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CAZyme Information: MGYG000000424_00798

You are here: Home > Sequence: MGYG000000424_00798

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-353 sp900768995
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; CAG-353; CAG-353 sp900768995
CAZyme ID MGYG000000424_00798
CAZy Family GH5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
681 74567.53 4.3698
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000424 2854163 MAG Sweden Europe
Gene Location Start: 55339;  End: 57384  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.4 3.2.1.91 3.2.1.73

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 297 635 8.8e-120 0.9967741935483871

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00150 Cellulase 3.07e-47 296 630 1 272
Cellulase (glycosyl hydrolase family 5).
COG2730 BglC 5.40e-36 305 643 47 378
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
smart00637 CBD_II 8.50e-09 158 237 2 77
CBD_II domain.
pfam00553 CBM_2 6.66e-06 150 239 1 86
Cellulose binding domain. Two tryptophan residues are involved in cellulose binding. Cellulose binding domain found in bacteria.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CUH91791.1 1.74e-254 144 679 33 575
AGS52139.1 1.20e-237 155 679 126 659
ADD61853.1 3.36e-236 276 681 97 503
QWT53501.1 2.73e-235 276 681 97 503
QNL98527.1 7.78e-235 276 681 97 503

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1ECE_A 1.52e-66 287 648 5 343
AcidothermusCellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose [Acidothermus cellulolyticus],1ECE_B Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose [Acidothermus cellulolyticus]
1VRX_A 1.12e-65 287 648 5 343
ChainA, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus],1VRX_B Chain B, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus]
4TUF_A 4.63e-55 294 657 8 344
Catalyticdomain of the major endoglucanase from Xanthomonas campestris pv. campestris [Xanthomonas campestris pv. campestris str. ATCC 33913],4TUF_B Catalytic domain of the major endoglucanase from Xanthomonas campestris pv. campestris [Xanthomonas campestris pv. campestris str. ATCC 33913],4TUF_C Catalytic domain of the major endoglucanase from Xanthomonas campestris pv. campestris [Xanthomonas campestris pv. campestris str. ATCC 33913],4TUF_D Catalytic domain of the major endoglucanase from Xanthomonas campestris pv. campestris [Xanthomonas campestris pv. campestris str. ATCC 33913]
3VVG_A 3.85e-54 305 656 30 376
TheCrystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_B The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_C The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3W6L_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
3W6M_A 5.33e-54 305 656 30 376
Contributionof disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P10474 1.07e-180 279 679 621 1021
Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
Q05332 2.88e-151 285 681 42 470
Endoglucanase G OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celG PE=3 SV=1
P50400 3.17e-147 276 680 34 438
Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
P04956 7.99e-135 281 679 35 467
Endoglucanase B OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celB PE=3 SV=1
P23548 5.56e-78 281 656 32 382
Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000005 1.000029 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000424_00798.