B1XQ71 (B1XQ71_SYNP2) 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 ACA99853.1
Ordered Locus Names:	SYNPCC7002_A1865

Organism

Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) [Complete proteome] [HAMAP]

Taxonomic identifier

32049 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechococcus

Protein attributes

Sequence length	777 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	434	1	Nucleophile By similarity HAMAP MF_00685
	Active site	487	1	Proton donor By similarity HAMAP MF_00685

Sequences

	Sequence		Length	Mass (Da)
	B1XQ71 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: F4CDCEF822206D09	FASTA	777	89,782
	10 20 30 40 50 60 MPTLLTPDQI NQIVSNHHDN PHAVLGCHPT NDDPNPKTWS IRAYLPSASQ AWVIDTPSQT 70 80 90 100 110 120 EHPMTTVHHP HFFECTLQSE TTPKYQLKLQ EGDRQHIIND PYAFAEAPHI SDLDLHLFAE 130 140 150 160 170 180 GNHHRIYNKL GAHLVEVDGI KGVYFAVWAP NARNVSILGD FNNWDGRKHQ MRRLNVGIWG 190 200 210 220 230 240 IFIPDLGPNT KYKYEIKNQH GHIYEKSDPY GFLREVRPDT ASIVADLDQY QWQDHDWLEQ 250 260 270 280 290 300 RAKQDPLKNP VSIYELHLGS WLHGSATEKM QLLSGEVDPI PVGDQKPGAR FLSYYELVDK 310 320 330 340 350 360 LIPYVKDMGY THIELLPVAE HPFDGSWGYQ VTGYYSPTSR FGNPEDLMYF IDQCHANGIG 370 380 390 400 410 420 VIVDWVPGHF PKDAHGLAYF DGTHLYEHAD PRKGEHKGWG TLIFNYNRNE VRNFLIANAL 430 440 450 460 470 480 FWFDKYHIDG IRVDAVASML YLDYDREDGE WLPNDYGGNE HLEAVEFLRQ TNNLIFKYYP 490 500 510 520 530 540 GIISVAEEST AWPMVSRPTY LGGLGFNLKW NMGWMHDNLK YFSMDPWFRQ HHQNSITFSM 550 560 570 580 590 600 WYHHSENYML ALSHDEVVHG KSSIIGKMPG DEWQKFANVR ALFAYMFTHP GKKTMFMSME 610 620 630 640 650 660 FGQWNEWNVW SDLSWDLLQH EPHAKLKGFF GALNSLYKQE PALYERDFEE EGFQWIDCSD 670 680 690 700 710 720 NQNSVLSFIR RAKDPNDFLV VVCNFTPQPH SHYRIGIPEE GYYQEILNSD AETFGGSNLL 730 740 750 760 770 NFGGVWTEDW RFHNLPYSID LCLPPLGVVV LKIDREKTAA MLAQKQADKA KALSGEI

References

[1]

"Complete sequence of Synechococcus sp. PCC 7002." Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A. Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000951 Genomic DNA. Translation: ACA99853.1.
RefSeq	YP_001735109.1. NC_010475.1.
3D structure databases
ProteinModelPortal	B1XQ71.
ModBase	Search...
Protein-protein interaction databases
STRING	B1XQ71.
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
GeneID	6055197.
GenomeReviews	Gene locus SYNPCC7002_A1865 in contig CP000951_GR.
KEGG	syp:SYNPCC7002_A1865.
PATRIC	23818368. VBISynSp37135_2125.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG287139.
OMA	WEIFAPD.
PhylomeDB	B1XQ71.
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

B1XQ71_SYNP2

Accession

Primary (citable) accession number: B1XQ71

Entry history

Integrated into UniProtKB/TrEMBL:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	December 14, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)