You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000001074_01613
You are here: Home > Sequence: MGYG000001074_01613
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 | Prevotella sp002251365 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp002251365 | |||||||||||
| CAZyme ID | MGYG000001074_01613 | |||||||||||
| CAZy Family | GH27 | |||||||||||
| CAZyme Description | Isomalto-dextranase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 43; End: 954 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH27 | 30 | 280 | 4.1e-33 | 0.9344978165938864 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam17801 | Melibiase_C | 9.00e-18 | 231 | 300 | 5 | 74 | Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes. |
| PLN02808 | PLN02808 | 4.83e-10 | 205 | 303 | 286 | 386 | alpha-galactosidase |
| PLN02229 | PLN02229 | 7.73e-10 | 205 | 303 | 316 | 420 | alpha-galactosidase |
| cd14792 | GH27 | 1.14e-06 | 16 | 214 | 96 | 271 | 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. |
| PLN02692 | PLN02692 | 9.90e-06 | 205 | 300 | 310 | 408 | alpha-galactosidase |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QNT67171.1 | 1.25e-173 | 3 | 300 | 176 | 473 |
| QUT44530.1 | 2.51e-138 | 1 | 301 | 184 | 491 |
| QUT79686.1 | 2.51e-138 | 1 | 301 | 184 | 491 |
| QRM98947.1 | 2.51e-138 | 1 | 301 | 184 | 491 |
| QUU07210.1 | 1.01e-137 | 1 | 301 | 184 | 491 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5AWO_A | 2.52e-74 | 12 | 301 | 170 | 466 | Arthrobacterglobiformis T6 isomalto-dextranse [Arthrobacter globiformis],5AWP_A Arthrobacter globiformis T6 isomalto-dextranase complexed with isomaltose [Arthrobacter globiformis],5AWQ_A Arthrobacter globiformis T6 isomalto-dextranse complexed with panose [Arthrobacter globiformis] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q44052 | 3.42e-74 | 12 | 301 | 196 | 492 | Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1 |
| P14749 | 1.89e-09 | 181 | 303 | 291 | 410 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
| Q42656 | 1.01e-08 | 169 | 303 | 241 | 378 | Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1 |
| Q99172 | 5.18e-06 | 169 | 294 | 271 | 417 | Alpha-galactosidase OS=Lachancea cidri OX=29831 GN=MEL 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 |
|---|---|---|---|---|---|
| 1.000058 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |