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CAZyme Information: MGYG000001429_00356

You are here: Home > Sequence: MGYG000001429_00356

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 Alistipes_A ihumii
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A ihumii
CAZyme ID MGYG000001429_00356
CAZy Family GH39
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
475 53127.71 4.9864
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001429 2772824 Isolate not provided not provided
Gene Location Start: 264228;  End: 265655  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001429_00356.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH39 105 403 5.8e-38 0.728538283062645

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01229 Glyco_hydro_39 2.86e-18 33 342 3 307
Glycosyl hydrolases family 39.
cd21510 agarase_cat 1.00e-06 181 258 100 187
alpha-beta barrel catalytic domain of agarase, such as GH86-like endo-acting agarases identified in non-marine organisms. Typically, agarases (E.C. 3.2.1.81) are found in ocean-dwelling bacteria since agarose is a principle component of red algae cell wall polysaccharides. Agarose is a linear polymer of alternating D-galactose and 3,6-anhydro-L-galactopyranose. Endo-acting agarases, such as glycoside hydrolase 16 (GH16) and GH86 hydrolyze internal beta-1,4 linkages. GH86-like endo-acting agarase of this protein family has been identified in the human intestinal bacterium Bacteroides uniformis. This acquired metabolic pathway, as demonstrated by the prevalence of agar-specific genetic cluster called polysaccharide utilization loci (PULs), varies considerably between human populations, being much more prevalent in a Japanese sample than in North America, European, or Chinese samples. Agarase activity was also identified in the non-marine bacterium Cellvibrio sp.
cd06542 GH18_EndoS-like 7.02e-05 78 295 19 213
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QGA22857.1 3.27e-255 1 468 87 552
AVM46100.1 1.21e-117 33 440 2 410
AVM46102.1 7.27e-91 41 440 15 409
QEL16017.1 1.49e-75 30 465 24 465
QJD85864.1 7.77e-72 31 462 2 445

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5Z3K_A 1.17e-35 31 398 7 368
Crystalstructure of glucosidase from Croceicoccus marinus at 1.8 Angstrom resolution [Croceicoccus marinus],5Z3K_B Crystal structure of glucosidase from Croceicoccus marinus at 1.8 Angstrom resolution [Croceicoccus marinus]
6UQJ_A 1.02e-10 153 291 134 286
Crystalstructure of the GH39 enzyme from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306]
4EKJ_A 1.26e-09 155 291 131 281
ChainA, Beta-xylosidase [Caulobacter vibrioides]
4M29_A 1.26e-09 155 291 131 281
Structureof a GH39 Beta-xylosidase from Caulobacter crescentus [Caulobacter vibrioides CB15]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P23552 4.37e-12 120 345 105 317
Beta-xylosidase OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=xynB 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
0.000245 0.999108 0.000151 0.000166 0.000149 0.000140

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001429_00356.