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CAZyme Information: MGYG000000915_02384

You are here: Home > Sequence: MGYG000000915_02384

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 Clostridium nigeriense
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium nigeriense
CAZyme ID MGYG000000915_02384
CAZy Family GH18
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
962 105335.91 4.9816
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000915 3503945 MAG China Asia
Gene Location Start: 17913;  End: 20801  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 49 459 1.1e-72 0.972972972972973

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06548 GH18_chitinase 3.77e-109 51 448 1 322
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.
COG3325 ChiA 1.05e-99 46 449 35 424
Chitinase, GH18 family [Carbohydrate transport and metabolism].
smart00636 Glyco_18 5.55e-98 50 448 1 334
Glyco_18 domain.
pfam00704 Glyco_hydro_18 6.58e-77 50 448 1 307
Glycosyl hydrolases family 18.
cd02872 GH18_chitolectin_chitotriosidase 2.12e-60 51 443 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AIY83497.1 0.0 1 740 1 737
BAA34922.1 0.0 1 962 1 832
QSW19024.1 0.0 1 740 1 731
AUM98212.1 5.06e-315 1 603 1 607
CBZ02608.1 5.06e-315 1 603 1 607

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4TXG_A 2.39e-110 49 582 154 755
CrystalStructure of a Family GH18 Chitinase from Chromobacterium violaceum [Chromobacterium violaceum ATCC 12472]
1ITX_A 5.83e-54 48 448 11 406
ChainA, Glycosyl Hydrolase [Niallia circulans]
6BT9_A 1.20e-52 48 538 36 508
ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
6KST_A 2.39e-49 48 448 6 357
Crystalstructure of the catalytic domain of chitinase ChiL from Chitiniphilus shinanonensis (CsChiL) [Chitiniphilus shinanonensis],6KST_B Crystal structure of the catalytic domain of chitinase ChiL from Chitiniphilus shinanonensis (CsChiL) [Chitiniphilus shinanonensis],6KXL_A Crystal structure of the catalytic domain of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXL_B Crystal structure of the catalytic domain of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]
6KXM_A 1.12e-48 48 448 6 357
Crystalstructure of D157N mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXM_B Crystal structure of D157N mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P96156 6.04e-94 46 599 317 955
Chitodextrinase OS=Vibrio furnissii OX=29494 GN=endo I PE=1 SV=1
P20533 5.72e-51 48 448 43 438
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q873X9 1.04e-37 33 448 27 389
Endochitinase B1 OS=Neosartorya fumigata OX=746128 GN=chiB1 PE=1 SV=1
E9QRF2 1.04e-37 33 448 27 389
Endochitinase B1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiB1 PE=3 SV=1
G5EAZ3 1.20e-35 50 450 5 349
Endochitinase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=chiB PE=1 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
0.000463 0.995452 0.003497 0.000219 0.000185 0.000167

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000915_02384.