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CAZyme Information: MGYG000003484_00401

You are here: Home > Sequence: MGYG000003484_00401

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 RUG806 sp900313475
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; RUG806; RUG806 sp900313475
CAZyme ID MGYG000003484_00401
CAZy Family GH36
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
503 56855.9 4.6961
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003484 2443711 MAG Fiji Oceania
Gene Location Start: 37888;  End: 39399  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003484_00401.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH36 145 389 2.2e-23 0.35901162790697677

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14791 GH36 2.18e-38 172 467 2 295
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 2.48e-09 172 424 292 569
Alpha-galactosidase [Carbohydrate transport and metabolism].
cd14792 GH27 2.02e-06 173 421 1 219
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.
cd14790 GH_D 1.73e-05 204 422 30 206
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AZN41597.1 3.24e-125 25 501 35 519
QCU01578.1 1.62e-119 46 501 78 539
CBL19648.1 2.29e-119 37 501 70 539
ANE49069.1 1.53e-118 57 501 18 473
SNU96820.1 4.98e-114 37 491 50 510

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5M0X_A 1.57e-09 165 425 198 457
Structureof apo structure of GH36 alpha-galactosidase from Thermotoga maritima [Thermotoga maritima],5M12_A Structure of GH36 alpha-galactosidase from Thermotoga maritima in complex with intact cyclopropyl-carbasugar. [Thermotoga maritima],5M16_A Structure of GH36 alpha-galactosidase from Thermotoga maritima in complex with a hydrolysed cyclopropyl carbasugar. [Thermotoga maritima],5M1I_A Structure of GH36 alpha-galactosidase from Thermotoga maritima in a covalent complex with a cyclopropyl carbasugar. [Thermotoga maritima],6GVD_A Alpha-galactosidase from Thermotoga maritima in complex with cyclohexene-based carbasugar mimic of galactose [Thermotoga maritima MSB8],6GWG_A Alpha-galactosidase from Thermotoga maritima in complex with cyclohexene-based carbasugar mimic of galactose covalently linked to the nucleophile [Thermotoga maritima MSB8],6GX8_A Alpha-galactosidase from Thermotoga maritima in complex with hydrolysed cyclohexene-based carbasugar mimic of galactose [Thermotoga maritima MSB8]
1ZY9_A 6.24e-09 165 425 187 446
Crystalstructure of Alpha-galactosidase (EC 3.2.1.22) (Melibiase) (tm1192) from Thermotoga maritima at 2.34 A resolution [Thermotoga maritima]
6GTA_A 1.46e-08 165 425 198 457
Alpha-galactosidasemutant D378A from Thermotoga maritima in complex with intact cyclohexene-based carbasugar mimic of galactose with 3,5 difluorophenyl leaving group [Thermotoga maritima MSB8],6GWF_A Alpha-galactosidase mutant D387A from Thermotoga maritima in complex with intact cyclohexene-based carbasugar mimic of galactose with 2,4-dinitro leaving group [Thermotoga maritima MSB8]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
G4FEF4 8.33e-09 165 425 175 434
Alpha-galactosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=galA 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
1.000067 0.000003 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003484_00401.