GLGL1_MAIZE
ID GLGL1_MAIZE Reviewed; 516 AA.
AC P55241;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic/amyloplastic;
DE EC=2.7.7.27;
DE AltName: Full=ADP-glucose pyrophosphorylase;
DE AltName: Full=ADP-glucose synthase;
DE AltName: Full=AGPase S;
DE AltName: Full=Alpha-D-glucose-1-phosphate adenyl transferase;
DE AltName: Full=Shrunken-2;
DE Flags: Precursor;
GN Name=SH2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1967077; DOI=10.2307/3869119;
RA Bhave M.R., Lawrence S., Barton C., Hannah L.C.;
RT "Identification and molecular characterization of shrunken-2 cDNA clones of
RT maize.";
RL Plant Cell 2:581-588(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=cv. Black Mexican Sweet; TISSUE=Leaf;
RX PubMed=16668750; DOI=10.1104/pp.98.3.1214;
RA Hannah L.C., Shaw J.R.;
RT "Genomic nucleotide sequence of a wild-type shrunken-2 allele of Zea
RT mays.";
RL Plant Physiol. 98:1214-1216(1992).
RN [3]
RP CHARACTERIZATION.
RX PubMed=8202085; DOI=10.1007/bf00280470;
RA Giroux M.J., Hannah L.C.;
RT "ADP-glucose pyrophosphorylase in shrunken-2 and brittle-2 mutants of
RT maize.";
RL Mol. Gen. Genet. 243:400-408(1994).
CC -!- FUNCTION: This protein plays a role in synthesis of starch. It
CC catalyzes the synthesis of the activated glycosyl donor, ADP-glucose
CC from Glc-1-P and ATP.
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 -!- ACTIVITY REGULATION: Activated by 3'phosphoglycerate, inhibited by
CC orthophosphate. Allosteric regulation.
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC -!- SUBUNIT: Heterotetramer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC Note=Found in the chloroplast in leaf. Found in the plastid in the
CC developing endosperm.
CC -!- TISSUE SPECIFICITY: Endosperm.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB24191.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S48563; AAB24191.2; ALT_INIT; mRNA.
DR EMBL; M81603; AAB52952.1; -; Genomic_DNA.
DR PIR; JQ1005; JQ1005.
DR RefSeq; NP_001121104.1; NM_001127632.1.
DR AlphaFoldDB; P55241; -.
DR SMR; P55241; -.
DR STRING; 4577.GRMZM2G429899_P01; -.
DR PaxDb; P55241; -.
DR GeneID; 542761; -.
DR KEGG; zma:542761; -.
DR MaizeGDB; 85022; -.
DR eggNOG; KOG1322; Eukaryota.
DR OrthoDB; 806744at2759; -.
DR BRENDA; 2.7.7.27; 6752.
DR SABIO-RK; P55241; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P55241; baseline and differential.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
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; Amyloplast; ATP-binding; Chloroplast;
KW Nucleotide-binding; Nucleotidyltransferase; Plastid; Reference proteome;
KW Starch biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..516
FT /note="Glucose-1-phosphate adenylyltransferase large
FT subunit 1, chloroplastic/amyloplastic"
FT /id="PRO_0000011165"
FT CONFLICT 436
FT /note="T -> I (in Ref. 1; AAB24191)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="V -> I (in Ref. 1; AAB24191)"
FT /evidence="ECO:0000305"
FT CONFLICT 495..514
FT /note="Missing (in Ref. 1; AAB24191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 57071 MW; B9B517905C4B0705 CRC64;
MQFALALDTN SGPHQIRSCE GDGIDRLEKL SIGGRKQEKA LRNRCFGGRV AATTQCILTS
DACPETLHSQ TQSSRKNYAD ANRVSAIILG GGTGSQLFPL TSTRATPAVP VGGCYRLIDI
PMSNCFNSGI NKIFVMSQFN STSLNRHIHR TYLEGGINFA DGSVQVLAAT QMPEEPAGWF
QGTADSIRKF IWVLEDYYSH KSIDNIVILS GDQLYRMNYM ELVQKHVEDD ADITISCAPV
DESRASKNGL VKIDHTGRVL QFFEKPKGAD LNSMRVETNF LSYAIDDAQK YPYLASMGIY
VFKKDALLDL LKSKYTQLHD FGSEILPRAV LDHSVQACIF TGYWEDVGTI KSFFDANLAL
TEQPSKFDFY DPKTPFFTAP RCLPPTQLDK CKMKYAFISD GCLLRECNIE HSVIGVCSRV
SSGCELKDSV MMGADTYETE EEASKLLLAG KVPVGIGRNT KIRNCIIDMN ARIGKNVVIT
NSKGIQEADH PEEGYYIRSG IVVILKNATI NDGSVI
