P23509 (GLGS_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic/amyloplastic EC=2.7.7.27 Alternative name(s): ADP-glucose pyrophosphorylase ADP-glucose synthase AGPase B Alpha-D-glucose-1-phosphate adenyl transferase
Organism	Solanum tuberosum (Potato)
Taxonomic identifier	4113 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	521 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Catalytic activity	ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-glucose.
Enzyme regulation	Activated by 3'phosphoglycerate, inhibited by orthophosphate. Allosteric regulation.
Pathway	Glycan biosynthesis; starch biosynthesis.
Subunit structure	Heterotetramer.
Subcellular location	Plastid › chloroplast. Plastid › amyloplast. Note: Found in the chloroplast in leaf. Found in the plastid in the developing endosperm.
Tissue specificity	Leaves and tubers.
Sequence similarities	Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.

Ontologies

Keywords
Biological process	Starch biosynthesis
Cellular component	Amyloplast Chloroplast Plastid
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Allosteric enzyme
Gene Ontology (GO)
Biological process	glycogen biosynthetic process Inferred from electronic annotation. Source: InterPro starch biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	amyloplast Inferred from electronic annotation. Source: UniProtKB-SubCell chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glucose-1-phosphate adenylyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 72

72

Chloroplast Potential

Chain

73 – 521

449

Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic/amyloplastic

PRO_0000011155

Regions

Region

444 – 454

11

Allosteric regulation By similarity

Sites

Binding site

268

1

Substrate Potential

Natural variations

Natural variant

520

1

I → V.

Experimental info

Sequence conflict

185

1

D → H in CAA39181. Ref.3

Sequence conflict

390

1

P → S in CAA39181. Ref.3

Secondary structure

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521

Helix Strand Turn

Details...

Helix

87 – 90

4

Beta strand

91 – 96

6

Turn

105 – 110

6

Helix

113 – 115

3

Turn

119 – 121

3

Helix

126 – 134

9

Beta strand

139 – 145

7

Helix

149 – 158

10

Beta strand

171 – 177

7

Helix

190 – 196

7

Helix

198 – 201

4

Beta strand

207 – 214

8

Helix

222 – 231

10

Beta strand

235 – 243

9

Helix

245 – 248

4

Beta strand

251 – 256

6

Beta strand

260 – 268

9

Helix

271 – 276

6

Helix

281 – 284

4

Helix

288 – 293

6

Beta strand

296 – 306

11

Helix

307 – 315

9

Turn

324 – 327

4

Helix

328 – 334

7

Beta strand

339 – 343

5

Helix

354 – 362

9

Helix

363 – 365

3

Beta strand

367 – 369

3

Beta strand

377 – 379

3

Beta strand

391 – 403

13

Beta strand

408 – 416

9

Beta strand

430 – 433

4

Helix

445 – 452

8

Turn

453 – 455

3

Beta strand

459 – 461

3

Beta strand

466 – 472

7

Beta strand

493 – 495

3

Helix

496 – 498

3

Beta strand

500 – 503

4

Beta strand

506 – 509

4

Sequences

	Sequence		Length	Mass (Da)
	P23509 [UniParc]. Last modified April 1, 1993. Version 2. Checksum: 2A30929D1CF7E88C	FASTA	521	57,240
	10 20 30 40 50 60 MAASIGALKS SPSSNNCINE RRNDSTRAVS SRNLSFSSSH LAGDKLMPVS SLRSQGVRFN 70 80 90 100 110 120 VRRSPMIVSP KAVSDSQNSQ TCLDPDASRS VLGIILGGGA GTRLYPLTKK RAKPAVPLGA 130 140 150 160 170 180 NYRLIDIPVS NCLNSNISKI YVLTQFNSAS LNRHLSRAYA SNMGGYKNEG FVEVLAAQQS 190 200 210 220 230 240 PENPDWFQGT ADAVRQYLWL FEEHTVLEYL ILAGDHLYRM DYEKFIQAHR ETDADITVAA 250 260 270 280 290 300 LPMDEKRATA FGLMKIDEEG RIIEFAEKPQ GEQLQAMKVD TTILGLDDKR AKEMPFIASM 310 320 330 340 350 360 GIYVISKDVM LNLLRDKFPG ANDFGSEVIP GATSLGMRVQ AYLYDGYWED IGTIEAFYNA 370 380 390 400 410 420 NLGITKKPVP DFSFYDRSAP IYTQPRYLPP SKMLDADVTD SVIGEGCVIK NCKIHHSVVG 430 440 450 460 470 480 LRSCISEGAI IEDSLLMGAD YYETDADRKL LAAKGSVPIG IGKNCHIKRA IIDKNARIGD 490 500 510 520 NVKIINKDNV QEAARETDGY FIKSGIVTVI KDALIPSGII I

References

[1]	"Comparison of the primary sequences of two potato tuber ADP-glucose pyrophosphorylase subunits." Nakata P.A., Greene T.W., Anderson J.M., Smith-White B.J., Okita T.W., Preiss J. Plant Mol. Biol. 17:1089-1093(1991) [PubMed: 1657244] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: cv. Russet Burbank-0. Tissue: Tuber.
[2]	"Structure and expression of the potato ADP-glucose pyrophosphorylase small subunit." Nakata P.A., Anderson J.M., Okita T.W. J. Biol. Chem. 269:30798-30807(1994) [PubMed: 7983010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Russet Burbank-0. Tissue: Leaf.
[3]	"Isolation and sequence analysis of a cDNA clone encoding a subunit of the ADP-glucose pyrophosphorylase of potato tuber amyloplasts." du Jardin P., Berhin A. Plant Mol. Biol. 16:349-351(1991) [PubMed: 1654156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 80-521. Strain: cv. Desiree. Tissue: Tuber.
[4]	"One of two different ADP-glucose pyrophosphorylase genes from potato responds strongly to elevated levels of sucrose." Mueller-Roeber B.T., Kossmann J., Hannah L.C., Willmitzer L., Sonnewald U. Mol. Gen. Genet. 224:136-146(1990) [PubMed: 1703626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 80-521. Strain: cv. Desiree.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X61186 mRNA. Translation: CAA43489.1.
L36648 Genomic DNA. Translation: AAA66057.1.
X55650 mRNA. Translation: CAA39181.1.
X55155 mRNA. Translation: CAA38954.1.

PIR

A55317.
S13380.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YP2	X-ray	2.11	A/B/C/D	72-521	[»]
1YP3	X-ray	2.60	A/B/C/D	72-521	[»]
1YP4	X-ray	2.30	A/B/C/D	72-521	[»]

ProteinModelPortal

P23509.

SMR

P23509. Positions 80-521.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48347N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

2.7.7.27. 5757.

Family and domain databases

InterPro

IPR005836. ADP_Glu_pyroP_CS.
IPR011831. GlgC.
IPR005835. NTP_transferase.
IPR011004. Trimer_LpxA-like.
[Graphical view]

Pfam

PF00483. NTP_transferase. 1 hit.
[Graphical view]

SUPFAM

SSF51161. Trimer_LpxA_like. 1 hit.

TIGRFAMs

TIGR02091. GlgC. 1 hit.

PROSITE

PS00808. ADP_GLC_PYROPHOSPH_1. 1 hit.
PS00809. ADP_GLC_PYROPHOSPH_2. 1 hit.
PS00810. ADP_GLC_PYROPHOSPH_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GLGS_SOLTU

Accession

Primary (citable) accession number: P23509

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	April 1, 1993
Last modified:	May 31, 2011
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program