logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000501_01622

You are here: Home > Sequence: MGYG000000501_01622

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 CAG-127 sp900553925
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-127; CAG-127 sp900553925
CAZyme ID MGYG000000501_01622
CAZy Family GH1
CAZyme Description Aryl-phospho-beta-D-glucosidase BglC
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
482 MGYG000000501_10|CGC1 55458.55 5.2487
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000501 2730672 MAG Fiji Oceania
Gene Location Start: 3779;  End: 5227  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.86 3.2.1.85 3.2.1.21 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH1 7 479 3.7e-166 0.9906759906759907

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG2723 BglB 0.0 7 481 2 456
Beta-glucosidase/6-phospho-beta-glucosidase/beta-galactosidase [Carbohydrate transport and metabolism].
pfam00232 Glyco_hydro_1 0.0 9 480 5 453
Glycosyl hydrolase family 1.
TIGR03356 BGL 8.22e-164 10 471 1 426
beta-galactosidase.
PRK13511 PRK13511 1.59e-128 5 477 1 465
6-phospho-beta-galactosidase; Provisional
PRK09589 celA 1.43e-126 8 482 3 476
6-phospho-beta-glucosidase; Reviewed

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QWT51984.1 0.0 1 482 1 482
QNM00066.1 0.0 1 482 1 482
CBK82929.1 0.0 1 482 1 482
QMW75724.1 2.10e-317 1 482 1 482
QQY27239.1 2.10e-317 1 482 1 482

