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CAZyme Information: MGYG000000971_02083

You are here: Home > Sequence: MGYG000000971_02083

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 UMGS1518 sp900552575
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; UMGS1518; UMGS1518 sp900552575
CAZyme ID MGYG000000971_02083
CAZy Family GH36
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
650 74176.59 4.791
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000971 3501016 MAG Australia Oceania
Gene Location Start: 631;  End: 2583  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000971_02083.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH36 139 471 3.9e-66 0.48401162790697677

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14791 GH36 4.43e-48 276 471 31 219
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.
pfam02065 Melibiase 3.29e-39 270 472 64 261
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.
COG3345 GalA 2.81e-24 148 473 185 507
Alpha-galactosidase [Carbohydrate transport and metabolism].
cd11313 AmyAc_arch_bac_AmyA 8.14e-07 327 413 83 179
Alpha amylase catalytic domain found in archaeal and bacterial 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 firmicutes, bacteroidetes, and proteobacteria. 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.
COG1501 YicI 1.08e-05 256 403 270 414
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AZN42907.1 2.66e-107 104 647 105 644
QGA23301.1 2.35e-90 48 646 69 689
QOY88337.1 8.46e-89 12 628 177 770
QGA24711.1 9.85e-88 117 649 125 662
AVM44715.1 4.07e-87 13 650 196 838

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6JHP_A 4.76e-27 148 634 252 742
Crystalstructure of the glycoside hydrolase family 36 alpha-galactosidase from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],6JHP_B Crystal structure of the glycoside hydrolase family 36 alpha-galactosidase from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],6JHP_C Crystal structure of the glycoside hydrolase family 36 alpha-galactosidase from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],6JHP_D Crystal structure of the glycoside hydrolase family 36 alpha-galactosidase from Paecilomyces thermophila [Paecilomyces sp. 'thermophila']
4FNQ_A 7.89e-27 144 471 218 548
Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
4FNR_A 5.72e-26 144 471 218 548
Crystalstructure 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]
4FNT_A 1.01e-25 144 457 218 534
Crystalstructure 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]
3MI6_A 1.83e-25 270 557 353 639
ChainA, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_B Chain B, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_C Chain C, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_D Chain D, Alpha-galactosidase [Levilactobacillus brevis ATCC 367]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q5AU92 7.96e-26 148 471 244 573
Alpha-galactosidase C OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=aglC PE=1 SV=1
P43469 9.87e-26 250 559 324 634
Alpha-galactosidase 2 OS=Pediococcus pentosaceus OX=1255 GN=agaS PE=3 SV=1
B8NWY6 2.47e-25 148 471 244 572
Probable alpha-galactosidase C OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=aglC PE=3 SV=2
Q2TW69 2.47e-25 148 471 244 572
Probable alpha-galactosidase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aglC PE=3 SV=1
Q9ALJ4 3.13e-25 144 471 218 548
Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000053 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000971_02083.