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CAZyme Information: MGYG000002007_02032

You are here: Home > Sequence: MGYG000002007_02032

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 dispar
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes dispar
CAZyme ID MGYG000002007_02032
CAZy Family GH18
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
344 MGYG000002007_11|CGC1 38534.03 5.1758
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002007 2708946 MAG Spain Europe
Gene Location Start: 15868;  End: 16902  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002007_02032.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 53 330 1.1e-57 0.847972972972973

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06548 GH18_chitinase 8.69e-65 81 329 72 322
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.
pfam00704 Glyco_hydro_18 1.77e-61 42 329 9 307
Glycosyl hydrolases family 18.
smart00636 Glyco_18 5.40e-55 52 329 22 334
Glyco_18 domain.
cd02872 GH18_chitolectin_chitotriosidase 8.86e-44 82 328 59 342
This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
COG3325 ChiA 2.36e-40 87 329 120 423
Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBL06865.1 2.05e-256 1 344 1 344
BBB35952.1 2.20e-76 6 337 10 342
QIH36004.1 1.97e-74 6 337 10 342
QIK61506.1 1.56e-73 40 344 43 348
QJR62159.1 2.02e-73 8 337 5 338

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6INX_A 3.98e-38 71 327 40 329
Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
4NZC_A 1.57e-37 66 330 59 386
Crystalstructure of Chitinase D from Serratia proteamaculans at 1.45 Angstrom resolution [Serratia proteamaculans 568],4Q22_A Crystal structure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine at 1.93 Angstrom resolution [Serratia proteamaculans 568]
6HM1_A 1.63e-37 66 330 56 383
Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A 1.72e-37 66 330 59 386
CrystalStructure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine, a hydrolyzed product of hexasaccharide at 1.7 Angstrom resolution [Serratia proteamaculans 568]
4LGX_A 1.81e-37 66 330 62 389
Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P20533 2.27e-25 69 329 133 438
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q5AM60 2.57e-24 45 327 60 355
Chitinase 4 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CHT4 PE=3 SV=1
E9QRF2 2.68e-23 81 343 115 406
Endochitinase B1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiB1 PE=3 SV=1
Q873X9 2.68e-23 81 343 115 406
Endochitinase B1 OS=Neosartorya fumigata OX=746128 GN=chiB1 PE=1 SV=1
E9ERT9 4.63e-23 66 343 95 401
Endochitinase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=chit1 PE=3 SV=1

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
0.000690 0.080565 0.918466 0.000088 0.000106 0.000086

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002007_02032.