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZE4_A 1.81e-217 7 482 14 485
Structureof Gan1D, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4ZE4_B Structure of Gan1D, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4ZEN_A Structure of Gan1D, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with 6-phospho-beta-galactose [Geobacillus stearothermophilus],4ZEN_B Structure of Gan1D, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with 6-phospho-beta-galactose [Geobacillus stearothermophilus],4ZEP_A Structure of Gan1D, a 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with 6-phospho-glucose [Geobacillus stearothermophilus],4ZEP_B Structure of Gan1D, a 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with 6-phospho-glucose [Geobacillus stearothermophilus],5OKB_A High resolution structure of native Gan1D, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5OKB_B High resolution structure of native Gan1D, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5OKB_C High resolution structure of native Gan1D, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5OKB_D High resolution structure of native Gan1D, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5OKH_A Conservatively refined structure of Gan1D-WT, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in the C2 spacegroup [Geobacillus stearothermophilus],5OKH_B Conservatively refined structure of Gan1D-WT, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in the C2 spacegroup [Geobacillus stearothermophilus],5OKJ_A Non-conservatively refined structure of Gan1D-WT, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in the C2 spacegroup [Geobacillus stearothermophilus],5OKJ_B Non-conservatively refined structure of Gan1D-WT, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in the C2 spacegroup [Geobacillus stearothermophilus],5OKK_A Conservatively refined structure of Gan1D-WT, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with 6-phospho-beta-galactose [Geobacillus stearothermophilus],5OKK_B Conservatively refined structure of Gan1D-WT, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with 6-phospho-beta-galactose [Geobacillus stearothermophilus],5OKQ_A Non-conservatively refined structure of Gan1D-WT, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with 6-phospho-beta-galactose [Geobacillus stearothermophilus],5OKQ_B Non-conservatively refined structure of Gan1D-WT, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with 6-phospho-beta-galactose [Geobacillus stearothermophilus],5OKR_A Conservatively refined structure of Gan1D-WT, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with 6-phospho-beta-glucose [Geobacillus stearothermophilus],5OKR_B Conservatively refined structure of Gan1D-WT, a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with 6-phospho-beta-glucose [Geobacillus stearothermophilus],5OKS_A Non-conservatively refined structure of Gan1D, a 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with 6-phospho-beta-glucose [Geobacillus stearothermophilus],5OKS_B Non-conservatively refined structure of Gan1D, a 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with 6-phospho-beta-glucose [Geobacillus stearothermophilus]
4ZE5_A 5.18e-217 7 482 14 485
Structureof Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4ZE5_B Structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4ZE5_C Structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4ZE5_D Structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4ZFM_A Structure of Gan1D-E170Q in complex with cellobiose-6-phosphate [Geobacillus stearothermophilus],4ZFM_B Structure of Gan1D-E170Q in complex with cellobiose-6-phosphate [Geobacillus stearothermophilus],4ZFM_C Structure of Gan1D-E170Q in complex with cellobiose-6-phosphate [Geobacillus stearothermophilus],4ZFM_D Structure of Gan1D-E170Q in complex with cellobiose-6-phosphate [Geobacillus stearothermophilus],5OK7_A Conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5OK7_B Conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5OK7_C Conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5OK7_D Conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5OKA_A Non-conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5OKA_B Non-conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5OKA_C Non-conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5OKA_D Non-conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a 6-phospho-beta-galactosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5OKE_A Conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with cellobiose-6-phosphate [Geobacillus stearothermophilus],5OKE_B Conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with cellobiose-6-phosphate [Geobacillus stearothermophilus],5OKE_C Conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with cellobiose-6-phosphate [Geobacillus stearothermophilus],5OKE_D Conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with cellobiose-6-phosphate [Geobacillus stearothermophilus],5OKG_A Non-conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with cellobiose-6-phosphate [Geobacillus stearothermophilus],5OKG_B Non-conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with cellobiose-6-phosphate [Geobacillus stearothermophilus],5OKG_C Non-conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with cellobiose-6-phosphate [Geobacillus stearothermophilus],5OKG_D Non-conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with cellobiose-6-phosphate [Geobacillus stearothermophilus]
7M1R_A 7.98e-208 1 482 3 480
ChainA, 6-phospho-beta-galactosidase [Bacillus licheniformis],7M1R_B Chain B, 6-phospho-beta-galactosidase [Bacillus licheniformis],7M1R_C Chain C, 6-phospho-beta-galactosidase [Bacillus licheniformis],7M1R_D Chain D, 6-phospho-beta-galactosidase [Bacillus licheniformis]
5YHS_A 2.30e-151 9 482 3 469
Pyruvylatedbeta-D-galactosidase from Bacillus sp. HMA207, apo form [Bacillus sp. (in: Bacteria)],5YHS_B Pyruvylated beta-D-galactosidase from Bacillus sp. HMA207, apo form [Bacillus sp. (in: Bacteria)]
5YIF_A 1.86e-150 9 482 3 469
Pyruvylatedbeta-D-galactosidase from Bacillus sp. HMA207, E163A mutant pyruvylated beta-D-galactose complex [Bacillus sp. (in: Bacteria)],5YIF_B Pyruvylated beta-D-galactosidase from Bacillus sp. HMA207, E163A mutant pyruvylated beta-D-galactose complex [Bacillus sp. (in: Bacteria)]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P42403 5.91e-209 1 482 1 477
Aryl-phospho-beta-D-glucosidase BglC OS=Bacillus subtilis (strain 168) OX=224308 GN=bglC PE=1 SV=1
Q46829 4.83e-116 5 482 4 479
6-phospho-beta-glucosidase BglA OS=Escherichia coli (strain K12) OX=83333 GN=bglA PE=1 SV=2
P42973 4.88e-113 10 482 5 479
Aryl-phospho-beta-D-glucosidase BglA OS=Bacillus subtilis (strain 168) OX=224308 GN=bglA PE=1 SV=1
P40740 7.16e-113 7 482 6 469
Aryl-phospho-beta-D-glucosidase BglH OS=Bacillus subtilis (strain 168) OX=224308 GN=bglH PE=1 SV=2
P26208 2.69e-107 9 479 6 447
Beta-glucosidase A OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=bglA 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
1.000064 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000501_01622.