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CAZyme Information: AWU77038.1

You are here: Home > Sequence: AWU77038.1

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 Pichia kudriavzevii
Lineage Ascomycota; Saccharomycetes; ; Pichiaceae; Pichia; Pichia kudriavzevii
CAZyme ID AWU77038.1
CAZy Family GT39
CAZyme Description 1,4-alpha-glucan-branching enzyme [Source:UniProtKB/TrEMBL;Acc:A0A2U9R7X3]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
707 80692.01 6.2930
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PkudriavzeviiCBS573 5367 N/A 212 5155
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 242 541 2.1e-147 0.9965870307167235

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
215519 PLN02960 0.0 125 695 332 888
alpha-amylase
200460 AmyAc_bac_euk_BE 0.0 174 585 1 406
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 3 697 41 729
1,4-alpha-glucan-branching enzyme
178782 PLN03244 2.61e-163 125 695 337 863
alpha-amylase; Provisional
223373 GlgB 1.83e-139 61 697 20 627
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 1 707 1 707
0.0 15 704 18 707
0.0 18 705 9 696
0.0 19 697 18 698
0.0 19 697 18 698

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.91e-285 15 696 25 695
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]
5.42e-282 29 696 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]
7.89e-248 25 694 16 688
Structure of the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
2.24e-247 25 694 16 688
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]
3.07e-247 25 694 15 687
Chain A, Isoform 2 of 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic [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 15 697 4 700
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 15 697 4 701
1,4-alpha-glucan-branching enzyme OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GLC3 PE=1 SV=2
0.0 14 699 5 705
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
1.13e-317 10 707 3 719
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
4.60e-315 10 702 9 710
1,4-alpha-glucan-branching enzyme OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=GLC3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000073 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in AWU77038.1.