CAZyme Information: MGYG000002817_02971

Basic Information

• Species: Paenibacillus_B sp900539405
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B sp900539405
• CAZyme ID: MGYG000002817_02971
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
378	MGYG000002817_15|CGC1	43659.56	7.4437

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002817	6425839	MAG	United States	North America

• Gene Location: Start: 34247; End: 35383 Strand: +

Full Sequence      

MKVNLWTKCFIVVLLAGMGLYFYQISNAGDRKVTAVYVEAWKDYKNIKLSEKNVDIAFIA
FAKIDGTNIYFHEDGATNDQIKENIKKLKQHNPKTKMVLAVGGYGADGFSDASLDGNRYL
FTESIINMVKELELDGVDIDWEYPAFHAWNTQKARPEDTQNFTSLMKELREKLYRLPHPK
NKKYLLTFASGTQDWYFQNVEVKQVEKYVDYINVMTYDFTGRWADTTGYNSNLYPDREKK
AKHSIDQVITMYLDHEIDSKKLLLGVPAYSYGWKDVKSKTDGAFTPGKPIDIDKTDLSYK
TIEKSYLNKNGYKRYYDDQAKTAYLYNGSTFISYEDKEALAEKVKYIKAKELGGAMVWEY
SQDAEDGIVKFLGEKLNK

Enzyme Prediction     

No EC number prediction in MGYG000002817_02971.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	32	366	2e-72	0.9459459459459459

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	7.20e-92	35	363	2	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	6.61e-80	33	363	1	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	3.15e-76	33	363	1	307	Glycosyl hydrolases family 18.
COG3325	ChiA	2.27e-66	31	363	38	423	Chitinase, GH18 family [Carbohydrate transport and metabolism].
cd02872	GH18_chitolectin_chitotriosidase	2.51e-59	60	358	34	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
QDM45870.1	1.74e-272	1	378	1	378
SMF83918.1	4.78e-238	1	378	1	378
AWP30429.1	7.96e-232	1	378	1	380
AVV55897.1	9.27e-231	1	378	1	380
ANA80078.1	9.27e-231	1	378	1	380

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5GZU_A	5.01e-71	37	365	31	379	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	3.58e-70	37	365	282	630	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]
6INX_A	2.66e-62	83	376	48	342	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
1ITX_A	4.75e-62	85	363	113	406	ChainA, Glycosyl Hydrolase [Niallia circulans]
6KXN_A	5.53e-62	26	376	2	370	Crystalstructure of W50A mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXN_B Crystal structure of W50A mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	6.04e-59	85	363	145	438	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q13231	2.20e-37	29	363	19	363	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
Q9D7Q1	1.50e-36	15	377	5	384	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
C5P230	4.10e-34	22	377	71	396	Endochitinase 1 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS1 PE=3 SV=1
Q9BZP6	5.93e-34	88	363	83	365	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 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
0.968134	0.024168	0.006208	0.000075	0.000051	0.001378

TMHMM  Annotations     

start	end
5	27