GLGS_SOLTU
ID GLGS_SOLTU Reviewed; 521 AA.
AC P23509;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic/amyloplastic;
DE EC=2.7.7.27;
DE AltName: Full=ADP-glucose pyrophosphorylase;
DE AltName: Full=ADP-glucose synthase;
DE AltName: Full=AGPase B;
DE AltName: Full=Alpha-D-glucose-1-phosphate adenyl transferase;
DE Flags: Precursor;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Russet Burbank-0; TISSUE=Tuber;
RX PubMed=1657244; DOI=10.1007/bf00037149;
RA Nakata P.A., Greene T.W., Anderson J.M., Smith-White B.J., Okita T.W.,
RA Preiss J.;
RT "Comparison of the primary sequences of two potato tuber ADP-glucose
RT pyrophosphorylase subunits.";
RL Plant Mol. Biol. 17:1089-1093(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Russet Burbank-0; TISSUE=Leaf;
RX PubMed=7983010; DOI=10.1016/s0021-9258(18)47352-8;
RA Nakata P.A., Anderson J.M., Okita T.W.;
RT "Structure and expression of the potato ADP-glucose pyrophosphorylase small
RT subunit.";
RL J. Biol. Chem. 269:30798-30807(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-521.
RC STRAIN=cv. Desiree; TISSUE=Tuber;
RX PubMed=1654156; DOI=10.1007/bf00020568;
RA du Jardin P., Berhin A.;
RT "Isolation and sequence analysis of a cDNA clone encoding a subunit of the
RT ADP-glucose pyrophosphorylase of potato tuber amyloplasts.";
RL Plant Mol. Biol. 16:349-351(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 80-521.
RC STRAIN=cv. Desiree;
RX PubMed=1703626; DOI=10.1007/bf00259460;
RA Mueller-Roeber B.T., Kossmann J., Hannah L.C., Willmitzer L., Sonnewald U.;
RT "One of two different ADP-glucose pyrophosphorylase genes from potato
RT responds strongly to elevated levels of sucrose.";
RL Mol. Gen. Genet. 224:136-146(1990).
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 -!- INTERACTION:
CC P23509; Q00081: AGPS1; NbExp=2; IntAct=EBI-15812097, EBI-15812120;
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: Leaves and tubers.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; X61186; CAA43489.1; -; mRNA.
DR EMBL; L36648; AAA66057.1; -; Genomic_DNA.
DR EMBL; X55650; CAA39181.1; -; mRNA.
DR EMBL; X55155; CAA38954.1; -; mRNA.
DR PIR; A55317; A55317.
DR PIR; S13380; S13380.
DR PDB; 1YP2; X-ray; 2.11 A; A/B/C/D=72-521.
DR PDB; 1YP3; X-ray; 2.60 A; A/B/C/D=72-521.
DR PDB; 1YP4; X-ray; 2.30 A; A/B/C/D=72-521.
DR PDBsum; 1YP2; -.
DR PDBsum; 1YP3; -.
DR PDBsum; 1YP4; -.
DR AlphaFoldDB; P23509; -.
DR SMR; P23509; -.
DR DIP; DIP-48347N; -.
DR IntAct; P23509; 1.
DR STRING; 4113.PGSC0003DMT400079823; -.
DR eggNOG; KOG1322; Eukaryota.
DR BRENDA; 2.7.7.27; 5757.
DR SABIO-RK; P23509; -.
DR UniPathway; UPA00152; -.
DR EvolutionaryTrace; P23509; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P23509; 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 3D-structure; Allosteric enzyme; Amyloplast; ATP-binding; Chloroplast;
KW Nucleotide-binding; Nucleotidyltransferase; Plastid; Reference proteome;
KW Starch biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 73..521
FT /note="Glucose-1-phosphate adenylyltransferase small
FT subunit, chloroplastic/amyloplastic"
FT /id="PRO_0000011155"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..454
FT /note="Allosteric regulation"
FT /evidence="ECO:0000250"
FT COMPBIAS 7..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT VARIANT 520
FT /note="I -> V"
FT CONFLICT 185
FT /note="D -> H (in Ref. 3; CAA39181)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="P -> S (in Ref. 3; CAA39181)"
FT /evidence="ECO:0000305"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1YP2"
FT TURN 105..110
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1YP2"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1YP3"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 296..306
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:1YP2"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 328..334
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 391..403
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 408..416
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 445..452
FT /evidence="ECO:0007829|PDB:1YP2"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 466..472
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:1YP2"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:1YP2"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:1YP2"
SQ SEQUENCE 521 AA; 57240 MW; 2A30929D1CF7E88C CRC64;
MAASIGALKS SPSSNNCINE RRNDSTRAVS SRNLSFSSSH LAGDKLMPVS SLRSQGVRFN
VRRSPMIVSP KAVSDSQNSQ TCLDPDASRS VLGIILGGGA GTRLYPLTKK RAKPAVPLGA
NYRLIDIPVS NCLNSNISKI YVLTQFNSAS LNRHLSRAYA SNMGGYKNEG FVEVLAAQQS
PENPDWFQGT ADAVRQYLWL FEEHTVLEYL ILAGDHLYRM DYEKFIQAHR ETDADITVAA
LPMDEKRATA FGLMKIDEEG RIIEFAEKPQ GEQLQAMKVD TTILGLDDKR AKEMPFIASM
GIYVISKDVM LNLLRDKFPG ANDFGSEVIP GATSLGMRVQ AYLYDGYWED IGTIEAFYNA
NLGITKKPVP DFSFYDRSAP IYTQPRYLPP SKMLDADVTD SVIGEGCVIK NCKIHHSVVG
LRSCISEGAI IEDSLLMGAD YYETDADRKL LAAKGSVPIG IGKNCHIKRA IIDKNARIGD
NVKIINKDNV QEAARETDGY FIKSGIVTVI KDALIPSGII I
