logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003237_01022

You are here: Home > Sequence: MGYG000003237_01022

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 Victivallis sp002998355
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp002998355
CAZyme ID MGYG000003237_01022
CAZy Family GH5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
503 MGYG000003237_30|CGC2 57204.22 6.8359
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003237 4618450 MAG United States North America
Gene Location Start: 75527;  End: 77038  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003237_01022.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 207 477 1.3e-48 0.7709090909090909

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00150 Cellulase 1.12e-28 198 463 13 271
Cellulase (glycosyl hydrolase family 5).
COG2730 BglC 6.42e-16 207 478 72 377
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd11337 AmyAc_CMD_like 0.003 248 296 64 134
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is mainly bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AVM44326.1 0.0 1 503 17 519
AVM44708.1 4.68e-129 24 500 27 497
QNN21528.1 1.31e-108 69 501 75 517
AVM45838.1 1.21e-98 48 503 65 531
AVM46198.1 2.14e-97 91 501 78 500

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3NCO_A 9.59e-28 225 465 62 295
Crystalstructure of FnCel5A from F. nodosum Rt17-B1 [Fervidobacterium nodosum Rt17-B1],3NCO_B Crystal structure of FnCel5A from F. nodosum Rt17-B1 [Fervidobacterium nodosum Rt17-B1]
3RJX_A 1.80e-27 225 465 62 295
CrystalStructure of Hyperthermophilic Endo-Beta-1,4-glucanase [Fervidobacterium nodosum Rt17-B1]
3RJY_A 1.80e-27 225 465 62 295
CrystalStructure of Hyperthermophilic Endo-beta-1,4-glucanase in complex with substrate [Fervidobacterium nodosum Rt17-B1]
3AMC_A 3.86e-26 225 494 54 307
Crystalstructures of Thermotoga maritima Cel5A, apo form and dimer/au [Thermotoga maritima MSB8],3AMC_B Crystal structures of Thermotoga maritima Cel5A, apo form and dimer/au [Thermotoga maritima MSB8],3AMD_A Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_B Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_C Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_D Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3MMU_A Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_B Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_C Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_D Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_E Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_F Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_G Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_H Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_A Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_B Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_C Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_D Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima]
3AMG_A 2.50e-25 225 494 54 307
Crystalstructures of Thermotoga maritima Cel5A in complex with Cellobiose substrate, mutant form [Thermotoga maritima MSB8],3AMG_B Crystal structures of Thermotoga maritima Cel5A in complex with Cellobiose substrate, mutant form [Thermotoga maritima MSB8]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A3DJ77 8.99e-20 203 462 19 315
Endoglucanase C OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celC PE=3 SV=1
P0C2S3 8.99e-20 203 462 19 315
Endoglucanase C OS=Acetivibrio thermocellus OX=1515 GN=celC PE=1 SV=1
P23340 8.99e-20 203 462 19 315
Endoglucanase C307 OS=Clostridium sp. (strain F1) OX=1508 GN=celC307 PE=1 SV=1
P16169 3.78e-15 207 468 29 296
Cellodextrinase A OS=Ruminococcus flavefaciens OX=1265 GN=celA PE=3 SV=3
P25472 1.39e-11 225 387 77 228
Endoglucanase D OS=Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) OX=394503 GN=celCCD PE=3 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
0.010750 0.988258 0.000242 0.000270 0.000224 0.000227

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003237_01022.