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CAZyme Information: MGYG000004828_01029

You are here: Home > Sequence: MGYG000004828_01029

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 Fusobacterium_A sp900764925
Lineage Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae; Fusobacterium_A; Fusobacterium_A sp900764925
CAZyme ID MGYG000004828_01029
CAZy Family GH1
CAZyme Description Aryl-phospho-beta-D-glucosidase BglC
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
478 MGYG000004828_11|CGC1 55056.38 5.5173
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004828 2602027 MAG China Asia
Gene Location Start: 48442;  End: 49878  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 2 473 2e-162 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 1 477 1 460
Beta-glucosidase/6-phospho-beta-glucosidase/beta-galactosidase [Carbohydrate transport and metabolism].
pfam00232 Glyco_hydro_1 0.0 4 474 5 453
Glycosyl hydrolase family 1.
TIGR03356 BGL 3.91e-156 5 465 1 426
beta-galactosidase.
PRK13511 PRK13511 4.40e-140 1 471 2 465
6-phospho-beta-galactosidase; Provisional
PRK09589 celA 7.19e-132 1 476 1 476
6-phospho-beta-glucosidase; Reviewed

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL37915.1 1.62e-302 3 478 8 484
AQP40250.1 6.58e-302 3 478 8 484
QWY73207.1 2.69e-292 3 478 10 486
APB31969.1 8.82e-285 2 476 4 478
QMW91715.1 3.65e-279 2 476 4 479

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7M1R_A 1.27e-210 4 476 11 480
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 2.20e-205 4 476 16 485
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 6.29e-205 4 476 16 485
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]
5YHS_A 4.01e-151 3 476 2 469
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 3.24e-150 3 476 2 469
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 4.66e-212 3 476 8 477
Aryl-phospho-beta-D-glucosidase BglC OS=Bacillus subtilis (strain 168) OX=224308 GN=bglC PE=1 SV=1
P40740 2.48e-115 3 476 7 469
Aryl-phospho-beta-D-glucosidase BglH OS=Bacillus subtilis (strain 168) OX=224308 GN=bglH PE=1 SV=2
P42973 1.36e-111 1 476 1 479
Aryl-phospho-beta-D-glucosidase BglA OS=Bacillus subtilis (strain 168) OX=224308 GN=bglA PE=1 SV=1
Q46130 9.00e-111 3 478 6 473
6-phospho-beta-glucosidase OS=Clostridium longisporum OX=1523 GN=abgA PE=3 SV=1
P26208 1.18e-107 4 473 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
1.000062 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004828_01029.