dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: QHS69176.1

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Basic Information help

Species

[Candida] glabrata

Lineage

Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; [Candida] glabrata

CAZyme ID

QHS69176.1

CAZy Family

GT71

CAZyme Description

1,4-alpha-glucan-branching enzyme [Source:UniProtKB/TrEMBL;Acc:A0A0W0D805]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
706		81044.10	5.9972

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CglabrataCBS1382020	5508	N/A	250	5258

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	2.4.1.18:166	2.4.1.18:50

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	247	548	2.4e-147	0.9965870307167235

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200460	AmyAc_bac_euk_BE	0.0	176	591	1	405	Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
215519	PLN02960	0.0	125	704	333	893	alpha-amylase
215246	PLN02447	0.0	6	701	55	727	1,4-alpha-glucan-branching enzyme
223373	GlgB	1.01e-174	43	704	5	628	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
178782	PLN03244	6.14e-161	125	704	338	868	alpha-amylase; Provisional

CAZyme Hits help

E-Value	Query Start	Query End	Hit Start
1	706	1	706
1	706	1	706
1	706	1	706
1	706	1	706
1	706	1	706

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.50e-287	2	702	21	695	Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_B Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_C Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens]
1.95e-284	48	702	28	663	Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLW_A Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens]
8.10e-245	16	704	16	692	Structure of the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
1.57e-244	16	704	15	691	Chain A, Isoform 2 of 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic [Oryza sativa Japonica Group]
2.30e-244	16	704	16	692	Structure of the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L [Oryza sativa Japonica Group],3VU2_B Structure of the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L [Oryza sativa Japonica Group]

Swiss-Prot Hits download full data without filtering help

E-Value	Query Start	Query End	Hit Start	Hit End
6	704	4	701	1,4-alpha-glucan-branching enzyme OS=Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) OX=284811 GN=GLC3 PE=3 SV=1
6	702	8	709	1,4-alpha-glucan-branching enzyme OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=GLC3 PE=3 SV=1
1	706	1	706	1,4-alpha-glucan-branching enzyme OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=GLC3 PE=3 SV=1
6	702	4	700	1,4-alpha-glucan-branching enzyme OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GLC3 PE=1 SV=2
7	702	11	683	1,4-alpha-glucan-branching enzyme OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=gbeA PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000044	0.000000

TMHMM Annotations help

There is no transmembrane helices in QHS69176.1.