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CAZyme Information: MGYG000001760_02125
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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 | UBA1417 sp900549945 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA1417; UBA1417 sp900549945 | |||||||||||
| CAZyme ID | MGYG000001760_02125 | |||||||||||
| CAZy Family | CE1 | |||||||||||
| CAZyme Description | Hydroxyacylglutathione hydrolase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 4282; End: 5760 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE1 | 12 | 220 | 1.2e-19 | 0.5991189427312775 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd07712 | MBLAC2-like_MBL-fold | 1.52e-47 | 249 | 425 | 1 | 182 | uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain. Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. |
| COG4099 | COG4099 | 3.46e-44 | 17 | 235 | 178 | 387 | Predicted peptidase [General function prediction only]. |
| cd06262 | metallo-hydrolase-like_MBL-fold | 1.94e-26 | 260 | 425 | 13 | 188 | mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site. |
| smart00849 | Lactamase_B | 1.33e-24 | 258 | 413 | 1 | 171 | Metallo-beta-lactamase superfamily. Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor. |
| COG0491 | GloB | 6.60e-20 | 251 | 425 | 19 | 210 | Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ABS60377.1 | 2.53e-50 | 17 | 236 | 26 | 246 |
| BCI61582.1 | 1.93e-34 | 18 | 233 | 835 | 1041 |
| QDU56037.1 | 5.90e-32 | 26 | 235 | 817 | 1007 |
| QJW36208.1 | 4.75e-23 | 28 | 237 | 859 | 1090 |
| QJW99051.1 | 1.00e-22 | 2 | 235 | 36 | 240 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3DOH_A | 1.61e-49 | 27 | 235 | 173 | 380 | CrystalStructure of a Thermostable Esterase [Thermotoga maritima],3DOH_B Crystal Structure of a Thermostable Esterase [Thermotoga maritima],3DOI_A Crystal Structure of a Thermostable Esterase complex with paraoxon [Thermotoga maritima],3DOI_B Crystal Structure of a Thermostable Esterase complex with paraoxon [Thermotoga maritima] |
| 3WYD_A | 8.89e-16 | 6 | 203 | 14 | 195 | C-terminalesterase domain of LC-Est1 [uncultured organism],3WYD_B C-terminal esterase domain of LC-Est1 [uncultured organism] |
| 4Q82_A | 9.49e-14 | 18 | 235 | 70 | 277 | CrystalStructure of Phospholipase/Carboxylesterase from Haliangium ochraceum [Haliangium ochraceum DSM 14365],4Q82_B Crystal Structure of Phospholipase/Carboxylesterase from Haliangium ochraceum [Haliangium ochraceum DSM 14365] |
| 2ZWR_A | 7.14e-07 | 257 | 385 | 13 | 146 | Crystalstructure of TTHA1623 from thermus thermophilus HB8 [Thermus thermophilus HB8],2ZWR_B Crystal structure of TTHA1623 from thermus thermophilus HB8 [Thermus thermophilus HB8],2ZZI_A Crystal structure of TTHA1623 in a di-iron-bound form [Thermus thermophilus HB8],2ZZI_B Crystal structure of TTHA1623 in a di-iron-bound form [Thermus thermophilus HB8] |
| 6N36_A | 7.42e-06 | 232 | 379 | 13 | 181 | Beta-lactamasefrom Chitinophaga pinensis [Chitinophaga pinensis DSM 2588] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q68D91 | 3.41e-11 | 226 | 385 | 3 | 191 | Acyl-coenzyme A thioesterase MBLAC2 OS=Homo sapiens OX=9606 GN=MBLAC2 PE=1 SV=3 |
| A5PJT0 | 8.28e-11 | 226 | 385 | 3 | 191 | Acyl-coenzyme A thioesterase MBLAC2 OS=Bos taurus OX=9913 GN=MBLAC2 PE=2 SV=1 |
| Q5F336 | 1.97e-10 | 246 | 385 | 14 | 188 | Acyl-coenzyme A thioesterase MBLAC2 OS=Gallus gallus OX=9031 GN=MBLAC2 PE=2 SV=1 |
| Q8BL86 | 2.01e-10 | 226 | 385 | 3 | 191 | Acyl-coenzyme A thioesterase MBLAC2 OS=Mus musculus OX=10090 GN=Mblac2 PE=1 SV=2 |
| Q57544 | 5.08e-10 | 254 | 425 | 11 | 192 | Hydroxyacylglutathione hydrolase GloC OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=gloC 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 |
|---|---|---|---|---|---|
| 1.000057 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |