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CAZyme Information: MGYG000002941_00220
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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 | Actinomyces graevenitzii | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Actinomyces; Actinomyces graevenitzii | |||||||||||
| CAZyme ID | MGYG000002941_00220 | |||||||||||
| CAZy Family | GH42 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 4893; End: 7199 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH42 | 17 | 389 | 1.6e-147 | 0.9946091644204852 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam02449 | Glyco_hydro_42 | 2.25e-175 | 17 | 391 | 1 | 376 | Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues. |
| COG1874 | GanA | 9.03e-122 | 2 | 527 | 4 | 513 | Beta-galactosidase GanA [Carbohydrate transport and metabolism]. |
| pfam08532 | Glyco_hydro_42M | 8.19e-25 | 401 | 705 | 1 | 207 | Beta-galactosidase trimerisation domain. This is non catalytic domain B of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. This domain is related to glutamine amidotransferase enzymes, but the catalytic residues are replaced by non functional amino acids. This domain is involved in trimerisation. |
| cd03143 | A4_beta-galactosidase_middle_domain | 1.51e-15 | 403 | 528 | 1 | 112 | A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QLF54010.1 | 4.71e-239 | 13 | 765 | 36 | 743 |
| VEI16011.1 | 1.79e-237 | 13 | 765 | 47 | 754 |
| AMD99363.1 | 3.06e-237 | 13 | 764 | 25 | 731 |
| QQQ58730.1 | 5.99e-237 | 13 | 765 | 25 | 732 |
| QCT33733.1 | 1.40e-235 | 13 | 766 | 36 | 744 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4UCF_A | 1.51e-120 | 12 | 519 | 20 | 516 | Crystalstructure of Bifidobacterium bifidum beta-galactosidase in complex with alpha-galactose [Bifidobacterium bifidum S17],4UCF_B Crystal structure of Bifidobacterium bifidum beta-galactosidase in complex with alpha-galactose [Bifidobacterium bifidum S17],4UCF_C Crystal structure of Bifidobacterium bifidum beta-galactosidase in complex with alpha-galactose [Bifidobacterium bifidum S17],4UZS_A Crystal structure of Bifidobacterium bifidum beta-galactosidase [Bifidobacterium bifidum S17],4UZS_B Crystal structure of Bifidobacterium bifidum beta-galactosidase [Bifidobacterium bifidum S17],4UZS_C Crystal structure of Bifidobacterium bifidum beta-galactosidase [Bifidobacterium bifidum S17] |
| 5E9A_A | 9.00e-118 | 12 | 511 | 39 | 526 | Crystalstructure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_B Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_C Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_D Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_E Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_F Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3] |
| 3TTS_A | 1.49e-115 | 14 | 519 | 11 | 502 | ChainA, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_B Chain B, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_C Chain C, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_D Chain D, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_E Chain E, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_F Chain F, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_A Chain A, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_B Chain B, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_C Chain C, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_D Chain D, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_E Chain E, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_F Chain F, Beta-galactosidase [Niallia circulans subsp. alkalophilus] |
| 4UNI_A | 2.08e-113 | 14 | 510 | 25 | 511 | beta-(1,6)-galactosidasefrom Bifidobacterium animalis subsp. lactis Bl-04 in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04],4UNI_B beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04],4UNI_C beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04] |
| 4UOQ_A | 1.58e-112 | 14 | 510 | 25 | 511 | Nucleophilemutant (E324A) of beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis Bl-04],4UOQ_B Nucleophile mutant (E324A) of beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis Bl-04],4UOQ_C Nucleophile mutant (E324A) of beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis Bl-04],4UOZ_A beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 nucleophile mutant E324A in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04],4UOZ_B beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 nucleophile mutant E324A in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04],4UOZ_C beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 nucleophile mutant E324A in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| C7ASJ5 | 1.35e-146 | 12 | 519 | 42 | 534 | Beta-galactosidase OS=Arthrobacter sp. OX=1667 PE=1 SV=1 |
| C9S0R2 | 1.54e-145 | 11 | 536 | 6 | 523 | Beta-galactosidase BgaB OS=Geobacillus sp. (strain Y412MC61) OX=544556 GN=bgaB PE=3 SV=1 |
| P19668 | 4.30e-145 | 11 | 536 | 6 | 523 | Beta-galactosidase bgaB OS=Geobacillus kaustophilus OX=1462 GN=bgaB PE=1 SV=1 |
| D5JGG0 | 3.28e-135 | 14 | 519 | 10 | 497 | Beta-galactosidase LacZ OS=Weizmannia coagulans OX=1398 GN=lacZ PE=3 SV=1 |
| Q9RFN0 | 2.35e-120 | 12 | 519 | 7 | 496 | Beta-galactosidase BgaB OS=Carnobacterium maltaromaticum OX=2751 GN=bgaB 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 |
|---|---|---|---|---|---|
| 1.000049 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |