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A7ZSW4 (GLGX_ECO24) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycogen debranching enzyme

EC=3.2.1.-
Alternative name(s):
Glycogen operon protein GlgX
Gene names
Name:glgX
Ordered Locus Names:EcE24377A_3910
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length657 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Hydrolyzes the alpha-1,6-glucosidic linkages in glycogen which has first been partially depolymerized by phosphorylase. Shows only very little activity with native glycogen By similarity. HAMAP-Rule MF_01248

Pathway

Glycan degradation; glycogen degradation. HAMAP-Rule MF_01248

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 657657Glycogen debranching enzyme HAMAP-Rule MF_01248
PRO_1000067098

Sites

Active site3361Nucleophile By similarity
Active site3711Proton donor By similarity
Site4431Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZSW4 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: BF8BFC1F72E80B85

FASTA65773,603
        10         20         30         40         50         60 
MTQLAIGKPA PLGAHYDGQG VNFTLFSAHA ERVELCVFDA NGQEHRYDLP GHSGDIWHGY 

        70         80         90        100        110        120 
LPDARPGLRY GYRVHGPWQP AEGHRFNPAK LLIDPCARQI DGEFKDNPLL HAGHNEPDYR 

       130        140        150        160        170        180 
DNAAIAPKCV VVVDHYDWED DAPPRTPWGS TIIYEAHVKG LTYLHPEIPV EIRGTYKALG 

       190        200        210        220        230        240 
HPVMINYLKQ LGITALELLP VAQFASEPRL QRMGLSNYWG YNPVAMFALH PAYACSPETA 

       250        260        270        280        290        300 
LDEFRDAIKA LHKAGIEVIL DIVLNHSAEL DLDGPLFSLR GIDNRSYYWI REDGDYHNWT 

       310        320        330        340        350        360 
GCGNTLNLSH PAVVDYASAC LRYWVETCHV DGFRFDLAAV MGRTPEFRQD APLFTAIQNC 

       370        380        390        400        410        420 
PVLSQVKLIA EPWDIAPGGY QVGNFPPLFA EWNDHFRDAA RRFWLHYDLP LGAFAGRFAA 

       430        440        450        460        470        480 
SSDVFKRNGR LPSAAINLVT AHDGFTLRDC VCFNHKHNEA NGEENRDGTN NNYSNNHGKE 

       490        500        510        520        530        540 
GLGGSLDLVE RRRDSIHALL TTLLLSQGTP MLLAGDEHGH SQYGNNNAYC QDNQLTWLDW 

       550        560        570        580        590        600 
SQASSGLTAF TAALIHLRKR IPALVENRWW EEGDGNVRWL NRYAQPLSTD EWQNGPKQLQ 

       610        620        630        640        650 
ILLSDRFLIA INATLEVTEI VLPAGEWHAI PPFAGEDNPV ITAVWQGPAH GLCVFQR 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV16561.1.
RefSeqYP_001464893.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZSW4.
SMRA7ZSW4. Positions 2-657.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING331111.EcE24377A_3910.

Protein family/group databases

CAZyCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV16561; ABV16561; EcE24377A_3910.
GeneID5587748.
KEGGecw:EcE24377A_3910.
PATRIC18297092. VBIEscCol31211_4151.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1523.
HOGENOMHOG000239197.
KOK02438.
OMAGKTNYWG.
OrthoDBEOG64BQ3X.

Enzyme and pathway databases

BioCycECOL331111:GH7P-3889-MONOMER.
UniPathwayUPA00165.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.20.20.80. 1 hit.
HAMAPMF_01248. GlgX.
InterProIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR022844. Glycogen_debranch_bac.
IPR011837. Glycogen_debranch_GlgX.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
SSF81296. SSF81296. 1 hit.
TIGRFAMsTIGR02100. glgX_debranch. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLGX_ECO24
AccessionPrimary (citable) accession number: A7ZSW4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries