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CAZyme Information: MGYG000000364_01742

You are here: Home > Sequence: MGYG000000364_01742

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 Coprococcus sp900767685
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Coprococcus; Coprococcus sp900767685
CAZyme ID MGYG000000364_01742
CAZy Family GH36
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
735 MGYG000000364_12|CGC1 84727.99 5.0487
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000364 3039243 MAG Sweden Europe
Gene Location Start: 3070;  End: 5277  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000364_01742.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH36 5 659 2e-99 0.934593023255814

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14791 GH36 6.10e-98 324 617 2 299
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.
pfam02065 Melibiase 8.99e-42 285 624 1 346
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 3.32e-27 280 544 247 508
Alpha-galactosidase [Carbohydrate transport and metabolism].
cd14792 GH27 5.19e-08 328 474 5 124
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.
pfam16499 Melibiase_2 3.02e-04 353 408 45 98
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCN32114.1 0.0 1 729 1 703
ADL52223.1 0.0 1 730 1 700
QEH70556.1 0.0 1 732 1 702
ADZ85056.1 0.0 1 732 1 702
QHQ59595.1 2.10e-315 1 730 1 700

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4FNQ_A 1.82e-24 280 641 284 652
Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
2XN0_A 4.24e-24 270 527 277 538
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 5.60e-24 270 527 277 538
Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM]
6PHU_A 3.90e-19 280 637 298 662
SpAgawild type apo structure [Streptococcus pneumoniae TIGR4],6PHV_A Chain A, Alpha-galactosidase [Streptococcus pneumoniae TIGR4]
6PHW_A 1.56e-18 280 637 298 662
ChainA, Alpha-galactosidase [Streptococcus pneumoniae TIGR4],6PHX_A SpAga D472N structure in complex with raffinose [Streptococcus pneumoniae TIGR4],6PHY_A Chain A, Alpha-galactosidase [Streptococcus pneumoniae TIGR4],6PI0_A AgaD472N-Linear Blood group B type 2 trisaccharide complex structure [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
G1UB44 2.32e-23 270 527 277 538
Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1
P43467 6.96e-19 117 571 144 570
Alpha-galactosidase 1 OS=Pediococcus pentosaceus OX=1255 GN=agaR PE=3 SV=1
P27756 1.75e-16 279 544 277 544
Alpha-galactosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=aga PE=3 SV=3
P43469 1.11e-14 323 551 322 552
Alpha-galactosidase 2 OS=Pediococcus pentosaceus OX=1255 GN=agaS PE=3 SV=1
G4T4R7 3.03e-14 280 616 284 618
Bifunctional alpha-galactosidase/sucrose kinase AgaSK OS=Ruminococcus gnavus OX=33038 GN=agaSK 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
1.000056 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000364_01742.