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CAZyme Information: PHYBL_171639T0-p1

You are here: Home > Sequence: PHYBL_171639T0-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 Phycomyces blakesleeanus
Lineage Mucoromycota; Mucoromycetes; ; Phycomycetaceae; Phycomyces; Phycomyces blakesleeanus
CAZyme ID PHYBL_171639T0-p1
CAZy Family GH47
CAZyme Description Alpha-D-galactosidase (melibiase)
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
697 PblaNRRL1555-_SC19|CGC3 78569.28 6.5791
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PblakesleeanusNRRL1555 16528 763407 0 16528
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH36 18 675 7.7e-178 0.9898255813953488

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269892 GH36 2.63e-120 302 589 3 299
glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
307952 Melibiase 1.78e-119 264 597 1 347
Melibiase. Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.
225882 GalA 5.91e-101 13 652 2 650
Alpha-galactosidase [Carbohydrate transport and metabolism].
407116 Glyco_hydro_36N 3.97e-43 32 259 1 255
Glycosyl hydrolase family 36 N-terminal domain. This domain is found at the N-terminus of many family 36 glycoside hydrolases. It has a beta-supersandwich fold.
269893 GH27 2.39e-14 305 500 5 160
glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
7.50e-222 1 694 3 723
2.10e-220 5 694 27 750
2.31e-214 1 694 28 761
5.06e-213 2 694 2 726
2.96e-205 17 694 1 710

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.10e-99 4 650 1 692
Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_B Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_C Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_D Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
1.95e-98 4 650 1 692
Crystal structure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
1.46e-97 4 650 1 692
Crystal structure of GH36 alpha-galactosidase AgaA A355E D548N from Geobacillus stearothermophilus in complex with raffinose [Geobacillus stearothermophilus],4FNT_B Crystal structure of GH36 alpha-galactosidase AgaA A355E D548N from Geobacillus stearothermophilus in complex with raffinose [Geobacillus stearothermophilus],4FNT_C Crystal structure of GH36 alpha-galactosidase AgaA A355E D548N from Geobacillus stearothermophilus in complex with raffinose [Geobacillus stearothermophilus],4FNT_D Crystal structure of GH36 alpha-galactosidase AgaA A355E D548N from Geobacillus stearothermophilus in complex with raffinose [Geobacillus stearothermophilus]
2.04e-97 4 650 1 692
Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_B Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_C Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_D Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNS_A Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_B Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_C Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_D Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus]
4.00e-97 4 650 1 692
Crystal structure of GH36 alpha-galactosidase AgaA A355E D478A from Geobacillus stearothermophilus in complex with stachyose [Geobacillus stearothermophilus],4FNU_B Crystal structure of GH36 alpha-galactosidase AgaA A355E D478A from Geobacillus stearothermophilus in complex with stachyose [Geobacillus stearothermophilus],4FNU_C Crystal structure of GH36 alpha-galactosidase AgaA A355E D478A from Geobacillus stearothermophilus in complex with stachyose [Geobacillus stearothermophilus],4FNU_D Crystal structure of GH36 alpha-galactosidase AgaA A355E D478A from Geobacillus stearothermophilus in complex with stachyose [Geobacillus stearothermophilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.62e-98 4 650 1 692
Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA PE=1 SV=1
1.79e-93 23 695 23 731
Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1
6.31e-87 43 687 75 712
Alpha-galactosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=aga PE=3 SV=3
1.41e-83 39 652 28 650
Alpha-galactosidase OS=Escherichia coli OX=562 GN=rafA PE=1 SV=1
3.46e-83 111 566 131 597
Alpha-galactosidase 2 OS=Pediococcus pentosaceus OX=1255 GN=agaS PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000038 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in PHYBL_171639T0-p1.