Reviewed, UniProtKB/Swiss-Prot Q65FS4 (GLGB_BACLD)

Names and origin

Protein names

Recommended name:
    1,4-alpha-glucan-branching enzyme
    EC=2.4.1.18
Alternative name(s):
    Glycogen-branching enzyme
      Short name=BE
    1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase

Gene names

Name:	glgB
Ordered Locus Names:	BLi03230, BL01419

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	627 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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.
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.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Biological process	Glycogen biosynthesis
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycogen biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	1,4-alpha-glucan branching enzyme activity Inferred from electronic annotation. Source: HAMAP 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 – 627	627	1,4-alpha-glucan-branching enzyme HAMAP MF_00685		PRO_0000188681
Sites
	Active site	204	1	By similarity
	Active site	239	1	By similarity
	Active site	244	1	By similarity
	Active site	307	1	By similarity
	Active site	309	1	By similarity
	Active site	352	1	By similarity
	Active site	419	1	By similarity
	Active site	420	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q65FS4-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 15A2BBE6AFD55161	FASTA	627	73,820
	10 20 30 40 50 60 MAGVSASDIK AHLFHEGRLY ESYRFFGAHQ TEQDGRQGFR FCVWAPHAKE VRIAGTFNGW 70 80 90 100 110 120 SGVLHRMEKR HQEGIWELFI PGIGEGELYK YEMITAANET KLKADPYAFF SEVRPKTASV 130 140 150 160 170 180 TYQLAGYQWG DRKWQKKKQQ KAVYEKPISI YELHIGSWKK KADGRFFTYR ELSETVIPYV 190 200 210 220 230 240 KEHGFTHIEL MPLTEHPFDR SWGYQTTGYY SPTSRYGEPH DLMYFIDQCH QHEIGVIMDW 250 260 270 280 290 300 VSGHFCKDDH GLYLFDGMPL YEYKHEHDRE NWEWGTANFD LGKREVHSFL ISNALYWIEM 310 320 330 340 350 360 YHIDGFRVDA VANLLYWPNR PQPEANGFAI EFIQTLNEQV FAKDPHFLMI AEDSTDWPLV 370 380 390 400 410 420 THPTYEGGLG FNYKWNMGWM NDVLTYMEAS PEQRKHLHHL VSFSLMYAYS ENYILPFSHD 430 440 450 460 470 480 EVVYRKKSLL HKMPGDYWQK FAQYRLLISY FMMHPGKKLL FMGGEFAQFD EWKDEEELDW 490 500 510 520 530 540 FLDDFDMHRK ARMFTKEALH LYKKSRILYE NDHRQQGFEW IDVNNAEQSI VSFIRYGKQP 550 560 570 580 590 600 GEALIIVCNF TPSVYHEYRV GVPFQTEYIE VLNSDDAKYG GSHQINPKRL QARKGVLHGK 610 620 PYSISMTVPP LGAAVFRAVK KRGAKKG

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017333 Genomic DNA. Translation: AAU42090.1. CP000002 Genomic DNA. Translation: AAU24729.1.
RefSeq	YP_080367.1. YP_092783.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q65FS4.
Protein family/group databases
CAZy	CBM48. Carbohydrate-Binding Module Family 48. GH13. Glycoside Hydrolase Family 13.
Genome annotation databases
GeneID	3027988. 3099151.
GenomeReviews	Gene locus BLi03230 in contig AE017333_GR. Gene locus BL01419 in contig CP000002_GR.
KEGG	bld:BLi03230. bli:BL01419.
NMPDR	fig|279010.5.peg.153.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q65FS4.
OMA	PKTASIV.
Enzyme and pathway databases
BioCyc	BLIC279010:BL01419-MON.
Family and domain databases
HAMAP	MF_00685. [Tree]
InterPro	IPR006407. 1-4-A-glucan_branch_enz_core. IPR006048. A-amylase_b_C. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat. IPR004193. Glyco_hydro_13_N. IPR013781. Glyco_hydro_sg_catalytic. IPR013783. Ig-like_fold. [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. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF02806. Alpha-amylase_C. 1 hit. PF02922. CBM_48. 1 hit. [Graphical view]
TIGRFAMs	TIGR01515. branching_enzym. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GLGB_BACLD

Accession

Primary (citable) accession number: Q65FS4
Secondary accession number(s): Q62R81

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	October 25, 2004
Last modified:	November 3, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)