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CAZyme Information: MGYG000004180_03792

You are here: Home > Sequence: MGYG000004180_03792

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides;
CAZyme ID MGYG000004180_03792
CAZy Family GH76
CAZyme Description Cellobiose 2-epimerase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
396 MGYG000004180_78|CGC1 45881.49 4.6541
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004180 4626686 MAG United Kingdom Europe
Gene Location Start: 1948;  End: 3138  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.101

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH76 36 370 1.9e-81 0.8938547486033519

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam03663 Glyco_hydro_76 1.43e-34 86 301 36 255
Glycosyl hydrolase family 76. Family of alpha-1,6-mannanases.
COG4833 COG4833 7.02e-22 142 369 88 324
Predicted alpha-1,6-mannanase, GH76 family [Carbohydrate transport and metabolism].
cd04434 LanC_like 3.05e-08 88 343 1 240
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.
pfam07470 Glyco_hydro_88 8.23e-06 86 249 29 174
Glycosyl Hydrolase Family 88. Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases.
cd04434 LanC_like 7.94e-04 67 235 31 189
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT49827.1 8.36e-278 2 396 3 397
QCQ35470.1 7.43e-184 36 395 30 388
QUU05381.1 2.12e-183 36 395 30 388
AKA50425.1 2.12e-183 36 395 30 388
CBW20937.1 2.12e-183 36 395 30 388

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4MU9_A 5.53e-160 33 392 5 362
Crystalstructure of a putative glycosylhydrolase (BT_3782) from Bacteroides thetaiotaomicron VPI-5482 at 1.89 A resolution [Bacteroides thetaiotaomicron VPI-5482],4MU9_B Crystal structure of a putative glycosylhydrolase (BT_3782) from Bacteroides thetaiotaomicron VPI-5482 at 1.89 A resolution [Bacteroides thetaiotaomicron VPI-5482]
6U4Z_A 1.25e-58 85 390 169 489
CrystalStructure of a family 76 glycoside hydrolase from a bovine Bacteroides thetaiotaomicron strain [Bacteroides thetaiotaomicron]
4C1S_A 3.15e-55 83 392 43 367
Glycosidehydrolase family 76 (mannosidase) Bt3792 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],4C1S_B Glycoside hydrolase family 76 (mannosidase) Bt3792 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482]
4V1S_A 9.41e-40 76 368 73 361
Structureof the GH76 alpha-mannanase BT2949 from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],4V1S_B Structure of the GH76 alpha-mannanase BT2949 from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
4V1R_A 4.85e-37 76 368 73 361
Structureof a selenomethionine derivative of the GH76 alpha- mannanase BT2949 Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],4V1R_B Structure of a selenomethionine derivative of the GH76 alpha- mannanase BT2949 Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits      help

has no Swissprot hit.

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
0.000285 0.119279 0.880239 0.000064 0.000086 0.000062

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004180_03792.