logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: XP_001903564.1

You are here: Home > Sequence: XP_001903564.1

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 Podospora anserina
Lineage Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora anserina
CAZyme ID XP_001903564.1
CAZy Family AA16
CAZyme Description CBM20 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:B2AD24]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
426 CU633453|CGC3 45850.11 6.6544
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PanserinaSmat 10888 515849 370 10518
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.14.99.55:5 1.14.99.55:4

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA13 72 294 8.1e-133 0.9525862068965517
CBM20 325 415 9.1e-30 0.9666666666666667

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
412056 AA13_LPMO-like 7.63e-148 77 295 16 233
AA13 lytic polysaccharide monooxygenase, and similar proteins. This family contains starch-degrading (also called starch-active) lytic polysaccharide monooxygenase (LPMO), a representative of the new CAZy AA13 family and classified as an auxiliary activity enzyme. This enzyme acts on alpha-linked glycosidic bonds and displays a binding surface that is quite different from those of LPMOs acting on beta-linked glycosidic bonds, indicating that the AA13 family proteins interact with their substrate in a distinct fashion. The active site contains an amino-terminal histidine-ligated mononuclear copper. This enzyme generates aldonic acid-terminated malto-oligosaccharides from retrograded starch and significantly boosts the conversion of this recalcitrant substrate to maltose by beta-amylase.
99886 CBM20_glucoamylase 1.18e-56 319 425 1 106
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
395557 CBM_20 3.05e-45 325 416 1 91
Starch binding domain.
99883 CBM20_alpha_amylase 2.25e-39 325 426 1 95
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
119437 CBM20 5.77e-29 327 425 2 96
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 426 1 426
0.0 1 426 1 426
0.0 1 426 1 426
6.11e-185 77 426 33 371
8.53e-179 77 426 34 385

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.20e-127 77 294 16 232
AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae [Aspergillus oryzae RIB40],5LSV_A X-ray crystal structure of AA13 LPMO [Aspergillus oryzae RIB40],5T7J_A X-ray crystal structure of AA13 LPMO [Aspergillus oryzae RIB40],5T7K_A X-ray crystal structure of AA13 LPMO [Aspergillus oryzae RIB40],5T7N_A X-ray crystal structure of AA13 LPMO [Aspergillus oryzae RIB40],6TBQ_A AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae partially in Cu(II) state [Aspergillus oryzae RIB40],6TBR_A Glycosylated AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae in P1 space group [Aspergillus oryzae RIB40],6TBR_B Glycosylated AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae in P1 space group [Aspergillus oryzae RIB40],6TC4_A AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae measured with SSX [Aspergillus oryzae RIB40]
1.12e-31 319 426 1 108
GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN COMPLEX WITH CYCLODEXTRIN, NMR, MINIMIZED AVERAGE STRUCTURE [Aspergillus niger],1ACZ_A GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN COMPLEX WITH CYCLODEXTRIN, NMR, 5 STRUCTURES [Aspergillus niger],1KUL_A Chain A, GLUCOAMYLASE [Aspergillus niger],1KUM_A Chain A, GLUCOAMYLASE [Aspergillus niger],5GHL_A Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger],5GHL_B Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger],5GHL_C Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger],5GHL_D Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger]
5.72e-27 329 426 519 616
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
1.55e-24 277 426 441 598
Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
1.51e-17 297 425 470 606
Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.13e-33 277 426 472 626
Glucoamylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gla-1 PE=1 SV=3
4.73e-32 277 426 463 612
Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
1.18e-27 324 426 537 639
Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
9.54e-27 324 426 537 639
Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
3.15e-26 329 426 543 640
Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999932 0.000090

TMHMM  Annotations      help

There is no transmembrane helices in XP_001903564.1.