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A7ZSW5 (GLGB_ECO24) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
1,4-alpha-glucan branching enzyme GlgB

EC=2.4.1.18
Alternative name(s):
1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase
Alpha-(1->4)-glucan branching enzyme
Glycogen branching enzyme
Short name=BE
Gene names
Name:glgB
Ordered Locus Names:EcE24377A_3911
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length728 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position By similarity. HAMAP MF_00685

Catalytic activity

Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain. HAMAP MF_00685

Pathway

Glycan biosynthesis; glycogen biosynthesis. HAMAP MF_00685

Subunit structure

Monomer By similarity. HAMAP MF_00685

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7287281,4-alpha-glucan branching enzyme GlgB HAMAP MF_00685
PRO_1000061989

Sites

Active site4051Nucleophile By similarity
Active site4581Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZSW5 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 0F20AF3677BF2015

FASTA72884,337
        10         20         30         40         50         60 
MSDRIDRDVI NALIAGHFAD PFSVLGMHKT TAGLEVRALL PDATDVWVIE PKTGRKLAKL 

        70         80         90        100        110        120 
ECLDSRGFFS GVIPRRKNFF RYQLAVVWHG QQNLIDDPYR FGPLIQEMDA WLLSEGTHLR 

       130        140        150        160        170        180 
PYETLGAHAD TMDGVTGTRF SVWAPNARRV SVVGQFNYWD GRRHPMRLRK ESGIWELFIP 

       190        200        210        220        230        240 
GAHNGQLYKY EMIDANGNLR LKSDPYAFEA QMRPETASLI CGLPEKVVQT EERKKANQFD 

       250        260        270        280        290        300 
APISIYEVHL GSWRRHTDNN FWLSYRELAD QLVPYAKWMG FTHLELLPIN EHPFDGSWGY 

       310        320        330        340        350        360 
QPTGLYAPTR RFGTRDDFRY FIDAAHAAGL NVILDWVPGH FPTDDFALAE FDGTNLYEHS 

       370        380        390        400        410        420 
DPREGYHQDW NTLIYNYGRR EVSNFLVGNA LYWIERFGID ALRVDAVASM IYRDYSRKEG 

       430        440        450        460        470        480 
EWIPNEFGGR ENLEAIEFLR NTNRILGEQV SGAVTMAEES TDFPGVSRPQ DMGGLGFWYK 

       490        500        510        520        530        540 
WNLGWMHDTL DYMKLDPVYR QYHHDKLTFG ILYNYTENFV LPLSHDEVVH GKKSILDRMP 

       550        560        570        580        590        600 
GDAWQKFANL RAYYGWMWAF PGKKLLFMGN EFAQGREWNH DASLDWHLLE GGDNWHHGVQ 

       610        620        630        640        650        660 
RLVRDLNLTY RHHKAMHELD FDPYGFEWLV VDDKERSVLI FVRRDKEGNE IIVASNFTPV 

       670        680        690        700        710        720 
PRHDYRFGIN QPGKWREILN TDSMHYHGSN AGNGGTVHSD EIASHGRQHS LSLTLPPLAT 


IWLVREAE 

« 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: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV17243.1.
RefSeqYP_001464894.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZSW5.
SMRA7ZSW5. Positions 4-728.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZSW5.

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000023420; EBESCP00000022482; EBESCG00000022474.
GeneID5586828.
GenomeReviewsGene locus EcE24377A_3911 in contig CP000800_GR.
KEGGecw:EcE24377A_3911.
PATRIC18297094. VBIEscCol31211_4152.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0296.
GeneTreeEBGT00050000009924.
HOGENOMHBG287139.
OMARVYHQNG.
ProtClustDBPRK05402.

Enzyme and pathway databases

BioCycECOL331111:ECE24377A_3911-MONOMER.

Family and domain databases

HAMAPMF_00685. GlgB.
[Tree]
InterProIPR006407. 1-4-A-glucan_branch_enz.
IPR006048. A-amylase_b_C.
IPR015902. Alpha_amylase.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 2 hits.
KOK00700.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PTHR10357:SF13. PTHR10357:SF13. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFPIRSF000463. GlgB. 1 hit.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 2 hits.
TIGRFAMsTIGR01515. Branching_enzym. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLGB_ECO24
AccessionPrimary (citable) accession number: A7ZSW5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families