CAZyme Information: MGYG000000287_01353

Basic Information

• Species: Robinsoniella sp900539655
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella sp900539655
• CAZyme ID: MGYG000000287_01353
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
347	MGYG000000287_12|CGC2	39211.36	5.282

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000287	7249439	MAG	Sweden	Europe

• Gene Location: Start: 60124; End: 61167 Strand: -

Full Sequence      

MIFTKQKLDKQVIGYIYTNHLPGLTSEDAKMLSILNLSFGKIETGNIICDLDDYQECLLK
IRRESPDLKLVLSVGGWGAGGFSETMTTDAGRKQFAWSARNLVERYHLDGIDIDWEYPCI
GISGIKASGEDKENFTLMLKDLRSSLDQIEDRHCLVNIAGGGGNYFLRCTDMYNASRYLD
YVQIMTYDLRGGFTIATGHHTNLYDNQKDLLDVSTDRAVKAYLKAGVPREKLVIGAAFYS
RMWKGVPDANHGWMQMAESAGGYGPDYGELAESYINKNGFKRYWDDEAKAPWLFNGDTFI
SYEDGESIRHKAKYVKELGLAGMMFWEYGCDSTKTLTRIIRESFSGD

Enzyme Prediction     

No EC number prediction in MGYG000000287_01353.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	10	337	8.2e-73	0.956081081081081

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	6.65e-102	12	331	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.
smart00636	Glyco_18	2.12e-81	28	331	22	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	2.06e-79	11	331	1	307	Glycosyl hydrolases family 18.
COG3325	ChiA	9.23e-78	58	342	117	434	Chitinase, GH18 family [Carbohydrate transport and metabolism].
cd02872	GH18_chitolectin_chitotriosidase	2.42e-60	35	326	31	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCJ95062.1	2.63e-136	11	342	3	334
QOV20718.1	5.18e-133	10	342	2	334
QUH29766.1	4.34e-132	12	340	6	334
ALS30085.1	5.03e-130	14	336	10	335
BCJ97222.1	2.05e-128	11	341	3	333

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	4.60e-127	12	336	7	334	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	7.11e-77	28	332	46	378	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	7.74e-76	28	332	297	629	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]
6BT9_A	7.42e-64	50	346	135	473	ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
1ITX_A	4.05e-61	58	336	113	411	ChainA, Glycosyl Hydrolase [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	4.62e-58	58	336	145	443	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
A6N6J0	1.12e-40	58	331	113	390	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
P48827	5.25e-39	58	331	112	383	Endochitinase 42 OS=Trichoderma harzianum OX=5544 GN=chit42 PE=1 SV=1
P11797	4.63e-38	10	332	5	409	Chitinase B OS=Serratia marcescens OX=615 GN=chiB PE=1 SV=1
E9QRF2	4.25e-33	58	333	118	391	Endochitinase B1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiB1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000067	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000287_01353.