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CAZyme Information: MGYG000001553_02319

You are here: Home > Sequence: MGYG000001553_02319

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 Clostridium_P mediterraneense
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_P; Clostridium_P mediterraneense
CAZyme ID MGYG000001553_02319
CAZy Family GH1
CAZyme Description Aryl-phospho-beta-D-glucosidase BglC
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
479 MGYG000001553_5|CGC17 55376.58 5.1799
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001553 3045114 Isolate not provided not provided
Gene Location Start: 2029436;  End: 2030875  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 8 476 4.7e-169 0.9883449883449883

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG2723 BglB 0.0 8 477 3 455
Beta-glucosidase/6-phospho-beta-glucosidase/beta-galactosidase [Carbohydrate transport and metabolism].
pfam00232 Glyco_hydro_1 0.0 7 476 3 452
Glycosyl hydrolase family 1.
TIGR03356 BGL 1.82e-176 10 468 1 426
beta-galactosidase.
PRK09589 celA 2.38e-139 9 479 4 476
6-phospho-beta-glucosidase; Reviewed
PRK15014 PRK15014 1.91e-130 12 479 9 477
6-phospho-beta-glucosidase BglA; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QSW21125.1 0.0 1 479 1 479
AQS08914.1 4.83e-312 1 479 1 479
AQR99182.1 5.63e-311 1 479 1 479
AQS13170.1 5.63e-311 1 479 1 479
AQR89281.1 1.13e-310 1 479 1 479

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7M1R_A 1.69e-258 1 479 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]
4ZE4_A 4.52e-255 4 479 11 485
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 1.29e-254 4 479 11 485
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]
6Z1H_A 1.97e-150 9 479 11 452
ChainA, ANCESTRAL RECONSTRUCTED GLYCOSIDASE [synthetic construct],6Z1H_B Chain B, ANCESTRAL RECONSTRUCTED GLYCOSIDASE [synthetic construct],6Z1M_A Chain A, Ancestral reconstructed glycosidase [synthetic construct],6Z1M_B Chain B, Ancestral reconstructed glycosidase [synthetic construct],6Z1M_C Chain C, Ancestral reconstructed glycosidase [synthetic construct]
5YHS_A 3.72e-144 9 479 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)]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P42403 4.32e-260 1 479 1 477
Aryl-phospho-beta-D-glucosidase BglC OS=Bacillus subtilis (strain 168) OX=224308 GN=bglC PE=1 SV=1
Q46829 9.34e-124 1 479 1 479
6-phospho-beta-glucosidase BglA OS=Escherichia coli (strain K12) OX=83333 GN=bglA PE=1 SV=2
P42973 1.20e-121 6 479 1 479
Aryl-phospho-beta-D-glucosidase BglA OS=Bacillus subtilis (strain 168) OX=224308 GN=bglA PE=1 SV=1
P26208 3.67e-118 9 476 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
P40740 1.14e-116 9 479 8 469
Aryl-phospho-beta-D-glucosidase BglH OS=Bacillus subtilis (strain 168) OX=224308 GN=bglH PE=1 SV=2

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
1.000044 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001553_02319.