CAZyme Information: MGYG000004474_01139

Basic Information

• Species: Sodaliphilus sp004557565
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Sodaliphilus; Sodaliphilus sp004557565
• CAZyme ID: MGYG000004474_01139
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
363	MGYG000004474_23|CGC1	41194.95	6.1594

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004474	2861939	MAG	Israel	Asia

• Gene Location: Start: 24378; End: 25469 Strand: +

Full Sequence      

MIKNFVLSTFVVVLTALCPFGAFASQPQNKICLAYCTYYGDKLPDPNIVTHINYAFAELY
VVDGVYKTFKLQGNESRFRQVMALKKQNPNLKICLAFTHTVSNSDNRQGGGFSKMSASPE
MRKQFAADCLAFCKKWNLDGIDIDWEFPGLSWSGHASDPKTDTKNYTLLMKDLREALGND
YIISFAGYVMDMQSTDSGKKYVDIQAVVPYVDYINIMTYDMDAAPHFQSAIISSTSYYDC
MSAIRSYAKLGVPFEKMLLGIPFYLRHSHDGLTTVVDYKQIVKLKSNPNFEFDLWDEEAR
TPYAKYKGKFYGSYDNPRSIAVKGEWIHSLGLGGLLYWENSEDDADMTLAKACWEAITKN
YDE

Enzyme Prediction     

No EC number prediction in MGYG000004474_01139.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	45	348	2.3e-57	0.8581081081081081

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	4.00e-70	38	343	15	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	6.53e-63	35	343	9	307	Glycosyl hydrolases family 18.
smart00636	Glyco_18	2.23e-58	45	339	22	330	Glyco_18 domain.
cd02872	GH18_chitolectin_chitotriosidase	3.09e-57	45	338	24	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	4.24e-41	38	343	55	423	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGY54522.1	2.08e-138	24	359	40	375
QMI82040.1	3.08e-120	24	359	40	374
QPH57581.1	4.37e-120	24	359	40	374
QQA31286.1	4.37e-120	24	359	40	374
QUT99830.1	4.37e-120	24	359	40	374

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5GZU_A	2.95e-39	74	357	93	391	CrystalStructure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZU_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_A Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
5GZT_B	3.37e-39	74	357	344	642	CrystalStructure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
3QOK_A	1.35e-37	41	357	47	416	ChainA, Putative chitinase II [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]
4NZC_A	4.73e-37	45	344	30	384	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	4.91e-37	45	344	27	381	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	7.16e-29	34	343	55	438	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q9W092	5.30e-25	45	344	66	390	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
Q91XA9	2.29e-24	40	344	39	366	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
P36909	4.27e-24	49	346	270	597	Chitinase C OS=Streptomyces lividans OX=1916 GN=chiC PE=2 SV=1
Q6RY07	3.67e-23	40	344	39	366	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000354	0.998336	0.000766	0.000198	0.000162	0.000152

TMHMM  Annotations     

start	end
5	24