P07762 (GLGB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	b3432, JW3395

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	728 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen biosynthesis Glycogen metabolism
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glycogen biosynthetic process Inferred from mutant phenotype. Source: EcoCyc
Molecular function	1,4-alpha-glucan branching enzyme activity Inferred from direct assay. Source: EcoCyc cation binding Inferred from electronic annotation. Source: InterPro hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 728

728

1,4-alpha-glucan branching enzyme GlgB HAMAP MF_00685

PRO_0000188702

Sites

Active site

405

1

Nucleophile By similarity

Active site

458

1

Proton donor By similarity

Secondary structure

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728

Helix Strand Turn

Details...

Helix

121 – 123

3

Beta strand

125 – 134

10

Beta strand

136 – 143

8

Beta strand

150 – 154

5

Helix

155 – 157

3

Turn

161 – 163

3

Turn

170 – 172

3

Beta strand

174 – 180

7

Beta strand

187 – 193

7

Beta strand

199 – 202

4

Beta strand

208 – 211

4

Turn

213 – 215

3

Beta strand

217 – 219

3

Helix

231 – 237

7

Beta strand

244 – 248

5

Turn

257 – 259

3

Helix

265 – 278

14

Beta strand

282 – 287

6

Helix

295 – 297

3

Beta strand

303 – 308

6

Helix

310 – 312

3

Helix

315 – 327

13

Beta strand

331 – 336

6

Helix

351 – 353

3

Beta strand

356 – 358

3

Helix

380 – 396

17

Beta strand

401 – 404

4

Helix

408 – 411

4

Helix

433 – 448

16

Beta strand

454 – 457

4

Turn

464 – 467

4

Turn

470 – 473

4

Beta strand

478 – 481

4

Helix

483 – 494

12

Helix

497 – 502

6

Helix

505 – 508

4

Helix

509 – 511

3

Turn

512 – 516

5

Beta strand

519 – 523

5

Helix

525 – 527

3

Helix

535 – 538

4

Helix

543 – 559

17

Beta strand

560 – 567

8

Turn

568 – 573

6

Helix

586 – 589

4

Helix

595 – 610

16

Helix

614 – 616

3

Helix

623 – 625

3

Beta strand

626 – 633

8

Turn

634 – 637

4

Beta strand

638 – 644

7

Beta strand

650 – 656

7

Beta strand

662 – 665

4

Beta strand

673 – 680

8

Helix

685 – 687

3

Beta strand

713 – 715

3

Beta strand

719 – 726

8

Sequences

	Sequence		Length	Mass (Da)
	P07762 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 0F20AF3677BF2015	FASTA	728	84,337
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli 1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-alpha-D-(1,4-alpha-D-glucano)-transferase as deduced from the nucleotide sequence of the glg B gene." Baecker P.A., Greenberg E., Preiss J. J. Biol. Chem. 261:8738-8743(1986) [PubMed: 3013861] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The X-ray crystallographic structure of Escherichia coli branching enzyme." Abad M.C., Binderup K., Rios-Steiner J., Arni R.K., Preiss J., Geiger J.H. J. Biol. Chem. 277:42164-42170(2002) [PubMed: 12196524] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 113-728.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M13751 Genomic DNA. Translation: AAA23872.1.
U18997 Genomic DNA. Translation: AAA58230.1.
U00096 Genomic DNA. Translation: AAC76457.1.
AP009048 Genomic DNA. Translation: BAE77860.1.

PIR

NQECA. A25498.

RefSeq

NP_417890.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GTY	model	-	A	24-103	[»]
1M7X	X-ray	2.30	A/B/C/D	113-728	[»]
3O7Y	X-ray	2.41	A/B/C/D	117-728	[»]
3O7Z	X-ray	2.55	A/B/C/D	117-728	[»]

ProteinModelPortal

P07762.

SMR

P07762. Positions 4-728.

ModBase

Search...

Protein-protein interaction databases

IntAct

P07762. 13 interactions.

Protein family/group databases

CAZy

CBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004077; EBESCP00000004077; EBESCG00000003329.
EBESCT00000015971; EBESCP00000015262; EBESCG00000015031.

GeneID

947940.

GenomeReviews

Gene locus JW3395 in contig AP009048_GR.
Gene locus b3432 in contig U00096_GR.

KEGG

ecj:JW3395.
eco:b3432.

PATRIC

32122304. VBIEscCol129921_3529.

Organism-specific databases

EchoBASE

EB0373.

EcoGene

EG10378. glgB.

Phylogenomic databases

eggNOG

COG0296.

GeneTree

EBGT00050000009924.

HOGENOM

HBG287139.

OMA

RVYHQNG.

PhylomeDB

P07762.

ProtClustDB

PRK05402.

Enzyme and pathway databases

BioCyc

EcoCyc:GLYCOGEN-BRANCH-MONOMER.
MetaCyc:GLYCOGEN-BRANCH-MONOMER.

Gene expression databases

Genevestigator

P07762.

Family and domain databases

HAMAP

MF_00685. GlgB.
[Tree]

InterPro

IPR006407. 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]

Gene3D

G3DSA: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.

KO

K00700.

PANTHER

PTHR10357. Alpha_amylase. 1 hit.
PTHR10357:SF13. PTHR10357:SF13. 1 hit.

Pfam

PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]

PIRSF

PIRSF000463. GlgB. 1 hit.

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 2 hits.

TIGRFAMs

TIGR01515. Branching_enzym. 1 hit.

ProtoNet

Search...

Entry information

Entry name

GLGB_ECOLI

Accession

Primary (citable) accession number: P07762
Secondary accession number(s): Q2M796

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	January 25, 2012
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program