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CAZyme Information: PHPALM_12412-t46_1-p1

You are here: Home > Sequence: PHPALM_12412-t46_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 Phytophthora palmivora
Lineage Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora palmivora
CAZyme ID PHPALM_12412-t46_1-p1
CAZy Family AA17
CAZyme Description Alpha-glucosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
305 33037.62 5.1571
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Ppalmivorasbr112.9 28185 N/A 3511 24674
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.1:4 3.2.1.98:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM25 145 219 7.3e-17 0.9230769230769231

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
200456 AmyAc_bac_euk_AmyA 3.60e-23 246 305 1 53
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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.
198134 CBM_25 2.65e-10 43 116 15 82
Carbohydrate binding domain.
407028 CBM53 2.89e-10 38 114 1 75
Starch/carbohydrate-binding module (family 53).
198134 CBM_25 3.91e-10 149 218 14 78
Carbohydrate binding domain.
367491 CBM_25 2.48e-09 141 218 3 76
Carbohydrate binding domain (family 25).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
9.18e-30 25 223 48 241
1.72e-29 20 223 591 794
1.78e-23 21 238 634 881
1.09e-22 21 238 634 881
4.04e-22 33 237 986 1185

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.00e-11 137 222 5 86
Chain B, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3W_A Chain A, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3W_B Chain B, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3W_C Chain C, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3W_D Chain D, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3X_A Chain A, Alpha-amylase G-6 [Halalkalibacterium halodurans C-125],2C3X_B Chain B, Alpha-amylase G-6 [Halalkalibacterium halodurans C-125]
8.25e-11 137 222 5 86
Chain A, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125]
5.94e-09 248 305 12 64
Recombinant medaka fish alpha-amylase expressed in yeast Pichia pastoris [Oryzias latipes]
5.78e-08 246 305 10 62
YELLOW MEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE AMARANTH ALPHA-AMYLASE INHIBITOR [Tenebrio molitor],1JAE_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE [Tenebrio molitor],1TMQ_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR [Tenebrio molitor]
5.78e-08 246 305 10 62
TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX [Tenebrio molitor]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.19e-16 21 218 889 1167
Alpha-amylase OS=Niallia circulans OX=1397 GN=igtZ PE=1 SV=1
3.96e-09 218 305 2 82
Alpha-amylase-related protein OS=Drosophila subobscura OX=7241 GN=Amyrel PE=3 SV=1
9.47e-09 218 305 2 82
Alpha-amylase-related protein OS=Drosophila varians OX=30050 GN=Amyrel PE=3 SV=1
1.26e-08 244 305 27 81
Alpha-amylase-related protein OS=Drosophila melanogaster OX=7227 GN=Amyrel PE=2 SV=2
1.27e-08 244 305 9 63
Alpha-amylase (Fragment) OS=Dermatophagoides pteronyssinus OX=6956 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000241 0.999743 CS pos: 25-26. Pr: 0.9693

TMHMM  Annotations      help

There is no transmembrane helices in PHPALM_12412-t46_1-p1.