logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: K441DRAFT_618527-t45_1-p1

You are here: Home > Sequence: K441DRAFT_618527-t45_1-p1

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 Cenococcum geophilum
Lineage Ascomycota; Dothideomycetes; ; Gloniaceae; Cenococcum; Cenococcum geophilum
CAZyme ID K441DRAFT_618527-t45_1-p1
CAZy Family GH125
CAZyme Description glycosyltransferase family 5 protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2416 KV748225|CGC1 270351.25 6.3665
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Cgeophilum1.58 14745 794803 38 14707
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.183:18 2.4.1.-:2 2.4.1.183:36 2.4.1.-:11

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 97 494 1.5e-186 0.995
GH13 1161 1624 2.4e-76 0.98

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
200462 AmyAc_AGS 0.0 5 574 1 569
Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine diphosphoglucose-1,3-alpha-glucan glucosyltransferase and 1,3-alpha-D-glucan synthase). Alpha 1,3-glucan synthase (AGS, EC 2.4.1.183) is an enzyme that catalyzes the reversible chemical reaction of UDP-glucose and [alpha-D-glucosyl-(1-3)]n to form UDP and [alpha-D-glucosyl-(1-3)]n+1. AGS is a component of fungal cell walls. The cell wall of filamentous fungi is composed of 10-15% chitin and 10-35% alpha-1,3-glucan. AGS is triggered in fungi as a response to cell wall stress and elongates the glucan chains in cell wall synthesis. This group includes proteins from Ascomycetes and Basidomycetes. 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.
340822 GT5_Glycogen_synthase_DULL1-like 2.12e-111 1161 1616 2 459
Glycogen synthase GlgA and similar proteins. This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
223374 GlgA 1.17e-33 1951 2394 68 487
Glycogen synthase [Carbohydrate transport and metabolism].
223443 AmyA 8.45e-30 62 527 3 388
Glycosidase [Carbohydrate transport and metabolism].
200489 AmyAc_5 2.25e-24 62 496 2 397
Alpha amylase catalytic domain found in an uncharacterized protein family. 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 5 2416 4 2381
0.0 8 2416 9 2432
0.0 8 2416 9 2423
0.0 8 2416 9 2423
0.0 11 2416 13 2467

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.32e-16 63 495 12 329
Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
2.99e-16 63 495 46 363
Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
1.69e-15 63 495 13 330
Crystal structure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
3.83e-15 63 178 134 247
Chain A, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF6_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
3.83e-15 63 178 134 247
Chain A, Neopullulanase 2 [Thermoactinomyces vulgaris],1VFM_B Chain B, Neopullulanase 2 [Thermoactinomyces vulgaris],1VFO_A Chain A, Neopullulanase 2 [Thermoactinomyces vulgaris],1VFO_B Chain B, Neopullulanase 2 [Thermoactinomyces vulgaris],1VFU_A Chain A, Neopullulanase 2 [Thermoactinomyces vulgaris],1VFU_B Chain B, Neopullulanase 2 [Thermoactinomyces vulgaris]

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 2416 23 2410
Cell wall alpha-1,3-glucan synthase ags1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ags1 PE=1 SV=3
0.0 27 2416 31 2397
Cell wall alpha-1,3-glucan synthase mok11 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok11 PE=3 SV=2
0.0 11 2414 15 2351
Cell wall alpha-1,3-glucan synthase mok12 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok12 PE=3 SV=1
0.0 16 2416 19 2358
Cell wall alpha-1,3-glucan synthase mok13 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok13 PE=3 SV=2
5.09e-296 1027 2416 131 1369
Cell wall alpha-1,3-glucan synthase mok14 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok14 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000355 0.999614 CS pos: 18-19. Pr: 0.9787

TMHMM  Annotations      download full data without filtering help

Start End
2025 2043
2050 2072
2082 2104
2116 2138
2158 2180
2205 2224
2239 2261
2268 2290
2313 2335
2342 2364
2389 2408