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Protein

Glycogen synthase

Gene

glgA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Synthesizes alpha-1,4-glucan chains using ADP-glucose.

Catalytic activityi

ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP + (1,4-alpha-D-glucosyl)(n+1).

Pathway:iglycogen biosynthesis

This protein is involved in the pathway glycogen biosynthesis, which is part of Glycan biosynthesis.
View all proteins of this organism that are known to be involved in the pathway glycogen biosynthesis and in Glycan biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei15 – 151ADP-glucose

GO - Molecular functioni

  • starch synthase activity Source: EcoCyc

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • glycogen biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Glycogen biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:GLYCOGENSYN-MONOMER.
ECOL316407:JW3392-MONOMER.
MetaCyc:GLYCOGENSYN-MONOMER.
BRENDAi2.4.1.21. 2026.
UniPathwayiUPA00164.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen synthase (EC:2.4.1.21)
Alternative name(s):
Starch [bacterial glycogen] synthase
Gene namesi
Name:glgA
Ordered Locus Names:b3429, JW3392
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10377. glgA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 477477Glycogen synthasePRO_0000188611Add
BLAST

Proteomic databases

PaxDbiP0A6U8.
PRIDEiP0A6U8.

Interactioni

Protein-protein interaction databases

IntActiP0A6U8. 1 interaction.
STRINGi511145.b3429.

Structurei

Secondary structure

1
477
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Turni11 – 133Combined sources
Helixi18 – 3215Combined sources
Beta strandi36 – 427Combined sources
Helixi45 – 506Combined sources
Beta strandi55 – 606Combined sources
Beta strandi67 – 748Combined sources
Beta strandi77 – 837Combined sources
Helixi85 – 884Combined sources
Beta strandi91 – 933Combined sources
Beta strandi94 – 963Combined sources
Helixi106 – 12015Combined sources
Turni121 – 1233Combined sources
Beta strandi131 – 1366Combined sources
Helixi138 – 1403Combined sources
Helixi143 – 1497Combined sources
Beta strandi153 – 1619Combined sources
Beta strandi168 – 1703Combined sources
Helixi171 – 1755Combined sources
Turni176 – 1783Combined sources
Helixi181 – 1833Combined sources
Turni186 – 1894Combined sources
Beta strandi194 – 1963Combined sources
Helixi197 – 2048Combined sources
Beta strandi206 – 2127Combined sources
Helixi213 – 2186Combined sources
Helixi222 – 2254Combined sources
Helixi229 – 2379Combined sources
Beta strandi241 – 2433Combined sources
Turni250 – 2523Combined sources
Turni255 – 2573Combined sources
Beta strandi261 – 2633Combined sources
Helixi270 – 2734Combined sources
Helixi274 – 28411Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi294 – 3029Combined sources
Helixi303 – 3053Combined sources
Helixi307 – 31913Combined sources
Beta strandi323 – 3308Combined sources
Helixi332 – 34413Combined sources
Turni346 – 3483Combined sources
Beta strandi349 – 3546Combined sources
Helixi357 – 36610Combined sources
Beta strandi368 – 3725Combined sources
Helixi382 – 3898Combined sources
Beta strandi392 – 3987Combined sources
Helixi399 – 4046Combined sources
Helixi410 – 4145Combined sources
Beta strandi420 – 4234Combined sources
Beta strandi425 – 4273Combined sources
Helixi428 – 44215Combined sources
Helixi445 – 45713Combined sources
Helixi462 – 47615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QZSX-ray2.20A1-477[»]
2R4TX-ray2.26A1-477[»]
2R4UX-ray2.37A1-477[»]
3COPX-ray2.30A1-477[»]
3CX4X-ray2.29A1-477[»]
3D1JX-ray3.00A1-477[»]
3GUHX-ray2.79A1-477[»]
ProteinModelPortaliP0A6U8.
SMRiP0A6U8. Positions 1-477.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6U8.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0297.
HOGENOMiHOG000294941.
InParanoidiP0A6U8.
KOiK00703.
OMAiPFWRPDI.
OrthoDBiEOG6JTC6Z.
PhylomeDBiP0A6U8.

