| Species | Paenibacillus_A ihumii | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii | |||||||||||
| CAZyme ID | MGYG000001514_04506 | |||||||||||
| CAZy Family | GH94 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 3270364; End: 3273093 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH94 | 69 | 876 | 6.9e-150 | 0.6640926640926641 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd11749 | GH94N_LBP_like | 5.96e-132 | 74 | 302 | 1 | 229 | N-terminal-like domain of Paenibacillus sp. YM-1 Laminaribiose Phosphorylase and similar proteins. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes bacterial laminaribiose phosphorylase. This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Bacterial laminaribiose phosphorylase phosphorolyzes laminaribiose into alpha-glucose 1-phosphate and glucose, but does not phosphorolyze other glucobioses; it slightly phosphorolyzed laminaritriose and higher laminarioligosaccharides. The GH64N domain, as represented by this model, is also found at the N-terminus of GH94 members with uncharacterized specificities. |
| COG3459 | COG3459 | 1.98e-37 | 86 | 896 | 349 | 1056 | Cellobiose phosphorylase [Carbohydrate transport and metabolism]. |
| pfam17167 | Glyco_hydro_36 | 1.55e-22 | 322 | 814 | 1 | 425 | Glycosyl hydrolase 36 superfamily, catalytic domain. This is the catalytic region of the superfamily of enzymes referred to as GH36. UniProtKB:Q76IQ9 is a chitobiose phosphorylase that catalyzes the reversible phosphorolysis of chitobiose into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration. The full-length enzyme comprises a beta sandwich domain and an (alpha/alpha)(6) barrel domain. The alpha-helical barrel component of the domain, this family, is the catalytic region. |
| cd11746 | GH94N_like | 2.56e-22 | 79 | 292 | 7 | 179 | N-terminal domain of glycoside hydrolase family 94 and related domains. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. This GH64N domain also occurs in tandem repeat arrangements (not at the N-terminus) in cyclic beta 1-2 glucan synthetase and related proteins, and as a standalone domain in distantly related proteins of unknown function. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AZK48182.1 | 0.0 | 1 | 909 | 1 | 909 |
| BAJ10826.1 | 0.0 | 1 | 906 | 1 | 906 |
| AZS16671.1 | 0.0 | 1 | 907 | 1 | 906 |
| AVV57046.1 | 0.0 | 1 | 894 | 1 | 895 |
| ANA79038.1 | 0.0 | 1 | 894 | 1 | 895 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6GGY_A | 0.0 | 1 | 906 | 3 | 908 | Paenibacillussp. YM1 laminaribiose phosphorylase with sulphate bound [Paenibacillus sp. YM1],6GGY_B Paenibacillus sp. YM1 laminaribiose phosphorylase with sulphate bound [Paenibacillus sp. YM1],6GH2_A Paenibacillus sp. YM1 laminaribiose phosphorylase with alpha-glc-1-phosphate bound [Paenibacillus sp. YM1],6GH2_B Paenibacillus sp. YM1 laminaribiose phosphorylase with alpha-glc-1-phosphate bound [Paenibacillus sp. YM1],6GH3_A Paenibacillus sp. YM1 laminaribiose phosphorylase with alpha-man-1-phosphate bound [Paenibacillus sp. YM1],6GH3_B Paenibacillus sp. YM1 laminaribiose phosphorylase with alpha-man-1-phosphate bound [Paenibacillus sp. YM1] |
| 3RRS_A | 4.99e-14 | 124 | 826 | 112 | 761 | Crystalstructure analysis of cellobiose phosphorylase from Cellulomonas uda [Cellulomonas uda],3RRS_B Crystal structure analysis of cellobiose phosphorylase from Cellulomonas uda [Cellulomonas uda],3RSY_A Cellobiose phosphorylase from Cellulomonas uda in complex with sulfate and glycerol [Cellulomonas uda],3RSY_B Cellobiose phosphorylase from Cellulomonas uda in complex with sulfate and glycerol [Cellulomonas uda],3S4A_A Cellobiose phosphorylase from Cellulomonas uda in complex with cellobiose [Cellulomonas uda],3S4A_B Cellobiose phosphorylase from Cellulomonas uda in complex with cellobiose [Cellulomonas uda],3S4B_A Cellobiose phosphorylase from Cellulomonas uda in complex with glucose [Cellulomonas uda],3S4B_B Cellobiose phosphorylase from Cellulomonas uda in complex with glucose [Cellulomonas uda] |
| 3S4C_A | 1.96e-13 | 124 | 826 | 112 | 761 | Lactosephosphorylase in complex with sulfate [Cellulomonas uda],3S4D_A Lactose phosphorylase in a ternary complex with cellobiose and sulfate [Cellulomonas uda] |
| 1V7V_A | 4.11e-10 | 101 | 876 | 94 | 782 | Crystalstructure of Vibrio proteolyticus chitobiose phosphorylase [Vibrio proteolyticus],1V7W_A Crystal structure of Vibrio proteolyticus chitobiose phosphorylase in complex with GlcNAc [Vibrio proteolyticus],1V7X_A Crystal structure of Vibrio proteolyticus chitobiose phosphorylase in complex with GlcNAc and sulfate [Vibrio proteolyticus] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q7S0S2 | 1.29e-09 | 123 | 826 | 128 | 731 | Cellobionic acid phosphorylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=NCU09425 PE=1 SV=1 |
| Q76IQ9 | 2.24e-09 | 101 | 876 | 94 | 782 | N,N'-diacetylchitobiose phosphorylase OS=Vibrio proteolyticus OX=671 GN=chbP PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000049 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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