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CAZyme Information: OEJ86795.1

You are here: Home > Sequence: OEJ86795.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Hanseniaspora uvarum
Lineage Ascomycota; Saccharomycetes; ; Saccharomycodaceae; Hanseniaspora; Hanseniaspora uvarum
CAZyme ID OEJ86795.1
CAZy Family GH76
CAZyme Description 1,4-alpha-glucan-branching enzyme
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
715 LPNN01000005|CGC1 82597.88 5.5553
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_HuvarumAWRI3580 4061 N/A 0 4061
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 261 558 1.4e-143 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 0.0 194 602 2 406
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.
215246 PLN02447 0.0 28 714 62 730
1,4-alpha-glucan-branching enzyme
215519 PLN02960 2.16e-178 140 711 333 888
alpha-amylase
178782 PLN03244 5.58e-150 140 711 338 863
alpha-amylase; Provisional
223373 GlgB 4.27e-146 67 713 18 627
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 24 713 7 701
0.0 24 715 9 705
0.0 24 715 9 705
0.0 24 715 9 705
0.0 24 715 9 705

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.30e-277 28 712 31 695
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]
5.24e-272 35 712 6 663
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]
3.57e-238 28 710 13 688
Structure of the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
1.02e-237 28 710 13 688
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]
2.16e-237 28 710 13 688
Structure of the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 24 713 11 710
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
0.0 24 714 7 701
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
0.0 24 715 7 703
1,4-alpha-glucan-branching enzyme OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GLC3 PE=1 SV=2
0.0 24 715 9 705
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
6.38e-293 28 712 12 680
1,4-alpha-glucan-branching enzyme OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=GLC3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000076 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in OEJ86795.1.