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CAZyme Information: MGYG000000781_00240
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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 | Phocaeicola sp900541515 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900541515 | |||||||||||
| CAZyme ID | MGYG000000781_00240 | |||||||||||
| CAZy Family | GH91 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 18657; End: 20624 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH91 | 34 | 374 | 7.5e-87 | 0.9341772151898734 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd21111 | IFTase | 3.95e-54 | 35 | 365 | 39 | 351 | inulin fructotransferase. Inulin fructotransferase (IFTase; EC 4.2.2.17 and EC 4.2.2.18), a member of the glycoside hydrolase family 91, catalyzes depolymerization of beta-2,1-fructans inulin by successively removing the terminal difructosaccharide units as cyclic anhydrides via intramolecular fructosyl transfer. As a result, IFTase produces DFA-I (alpha-D-fructofuranose-beta-D-fructofuranose 2',1:2,1'-dianhydride) and DFA-III (alpha-D-fructofuranose-beta-D-fructofuranose 2',1:2,3'-dianhydride). |
| pfam16324 | DUF4960 | 1.46e-23 | 402 | 652 | 13 | 253 | Domain of unknown function (DUF4960). This family consists of uncharacterized proteins around 460 residues in length and is mainly found in various Bacteroides species. The function of this protein is unknown. |
| pfam12708 | Pectate_lyase_3 | 7.33e-07 | 34 | 102 | 4 | 72 | Pectate lyase superfamily protein. This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28. |
| pfam05048 | NosD | 0.004 | 203 | 330 | 20 | 133 | Periplasmic copper-binding protein (NosD). NosD is a periplasmic protein which is thought to insert copper into the exported reductase apoenzyme (NosZ). This region forms a parallel beta helix domain. |
| pfam13229 | Beta_helix | 0.007 | 205 | 326 | 3 | 113 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QRP58813.1 | 4.85e-205 | 2 | 652 | 5 | 646 |
| QQT79303.1 | 4.85e-205 | 2 | 652 | 5 | 646 |
| ASM67439.1 | 4.85e-205 | 2 | 652 | 5 | 646 |
| QUU10136.1 | 1.95e-204 | 2 | 652 | 5 | 646 |
| QNL38719.1 | 3.97e-201 | 15 | 652 | 18 | 645 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2INU_A | 4.78e-25 | 44 | 334 | 31 | 345 | Crystalstructure of Inulin fructotransferase in the absence of substrate [Bacillus sp. snu-7],2INU_B Crystal structure of Inulin fructotransferase in the absence of substrate [Bacillus sp. snu-7],2INU_C Crystal structure of Inulin fructotransferase in the absence of substrate [Bacillus sp. snu-7],2INV_A Crystal structure of Inulin fructotransferase in the presence of di-fructose [Bacillus sp. snu-7],2INV_B Crystal structure of Inulin fructotransferase in the presence of di-fructose [Bacillus sp. snu-7],2INV_C Crystal structure of Inulin fructotransferase in the presence of di-fructose [Bacillus sp. snu-7] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P19870 | 2.26e-17 | 33 | 334 | 8 | 329 | Inulin fructotransferase [DFA-I-forming] OS=Arthrobacter globiformis OX=1665 PE=1 SV=3 |
SignalP and Lipop Annotations help
This protein is predicted as LIPO
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000554 | 0.103536 | 0.895606 | 0.000098 | 0.000112 | 0.000101 |