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CAZyme Information: MGYG000004689_01609
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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 | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Bariatricus; | |||||||||||
| CAZyme ID | MGYG000004689_01609 | |||||||||||
| CAZy Family | GH27 | |||||||||||
| CAZyme Description | Isomalto-dextranase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 10161; End: 11501 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH27 | 173 | 423 | 4.9e-27 | 0.9432314410480349 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam17801 | Melibiase_C | 1.12e-10 | 374 | 442 | 6 | 74 | Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes. |
| PLN02808 | PLN02808 | 3.80e-06 | 300 | 445 | 237 | 386 | alpha-galactosidase |
| PLN02229 | PLN02229 | 7.27e-06 | 260 | 439 | 233 | 414 | alpha-galactosidase |
| cd14792 | GH27 | 2.90e-05 | 14 | 354 | 8 | 269 | 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 |
|---|---|---|---|---|---|
| AZB42116.1 | 3.03e-131 | 6 | 442 | 35 | 466 |
| QST00336.1 | 6.56e-130 | 7 | 446 | 36 | 470 |
| ARI79039.1 | 1.23e-127 | 7 | 446 | 37 | 471 |
| ALJ61711.1 | 2.94e-122 | 9 | 446 | 34 | 445 |
| QUT92727.1 | 8.33e-122 | 9 | 446 | 34 | 445 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5AWO_A | 3.12e-113 | 10 | 443 | 37 | 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 | 3.60e-113 | 10 | 443 | 63 | 492 | Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd 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 |
|---|---|---|---|---|---|
| 1.000085 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |