logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003215_00984

You are here: Home > Sequence: MGYG000003215_00984

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 1XD42-69 sp014287635
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; 1XD42-69; 1XD42-69 sp014287635
CAZyme ID MGYG000003215_00984
CAZy Family GH36
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
702 MGYG000003215_121|CGC1 79558.38 5.1829
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003215 2655157 MAG United States North America
Gene Location Start: 10125;  End: 12233  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003215_00984.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH36 57 671 7.8e-76 0.8822674418604651

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14791 GH36 1.12e-80 308 600 1 299
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.
COG3345 GalA 3.86e-22 262 612 246 596
Alpha-galactosidase [Carbohydrate transport and metabolism].
pfam02065 Melibiase 2.22e-21 268 608 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.
cd14790 GH_D 0.006 310 464 2 113
Glycoside hydrolases, clan D. This group of glycosyl hydrolase families is comprised of glycosyl hydrolase family 31 (GH31), family 36 (GH36), and family 27 (GH27). These structurally and mechanistically related protein families 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. They have a wide range of functions including alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase, alpha-N-acetylgalactosaminidase, stachyose synthase, raffinose synthase, and alpha-1,4-glucan lyase.
cd14792 GH27 0.009 313 391 5 84
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
BBF45383.1 9.41e-298 4 696 3 696
BBF42267.1 2.21e-293 4 695 2 695
BBI32765.1 1.09e-262 1 696 12 708
AIQ64284.1 6.46e-262 1 696 1 711
QNU68202.1 4.85e-250 4 696 3 692

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2XN0_A 2.00e-19 211 698 234 728
Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN0_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN1_A Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_C Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_D Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM]
2XN2_A 4.61e-19 211 698 234 728
Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM]
4FNQ_A 8.95e-17 247 612 271 639
Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
3MI6_A 2.09e-16 268 629 290 657
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]
4FNP_A 2.71e-16 247 612 271 639
Crystalstructure 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P43467 9.65e-21 211 646 232 669
Alpha-galactosidase 1 OS=Pediococcus pentosaceus OX=1255 GN=agaR PE=3 SV=1
G1UB44 1.10e-18 211 698 234 728
Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1
Q0CVH2 4.49e-18 128 643 185 686
Probable alpha-galactosidase C OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aglC PE=3 SV=1
Q9ALJ4 1.48e-15 247 612 271 639
Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA PE=1 SV=1
Q2TW69 3.49e-15 128 612 189 664
Probable alpha-galactosidase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aglC PE=3 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
1.000052 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003215_00984.