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B6I2Z8 (B6I2Z8_ECOSE) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | 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 HAMAP MF_00685

EC=2.4.1.18 HAMAP MF_00685
Alternative name(s):
1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase HAMAP MF_00685
Alpha-(1->4)-glucan branching enzyme HAMAP MF_00685
Glycogen branching enzyme HAMAP MF_00685
Gene names
Name:glgB HAMAP MF_00685
Ordered Locus Names:ECSE_3701
OrganismEscherichia coli (strain SE11) [Complete proteome] [HAMAP]
Taxonomic identifier409438 [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 SAAS SAAS006407

Pathway

Glycan biosynthesis; glycogen biosynthesis. HAMAP MF_00685 SAAS SAAS006407

Subunit structure

Monomer By similarity. HAMAP MF_00685

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. GlgB subfamily. HAMAP MF_00685

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site4051Nucleophile By similarity HAMAP MF_00685
Active site4581Proton donor By similarity HAMAP MF_00685

Sequences

Sequence LengthMass (Da)Tools
B6I2Z8 [UniParc].

Last modified December 16, 2008. 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]"Complete genome sequence and comparative analysis of the wild-type commensal Escherichia coli strain SE11 isolated from a healthy adult."
Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.
DNA Res. 15:375-386(2008) [PubMed: 18931093] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009240 Genomic DNA. Translation: BAG79225.1.
RefSeqYP_002294976.1. NC_011415.1.

3D structure databases

ProteinModelPortalB6I2Z8.
SMRB6I2Z8. Positions 4-728.
ModBaseSearch...

Protein-protein interaction databases

STRINGB6I2Z8.

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000110361; EBESCP00000103512; EBESCG00000107793.
GeneID7002086.
GenomeReviewsGene locus ECSE_3701 in contig AP009240_GR.
KEGGecy:ECSE_3701.
PATRIC18426033. VBIEscCol83070_3869.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009924.
HOGENOMHBG287139.
OMARVYHQNG.
ProtClustDBPRK05402.

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 nameB6I2Z8_ECOSE
AccessionPrimary (citable) accession number: B6I2Z8
Entry history
Integrated into UniProtKB/TrEMBL: December 16, 2008
Last sequence update: December 16, 2008
Last modified: December 14, 2011
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)