You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000004576_00674
You are here: Home > Sequence: MGYG000004576_00674
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 | UMGS1688 sp900553825 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-917; UMGS1688; UMGS1688 sp900553825 | |||||||||||
| CAZyme ID | MGYG000004576_00674 | |||||||||||
| CAZy Family | GH36 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 61312; End: 62985 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH36 | 184 | 415 | 4.7e-49 | 0.35755813953488375 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd14791 | GH36 | 8.59e-78 | 205 | 509 | 1 | 292 | 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 | 6.46e-25 | 205 | 360 | 291 | 454 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
| pfam02065 | Melibiase | 1.27e-15 | 243 | 356 | 75 | 190 | 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. |
| cd06592 | GH31_NET37 | 1.08e-13 | 210 | 376 | 5 | 169 | glucosidase NET37. NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 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. |
| cd14792 | GH27 | 3.80e-13 | 209 | 380 | 4 | 146 | 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 |
|---|---|---|---|---|---|
| BAV13128.1 | 1.40e-140 | 33 | 548 | 38 | 552 |
| ADU21146.1 | 1.23e-127 | 24 | 548 | 14 | 547 |
| AXB28857.1 | 1.75e-121 | 65 | 515 | 54 | 501 |
| ATO98961.1 | 2.00e-119 | 65 | 546 | 54 | 532 |
| QIA42637.1 | 2.00e-119 | 65 | 546 | 54 | 532 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6LCJ_A | 4.13e-45 | 183 | 414 | 138 | 359 | TtGalA,alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_B TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_C TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_D TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_E TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_F TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCK_A TtGalA, alpha-galactosidase from Thermus thermophilus in complex with p-nitrophenyl alpha-D-galactopyranoside (alpha-NPG) [Thermus thermophilus HB8],6LCK_B TtGalA, alpha-galactosidase from Thermus thermophilus in complex with p-nitrophenyl alpha-D-galactopyranoside (alpha-NPG) [Thermus thermophilus HB8],6LCK_C TtGalA, alpha-galactosidase from Thermus thermophilus in complex with p-nitrophenyl alpha-D-galactopyranoside (alpha-NPG) [Thermus thermophilus HB8],6LCL_A TtGalA, alpha-galactosidase from Thermus thermophilus in complex with stachyose [Thermus thermophilus HB8],6LCL_C TtGalA, alpha-galactosidase from Thermus thermophilus in complex with stachyose [Thermus thermophilus HB8],6LCL_E TtGalA, alpha-galactosidase from Thermus thermophilus in complex with stachyose [Thermus thermophilus HB8] |
| 5M0X_A | 4.01e-37 | 168 | 551 | 165 | 543 | 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] |
| 6GTA_A | 3.44e-36 | 168 | 551 | 165 | 543 | 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] |
| 1ZY9_A | 5.69e-36 | 208 | 551 | 197 | 532 | Crystalstructure of Alpha-galactosidase (EC 3.2.1.22) (Melibiase) (tm1192) from Thermotoga maritima at 2.34 A resolution [Thermotoga maritima] |
| 2XN0_A | 3.12e-10 | 242 | 356 | 366 | 482 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| G4FEF4 | 1.71e-36 | 168 | 551 | 142 | 520 | Alpha-galactosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=galA PE=1 SV=1 |
| P43467 | 9.83e-10 | 242 | 384 | 364 | 511 | Alpha-galactosidase 1 OS=Pediococcus pentosaceus OX=1255 GN=agaR PE=3 SV=1 |
| G1UB44 | 1.71e-09 | 242 | 356 | 366 | 482 | Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1 |
| P27756 | 2.95e-09 | 242 | 357 | 356 | 473 | Alpha-galactosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=aga PE=3 SV=3 |
| P43469 | 1.07e-07 | 247 | 337 | 368 | 453 | 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 | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000086 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |