CAZyme Information: MGYG000004636_01420

Basic Information

• Species: Paramuribaculum sp009775605
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Paramuribaculum; Paramuribaculum sp009775605
• CAZyme ID: MGYG000004636_01420
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
385		42307.84	5.0845

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004636	2253564	MAG	Germany	Europe

• Gene Location: Start: 15765; End: 16922 Strand: +

Full Sequence      

MKKTIFRLILAAAVVALGFAQTACTGKSNTDSETKAKVDSVHPRIIIAYVTSGSDVMPDP
NSMTHINYAFGHVNQTFNGIDVANPDRLHQISALKQQNPDLKVILSVGGWGSGRFSEMAA
DSLNRAAFAADAKRVIDEFNLDGIDIDWEYPTSSSAGISSSPDDTQNYTLLMRDLRSAIG
PDKLLTLATPGNARYYDFPAILPYIDFVNIMSYDIGTAARHKHQAPLYASEHTALTADQA
LKAHLEAGIPKEKLTLGLPFYGRGAYEYPDYMDYKDFKLLDSCTIVWDEKAQVPYVANSK
GELVMGYNDPRAIEIKCKYILDNDLLGAMYWEYTCDDAQGTLRKIVTDYMMGQKGLDYQQ
APAEHNVPTDTTAPAPKPAPAIPAN

Enzyme Prediction     

No EC number prediction in MGYG000004636_01420.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	48	341	3e-72	0.9391891891891891

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	1.27e-94	46	336	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	9.58e-77	46	336	2	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	1.26e-75	46	332	2	303	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	1.94e-71	59	341	24	346	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	4.77e-55	31	342	25	428	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SCD19272.1	5.27e-139	43	351	34	342
ADV45176.1	1.05e-130	44	354	34	343
QUT34047.1	1.19e-129	6	354	4	343
QQA31016.1	3.49e-128	1	353	1	344
QBJ17604.1	3.49e-128	1	353	1	344

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	7.09e-57	63	336	27	329	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
6TSB_AAA	2.49e-56	46	338	37	339	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]
6T9M_AAA	4.02e-56	46	338	56	358	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]
4NZC_A	1.37e-51	47	337	9	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	1.43e-51	47	337	6	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	3.71e-43	50	375	111	466	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q9W092	2.91e-34	36	343	33	396	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
P36362	1.16e-33	64	377	53	413	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
Q13231	1.01e-31	59	340	47	367	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
Q95M17	7.31e-31	59	341	47	370	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000003	1.000060	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004636_01420.