:58601; EC=2.7.7.27;
CC         Evidence={ECO:0000305|PubMed:17406793};
CC   -!- ACTIVITY REGULATION: Activated by 3'phosphoglycerate, inhibited by
CC       orthophosphate. Allosteric regulation. {ECO:0000305|PubMed:17406793}.
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}.
CC   -!- SUBUNIT: Heterotetramer composed of two small and two large subunits.
CC       {ECO:0000305|PubMed:17406793}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:17406793}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves and stems.
CC       {ECO:0000269|PubMed:15821022}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in developing seeds from 1 to 20 days
CC       after flowering (DAF). {ECO:0000269|PubMed:15821022}.
CC   -!- INDUCTION: Induced by sucrose and glucose.
CC       {ECO:0000269|PubMed:15821022}.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC16096.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAD30207.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP004382; BAC16096.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP003754; BAD30207.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008213; BAF21190.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT00789.1; -; Genomic_DNA.
DR   EMBL; AK121036; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015645226.1; XM_015789740.1.
DR   AlphaFoldDB; Q0D7I3; -.
DR   SMR; Q0D7I3; -.
DR   STRING; 4530.OS07T0243200-01; -.
DR   PaxDb; Q0D7I3; -.
DR   PRIDE; Q0D7I3; -.
DR   EnsemblPlants; Os07t0243200-01; Os07t0243200-01; Os07g0243200.
DR   GeneID; 4342819; -.
DR   Gramene; Os07t0243200-01; Os07t0243200-01; Os07g0243200.
DR   KEGG; osa:4342819; -.
DR   eggNOG; KOG1322; Eukaryota.
DR   HOGENOM; CLU_029499_14_4_1; -.
DR   InParanoid; Q0D7I3; -.
DR   OMA; QKHLRDG; -.
DR   OrthoDB; 806744at2759; -.
DR   PlantReactome; R-OSA-1119477; Starch biosynthesis.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR011831; ADP-Glc_PPase.
DR   InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   PANTHER; PTHR43523; PTHR43523; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR02091; glgC; 1.
DR   PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1.
DR   PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR   PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Chloroplast; Nucleotide-binding;
KW   Nucleotidyltransferase; Plastid; Reference proteome; Starch biosynthesis;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..36
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..509
FT                   /note="Glucose-1-phosphate adenylyltransferase large
FT                   subunit 4, chloroplastic/amyloplastic"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000441127"
SQ   SEQUENCE   509 AA;  55829 MW;  0B4CF62DD102E613 CRC64;
     MATCSWAATT AAAAPPRPPA RCRSRVAALR RTAAASAAAA SCVLAEAPKG LKVEQADAVE
     PAAAAAARRD VGPDTVASII LGGGAGTRLF PLTRTRAKPA VPVGGCYRLI DIPMSNCINS
     KINKIYVLTQ FNSQSLNRHI ARTYNIGEGV GFGDGFVEVL AATQTTGESG KRWFQGTADA
     VRQFLWLFED ARLKRIENIL ILSGDHLYRM DYMDFVQKHV DKGADISVAC VPVDESRASD
     FGLMKTDKNG RITDFLEKPK DESLKSMQLD MGTFGLRPEV ADTCKYMASM GIYVFRTDIL
     LRLLRGHYPT ANDFGSEVIP MAAKDYNVQA YLFDGYWEDI GTIKSFFEAN LALTDQSPNF
     YFYDPVKPIF TSPRFLPPTK VENCKVLNSI VSHGCFLTEC SVDRSVIGVR SRLEPGVQLK
     DTMMMGADYY QTEAERFSEL SDGKVPVGVG ENTIIRNCII DKNARIGKNV MIMNSQNVQE
     AERPLEGFYI RSGITVVLKN AVIPDGTVI
 
 
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