logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001929_01025

You are here: Home > Sequence: MGYG000001929_01025

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 Paramuribaculum sp900752995
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Paramuribaculum; Paramuribaculum sp900752995
CAZyme ID MGYG000001929_01025
CAZy Family GH18
CAZyme Description Chitinase A1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
349 MGYG000001929_9|CGC1 37934.27 5.6161
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001929 2523600 MAG Denmark Europe
Gene Location Start: 8415;  End: 9464  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001929_01025.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 42 333 1.3e-67 0.9222972972972973

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06548 GH18_chitinase 4.27e-95 42 334 1 321
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.
smart00636 Glyco_18 1.15e-82 42 331 2 330
Glyco_18 domain.
pfam00704 Glyco_hydro_18 2.89e-79 42 331 2 303
Glycosyl hydrolases family 18.
cd02872 GH18_chitolectin_chitotriosidase 4.87e-69 42 330 1 336
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 8.81e-58 17 334 18 422
Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT34047.1 3.11e-119 1 337 1 327
ADV45176.1 6.33e-116 32 337 26 327
QDO71383.1 1.10e-113 21 337 16 326
SCD19272.1 9.63e-113 40 349 35 343
QPH57945.1 5.26e-111 14 348 9 342

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4NZC_A 4.90e-47 55 347 30 396
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 5.12e-47 55 347 27 393
Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A 5.46e-47 55 347 30 396
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 5.82e-47 55 347 33 399
Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]
6F8N_A 1.88e-46 55 347 35 401
Keyresidues affecting transglycosylation activity in family 18 chitinases - Insights into donor and acceptor subsites [Serratia proteamaculans 568],6F8N_B Key residues affecting transglycosylation activity in family 18 chitinases - Insights into donor and acceptor subsites [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 3.88e-37 7 331 14 434
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q9W092 4.01e-31 40 330 41 384
Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
P36362 4.86e-30 31 330 14 370
Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
P32470 1.25e-29 60 348 85 391
Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
Q13231 1.01e-28 42 330 24 358
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 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
0.000000 0.000086 0.999963 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001929_01025.