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CAZyme Information: MGYG000001735_02944

You are here: Home > Sequence: MGYG000001735_02944

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; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides;
CAZyme ID MGYG000001735_02944
CAZy Family CE3
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
486 MGYG000001735_41|CGC1 54678.57 7.6181
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001735 5309957 MAG Sweden Europe
Gene Location Start: 10750;  End: 12210  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001735_02944.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE3 34 222 3e-41 0.9845360824742269

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0657 Aes 1.49e-32 245 478 60 312
Acetyl esterase/lipase [Lipid transport and metabolism].
pfam07859 Abhydrolase_3 1.69e-29 268 453 1 205
alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.
cd01833 XynB_like 2.49e-28 32 222 1 157
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
COG1506 DAP2 2.05e-21 234 453 364 594
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
pfam00326 Peptidase_S9 2.19e-14 283 453 2 187
Prolyl oligopeptidase family.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAX78799.1 2.40e-173 25 483 31 494
ATC65549.1 6.34e-138 34 483 40 492
QOV88633.1 4.36e-65 34 222 32 222
QDT00894.1 1.49e-60 236 483 34 283
QNN20991.1 2.79e-58 18 226 18 226

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5AO9_A 6.45e-51 236 486 16 281
Thestructure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-native [Thermogutta terrifontis],5AOA_A The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-Propionate bound [Thermogutta terrifontis],5AOB_A The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-butyrate bound [Thermogutta terrifontis],5AOC_A The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-valerate bound [Thermogutta terrifontis]
7BFN_A 6.63e-51 236 486 17 282
ChainA, Esterase [Thermogutta terrifontis]
7BFO_A 3.56e-50 236 486 17 282
ChainA, Esterase [Thermogutta terrifontis],7BFR_A Chain A, Esterase [Thermogutta terrifontis],7BFT_A Chain A, Esterase [Thermogutta terrifontis],7BFU_A Chain A, Esterase [Thermogutta terrifontis],7BFV_A Chain A, Esterase [Thermogutta terrifontis]
2YH2_A 2.51e-13 246 354 60 164
Pyrobaculumcalidifontis esterase monoclinic form [Pyrobaculum calidifontis],2YH2_B Pyrobaculum calidifontis esterase monoclinic form [Pyrobaculum calidifontis],2YH2_C Pyrobaculum calidifontis esterase monoclinic form [Pyrobaculum calidifontis],2YH2_D Pyrobaculum calidifontis esterase monoclinic form [Pyrobaculum calidifontis],3ZWQ_A Hyperthermophilic Esterase From The Archeon Pyrobaculum Calidifontis [Pyrobaculum calidifontis JCM 11548],3ZWQ_B Hyperthermophilic Esterase From The Archeon Pyrobaculum Calidifontis [Pyrobaculum calidifontis JCM 11548]
1QZ3_A 1.91e-12 246 453 57 282
CRYSTALSTRUCTURE OF MUTANT M211S/R215L OF CARBOXYLESTERASE EST2 COMPLEXED WITH HEXADECANESULFONATE [Alicyclobacillus acidocaldarius],1U4N_A Crystal Structure Analysis of the M211S/R215L EST2 mutant [Alicyclobacillus acidocaldarius]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P96402 1.08e-11 266 453 157 367
Esterase LipC OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=lipC PE=1 SV=1
Q9US38 1.04e-09 253 480 88 340
AB hydrolase superfamily protein C1039.03 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC1039.03 PE=3 SV=1
Q8VYP9 2.24e-09 233 453 176 420
Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL1 OS=Arabidopsis thaliana OX=3702 GN=ICMEL1 PE=2 SV=1
Q84LM4 2.15e-08 187 455 460 741
Acylamino-acid-releasing enzyme OS=Arabidopsis thaliana OX=3702 GN=AARE PE=1 SV=1
W7MTJ1 9.18e-08 229 457 42 289
Esterase FVEG_12639 OS=Gibberella moniliformis (strain M3125 / FGSC 7600) OX=334819 GN=FVEG_12639 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.231333 0.765897 0.001476 0.000401 0.000389 0.000480

TMHMM  Annotations      download full data without filtering help

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