CAZyme Information: MGYG000003490_00910

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74
• CAZyme ID: MGYG000003490_00910
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
374		39808.08	4.2788

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003490	2488924	MAG	Fiji	Oceania

• Gene Location: Start: 649; End: 1773 Strand: +

Full Sequence      

MVVAGMTLTTGLAAVKGDPVAAEEAVPLPGRDGRVVLYVMDQPDLGLTDDMAPHIDQINY
AFALLEGGEAHGSHWQGIRQLEGYLARHGHIDGVLSVGGWGAEGFSDACATAEGRQRLAD
SILQLMDSHGFTGVDIDWEYPGSSAAGIRSREEDVDNWYALLALLREGLDQRQTERGRDY
LLSVALGAGAEQLAMVDGERLGGLVDQAVVMAYDLQGFDRITGHHAGLYPAGDTPDSGAF
AVNALTDSGLFAGKILLGIPAYGRVWRQVSGDNDGLHQRAATAGNRTLRYDELQQLDSRG
YTRHYDEEAQAAWWLGGGNFVSGEDEASLAAKARWLKENGLLGAAVWAQHQDPEGALLAE
LSAALTPADGAEGD

Enzyme Prediction     

No EC number prediction in MGYG000003490_00910.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	52	353	1.2e-56	0.8412162162162162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	7.34e-74	35	352	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	9.46e-69	47	352	18	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	2.37e-62	58	352	26	307	Glycosyl hydrolases family 18.
COG3325	ChiA	1.07e-55	34	355	39	426	Chitinase, GH18 family [Carbohydrate transport and metabolism].
cd02872	GH18_chitolectin_chitotriosidase	5.38e-55	54	348	22	337	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
AUS97898.1	1.47e-67	35	347	12	329
AJS60325.1	1.18e-60	38	347	10	324
SDS91884.1	3.40e-60	38	365	8	340
ANS77385.1	1.43e-59	34	358	13	342
QLG42679.1	2.26e-59	19	366	18	362

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	6.36e-50	31	347	3	324	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	1.97e-49	81	354	100	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	2.98e-49	81	354	351	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]
6KXN_A	3.45e-41	30	347	4	352	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]
6KST_A	4.82e-41	30	347	4	352	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	8.40e-36	78	365	142	451	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q6RY07	2.18e-27	42	348	35	361	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
P32470	1.99e-25	78	347	109	378	Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
Q92222	2.81e-25	78	355	76	350	Endochitinase B OS=Emericella nidulans OX=162425 GN=chiB PE=1 SV=3
G5EAZ3	2.81e-25	78	355	76	350	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

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.998336	0.001692	0.000006	0.000002	0.000001	0.000002

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003490_00910.