B3DSS9 (B3DSS9_BIFLD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended 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 EMBL ACD98198.1
Ordered Locus Names:	BLD_0752

Organism

Bifidobacterium longum (strain DJO10A) [Complete proteome] [HAMAP]

Taxonomic identifier

205913 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length	750 AA.
Sequence status	Complete.
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. 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

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen biosynthesis HAMAP MF_00685 SAAS SAAS006407 Glycogen metabolism HAMAP MF_00685
Molecular function	Glycosyltransferase HAMAP MF_00685 SAAS SAAS006407 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
Sites
	Active site	431	1	Nucleophile By similarity HAMAP MF_00685
	Active site	484	1	Proton donor By similarity HAMAP MF_00685

Sequences

	Sequence		Length	Mass (Da)
	B3DSS9 [UniParc]. Last modified July 22, 2008. Version 1. Checksum: C78BCE1ADDCD26C9	FASTA	750	84,550
	10 20 30 40 50 60 MAKETKIEED TVTVPVAQGD LDATSNAEFY NPHGVLGGHL GIGKHADTAT IRVLRPLAKS 70 80 90 100 110 120 VTILTQDGEY PMTHEYNGVF VVTVPASGTK KQPTIPDYRV RTEWESGAVL IEDDPYRYMP 130 140 150 160 170 180 TVGDMDTYLF GEGRHEKLWE TLGAHVLRYD DPMGGADGTP GEQVVGTAFS VWAPNAHAVR 190 200 210 220 230 240 VVGNFNAWDG RRHAMRELGS SGVWEIFIPG IGAGETYKFQ ILNANYTWEM KADPMERQHE 250 260 270 280 290 300 VPPNTASIVT ESTYKWNDDA WMQHRRTTNP HDGPVSIYEV HAGSWRQGLT YRDLAKQLVD 310 320 330 340 350 360 YVKQEGFTHV EFMPLAQHPF SGSWGYQVTG YYAVDSRLGS PDDFRYLVDQ FHQAGIGVIM 370 380 390 400 410 420 DWVPAHFPKD AFALGRFDGT PLYEDPDPLR GEHPEWGTYV FNFGRREVRN FLVANALFWL 430 440 450 460 470 480 EDLHVDALRV DAVSSMLYLD YSREPGHWRP NIYGGRENLE AIDFLKEATA TAYKNNPGVM 490 500 510 520 530 540 VIAEESTAWP GITAPTSAGG IGFGMKWNMG WMHDTLEYLH EEPINRKWHH NEITFSMVYA 550 560 570 580 590 600 YSEHYVLPIS HDEVVYGKGS LYGKMPGDDW QKLAGVRSMF AYQWAHPGKK LSFMGNELAQ 610 620 630 640 650 660 WGEWDHDASI DWDCLNWQEH RQVQTMVADL NAFYKAHPAL WSQDFDPAGF QWLTSDDADH 670 680 690 700 710 720 NTLSFLRIGT KGETLAVVVN FSGEAWSDYQ VALPTGGKWT EVFTTDDAKY GGSDIHNGTF 730 740 750 EAVEGEYHSR PFSAKITVPA LGVVFLKPED

References

[1]

"Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth." Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V., Slesarev A.I., Weimer B., O'Sullivan D.J. BMC Genomics 9:247-247(2008) [PubMed: 18505588] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000605 Genomic DNA. Translation: ACD98198.1.
RefSeq	YP_001954696.1. NC_010816.1.
3D structure databases
ProteinModelPortal	B3DSS9.
ModBase	Search...
Protein-protein interaction databases
STRING	B3DSS9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6362779.
GenomeReviews	Gene locus BLD_0752 in contig CP000605_GR.
KEGG	blj:BLD_0752.
PATRIC	21114442. VBIBifLon134794_0762.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG287139.
OMA	DGTCLYE.
ProtClustDB	PRK05402.
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. 1 hit.
TIGRFAMs	TIGR01515. Branching_enzym. 1 hit.
ProtoNet	Search...

Entry information

Entry name

B3DSS9_BIFLD

Accession

Primary (citable) accession number: B3DSS9

Entry history

Integrated into UniProtKB/TrEMBL:	July 22, 2008
Last sequence update:	July 22, 2008
Last modified:	December 14, 2011
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)