Family and domain databases

HAMAPiMF_00484. Glycogen_synth.
InterProiIPR001296. Glyco_trans_1.
IPR011835. GS/SS.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamiPF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02095. glgA. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6U8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVLHVCSEM FPLLKTGGLA DVIGALPAAQ IADGVDARVL LPAFPDIRRG
60 70 80 90 100
VTDAQVVSRR DTFAGHITLL FGHYNGVGIY LIDAPHLYDR PGSPYHDTNL
110 120 130 140 150
FAYTDNVLRF ALLGWVGAEM ASGLDPFWRP DVVHAHDWHA GLAPAYLAAR
160 170 180 190 200
GRPAKSVFTV HNLAYQGMFY AHHMNDIQLP WSFFNIHGLE FNGQISFLKA
210 220 230 240 250
GLYYADHITA VSPTYAREIT EPQFAYGMEG LLQQRHREGR LSGVLNGVDE
260 270 280 290 300
KIWSPETDLL LASRYTRDTL EDKAENKRQL QIAMGLKVDD KVPLFAVVSR
310 320 330 340 350
LTSQKGLDLV LEALPGLLEQ GGQLALLGAG DPVLQEGFLA AAAEYPGQVG
360 370 380 390 400
VQIGYHEAFS HRIMGGADVI LVPSRFEPCG LTQLYGLKYG TLPLVRRTGG
410 420 430 440 450
LADTVSDCSL ENLADGVASG FVFEDSNAWS LLRAIRRAFV LWSRPSLWRF
460 470
VQRQAMAMDF SWQVAAKSYR ELYYRLK
Length:477
Mass (Da):52,822
Last modified:March 29, 2005 - v1
Checksum:i177CF37F8C97CF42
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631F → S in AAA23870 (PubMed:3097003).Curated
Sequence conflicti102 – 1032AY → VH in AAA23870 (PubMed:3097003).Curated
Sequence conflicti245 – 2451L → P in AAA23870 (PubMed:3097003).Curated
Sequence conflicti280 – 2801L → S in AAA23870 (PubMed:3097003).Curated
Sequence conflicti286 – 2861L → S in AAA23870 (PubMed:3097003).Curated
Sequence conflicti309 – 3091L → S in AAA23870 (PubMed:3097003).Curated
Sequence conflicti314 – 3141L → S in AAA23870 (PubMed:3097003).Curated
Sequence conflicti317 – 3182LL → SS in AAA23870 (PubMed:3097003).Curated
Sequence conflicti387 – 3871L → S in AAA23870 (PubMed:3097003).Curated
Sequence conflicti419 – 4191S → N in AAA23870 (PubMed:3097003).Curated
Sequence conflicti422 – 4221V → I in AAA23870 (PubMed:3097003).Curated
Sequence conflicti434 – 4341A → T in AAA23870 (PubMed:3097003).Curated
Sequence conflicti444 – 4441R → C (PubMed:3097003).Curated
Sequence conflicti446 – 4461S → P (PubMed:3097003).Curated
Sequence conflicti461 – 4611S → G in AAA23870 (PubMed:3097003).Curated
Sequence conflicti476 – 4761L → S in AAA23870 (PubMed:3097003).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00281 Genomic DNA. Translation: CAA23545.1.
J02616 Genomic DNA. Translation: AAA23870.1.
U18997 Genomic DNA. Translation: AAA58227.1.
U00096 Genomic DNA. Translation: AAC76454.1.
AP009048 Genomic DNA. Translation: BAE77863.1.
J01616 Genomic DNA. Translation: AAA98737.1.
PIRiH65138. SYECGL.
RefSeqiNP_417887.1. NC_000913.3.
WP_001197646.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC76454; AAC76454; b3429.
BAE77863; BAE77863; BAE77863.
GeneIDi947932.
KEGGieco:b3429.
PATRICi32122298. VBIEscCol129921_3526.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00281 Genomic DNA. Translation: CAA23545.1.
J02616 Genomic DNA. Translation: AAA23870.1.
U18997 Genomic DNA. Translation: AAA58227.1.
U00096 Genomic DNA. Translation: AAC76454.1.
AP009048 Genomic DNA. Translation: BAE77863.1.
J01616 Genomic DNA. Translation: AAA98737.1.
PIRiH65138. SYECGL.
RefSeqiNP_417887.1. NC_000913.3.
WP_001197646.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QZSX-ray2.20A1-477[»]
2R4TX-ray2.26A1-477[»]
2R4UX-ray2.37A1-477[»]
3COPX-ray2.30A1-477[»]
3CX4X-ray2.29A1-477[»]
3D1JX-ray3.00A1-477[»]
3GUHX-ray2.79A1-477[»]
ProteinModelPortaliP0A6U8.
SMRiP0A6U8. Positions 1-477.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0A6U8. 1 interaction.
STRINGi511145.b3429.

Proteomic databases

PaxDbiP0A6U8.
PRIDEiP0A6U8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76454; AAC76454; b3429.
BAE77863; BAE77863; BAE77863.
GeneIDi947932.
KEGGieco:b3429.
PATRICi32122298. VBIEscCol129921_3526.

Organism-specific databases

EchoBASEiEB0372.
EcoGeneiEG10377. glgA.

Phylogenomic databases

eggNOGiCOG0297.
HOGENOMiHOG000294941.
InParanoidiP0A6U8.
KOiK00703.
OMAiPFWRPDI.
OrthoDBiEOG6JTC6Z.
PhylomeDBiP0A6U8.

Enzyme and pathway databases

UniPathwayiUPA00164.
BioCyciEcoCyc:GLYCOGENSYN-MONOMER.
ECOL316407:JW3392-MONOMER.
MetaCyc:GLYCOGENSYN-MONOMER.
BRENDAi2.4.1.21. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A6U8.
PROiP0A6U8.

Family and domain databases

HAMAPiMF_00484. Glycogen_synth.
InterProiIPR001296. Glyco_trans_1.
IPR011835. GS/SS.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamiPF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02095. glgA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-glucose:alpha-1,4-glucan, 4-glucosyltransferase as deduced from the nucleotide sequence of the glgA gene."
    Kumar A., Larsen C.E., Preiss J.
    J. Biol. Chem. 261:16256-16259(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-glucose synthetase as deduced from the nucleotide sequence of the glg C gene."
    Baecker P.A., Furlong C.E., Preiss J.
    J. Biol. Chem. 258:5084-5088(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
  5. "The 55-kilodalton protein in an oriC complex fraction is glycogen synthase."
    Kaidow A., Kataoka T., Wachi M., Takada A., Yamasaki M., Nagai K.
    J. Bacteriol. 174:5454-5456(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-10.

Entry informationi

Entry nameiGLGA_ECOLI
AccessioniPrimary (citable) accession number: P0A6U8
Secondary accession number(s): P08323, Q2M793
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: March 29, 2005
Last modified: July 22, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.