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CAZyme Information: KFL61484.1

You are here: Home > Sequence: KFL61484.1

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 Trichophyton rubrum
Lineage Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton rubrum
CAZyme ID KFL61484.1
CAZy Family GT39
CAZyme Description 1,4-alpha-glucan-branching enzyme
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
353 GG700651|CGC3 40361.73 7.4522
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_TrubrumCBS118892 8713 559305 97 8616
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 230 352 1.8e-67 0.41638225255972694

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
215246 PLN02447 0.0 7 351 58 402
1,4-alpha-glucan-branching enzyme
200460 AmyAc_bac_euk_BE 4.57e-146 163 353 2 192
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 1.83e-100 114 353 333 570
alpha-amylase
223373 GlgB 1.97e-82 53 351 23 315
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
178782 PLN03244 1.54e-69 114 353 338 545
alpha-amylase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.50e-213 6 353 8 355
3.67e-213 3 353 6 356
2.57e-212 6 353 15 362
2.57e-212 6 353 15 362
5.95e-211 6 353 15 362

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.39e-150 3 352 23 370
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]
9.25e-146 18 352 6 338
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]
4.15e-135 7 351 9 356
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]
4.15e-135 7 351 9 356
Structure of the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
8.05e-135 7 351 8 355
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
8.73e-209 7 353 8 354
1,4-alpha-glucan-branching enzyme OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=be1 PE=2 SV=3
3.38e-207 6 353 12 359
1,4-alpha-glucan-branching enzyme OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=gbeA PE=2 SV=1
9.32e-178 10 353 15 356
1,4-alpha-glucan-branching enzyme OS=Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194) OX=747089 GN=GLC3 PE=2 SV=2
3.54e-172 2 353 3 356
1,4-alpha-glucan-branching enzyme OS=Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) OX=214684 GN=GLC3 PE=3 SV=1
3.54e-172 2 353 3 356
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
1.000060 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in KFL61484.1.