Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

1,4-alpha-glucan branching enzyme GlgB 2

Gene

glgB2

Organism
Rhizobium leguminosarum bv. viciae (strain 3841)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

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

Pathwayi: glycogen biosynthesis

This protein is involved in the pathway glycogen biosynthesis, which is part of Glycan biosynthesis.UniRule annotation
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)DescriptionActionsGraphical viewLength
Active sitei415NucleophileUniRule annotation1
Active sitei468Proton donorUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processCarbohydrate metabolism, Glycogen biosynthesis, Glycogen metabolism

Enzyme and pathway databases

UniPathwayiUPA00164

Protein family/group databases

CAZyiCBM48 Carbohydrate-Binding Module Family 48
GH13 Glycoside Hydrolase Family 13

Names & Taxonomyi

Protein namesi
Recommended name:
1,4-alpha-glucan branching enzyme GlgB 2UniRule annotation (EC:2.4.1.18UniRule annotation)
Alternative name(s):
1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase 2UniRule annotation
Alpha-(1->4)-glucan branching enzyme 2UniRule annotation
Glycogen branching enzyme 2UniRule annotation
Short name:
BE 2UniRule annotation
Gene namesi
Name:glgB2UniRule annotation
Ordered Locus Names:pRL120710
OrganismiRhizobium leguminosarum bv. viciae (strain 3841)
Taxonomic identifieri216596 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium
Proteomesi
  • UP000006575 Componenti: Plasmid pRL12

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002606851 – 7361,4-alpha-glucan branching enzyme GlgB 2Add BLAST736

Proteomic databases

PRIDEiQ1M3A7

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ1M3A7
SMRiQ1M3A7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000283037
KOiK00700
OMAiEVVHGKS
OrthoDBiPOG091H08D1

Family and domain databases

Gene3Di2.60.40.10, 1 hit
2.60.40.1180, 1 hit
HAMAPiMF_00685 GlgB, 1 hit
InterProiView protein in InterPro
IPR006048 A-amylase/branching_C
IPR037439 Branching_enzy
IPR006407 GlgB
IPR006047 Glyco_hydro_13_cat_dom
IPR004193 Glyco_hydro_13_N
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
PANTHERiPTHR43651 PTHR43651, 2 hits
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF02806 Alpha-amylase_C, 1 hit
PF02922 CBM_48, 1 hit
PIRSFiPIRSF000463 GlgB, 1 hit
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
SSF81296 SSF81296, 2 hits
TIGRFAMsiTIGR01515 branching_enzym, 1 hit

Sequencei

Sequence statusi: Complete.

Q1M3A7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVERSELLA GIGQDALWAL IEGRHGDPFS ILGPHQSGGM TIVRVYLPGA
60 70 80 90 100
EAVDLIDATS GRVVAPFSIA HPSGLFAATV ASRTGYRLRI TWPDAVQITE
110 120 130 140 150
DPYSFGLLLG ELDLHLISEG THYSLSRTLG AVAMSIDGIS GVRFAVWAPN
160 170 180 190 200
ARRVSVVGDF NAWDGRRNPM RLRPSAGVWE LFIPRLAPGE RYKFEIVDAE
210 220 230 240 250
GTCLPQKADP VARASEAAPS TASIVASSTP FRWTDDGWMK GRSRQDRLEG
260 270 280 290 300
AFSVYEVHVG SWLRDQKDGN RSLDWVELSQ RLVPYVSDMG FTHIELLPIM
310 320 330 340 350
EHPFGGSWGY QPLGLFAPTG RYGTPEDFAY FVDRCHGAGL GVILDWVPAH
360 370 380 390 400
FPTDVWGLAR FDGSALYEHE DPREGFHRDW NTLIYNLGRN EVKGFLIASA
410 420 430 440 450
LEWLERYHID GLRVDAVASM LYRDYSRNEG EWIPNQYGGR ENLEAVEFFK
460 470 480 490 500
HLNSIIHERC PHAMTIAEES TAWPGVTKPP EQGGLGFDIK WNMGWMHDSL
510 520 530 540 550
SYIEKDPIYR SYAHGTMTFG MIYAYSERFI LPISHDEVVY GKGSLLTKMP
560 570 580 590 600
GDEWQKFANL RSYLAFMWGH PGKKLLFMGS EIAQPSEWNH DGSVTWDVLD
610 620 630 640 650
QPQHVGIQRL VKDLNGLYGD EPALQFGDFH SEGFEWAAAD DAVNSVLGML
660 670 680 690 700
RYAPDRASSV LVMSNFTPVP RYGYRIGVPS DGVWIERITT DAREYGGSGL
710 720 730
VNGAVSSEPV PAHGRPVSLS LTLPPLSTIF LQGPSP
Length:736
Mass (Da):81,853
Last modified:May 30, 2006 - v1
Checksum:iF81E22D2BE2DA1CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM236086 Genomic DNA Translation: CAK12419.1
RefSeqiWP_011649463.1, NC_008378.1

Genome annotation databases

EnsemblBacteriaiCAK12419; CAK12419; pRL120710
KEGGirle:pRL120710

Similar proteinsi

Entry informationi

Entry nameiGLGB2_RHIL3
AccessioniPrimary (citable) accession number: Q1M3A7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: May 30, 2006
Last modified: May 23, 2018
This is version 92 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health