CAZyme Information: MGYG000001514_05045

Basic Information

• Species: Paenibacillus_A ihumii
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii
• CAZyme ID: MGYG000001514_05045
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
428	MGYG000001514_12|CGC66	48547.03	5.0442

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001514	5923787	Isolate	not provided	not provided

• Gene Location: Start: 3871938; End: 3873224 Strand: -

Full Sequence      

MKKRWLQTLFIFMLAVSLPVVSVNGVQAKEVTKPKEYRNVGYVFQRGSDISKIDVTQITH
LNYSFGLIYNEEYKDVKNSETGELFGPELNPDVATPQYFRPEQLHTIYLPPKVASDLSRL
DELKAKNPDLKVLLSIGGYDARGFSDAAATEEARKTFAKSTKEVIAQYDLDGIDLDWEYP
VNGGWGSIKARKEDKHNFTLLLQEVRKAIGHDKLLTIAGSANTLFTGTEAGGEDGTWTEF
DKIIPILDFINIMTYDFQYDSNYFGSALYPSKKWPAKNANEGYWVDKAVQNYLKNGCPPE
KINLGLAFAAPIPQIVRSDEHYPIIKERLQQAGFYDSQDPGLKRVKDLLENKNGFTKEWD
EDAKVMYIATVFDNKKQFVMSYIEPKGLTEKLNYVKDLGLGGTMFWEFGSDYDNSMVTQI
AEELSINK

Enzyme Prediction     

EC	3.2.1.14

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	37	417	9.8e-65	0.956081081081081

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	1.04e-86	39	411	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	9.17e-71	38	411	1	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	9.20e-64	38	411	1	307	Glycosyl hydrolases family 18.
COG3325	ChiA	7.95e-60	1	427	1	439	Chitinase, GH18 family [Carbohydrate transport and metabolism].
cd02872	GH18_chitolectin_chitotriosidase	5.29e-54	49	406	19	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
QPF06903.1	3.54e-102	14	426	6	385
AJF72770.1	4.08e-100	14	426	6	415
QEU16233.1	4.08e-100	47	426	40	415
VDZ83594.1	4.08e-100	14	426	6	415
AWS78508.1	8.15e-100	47	426	40	415

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6HM1_A	1.12e-99	47	427	20	396	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A	1.23e-99	47	427	23	399	CrystalStructure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine, a hydrolyzed product of hexasaccharide at 1.7 Angstrom resolution [Serratia proteamaculans 568]
4LGX_A	1.35e-99	47	427	26	402	Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]
6F8N_A	4.87e-99	47	427	28	404	Keyresidues affecting transglycosylation activity in family 18 chitinases - Insights into donor and acceptor subsites [Serratia proteamaculans 568],6F8N_B Key residues affecting transglycosylation activity in family 18 chitinases - Insights into donor and acceptor subsites [Serratia proteamaculans 568]
4NZC_A	8.39e-99	47	426	23	398	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	1.47e-46	37	424	44	451	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
P32470	1.70e-31	15	407	20	379	Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
P48827	5.13e-29	43	411	49	383	Endochitinase 42 OS=Trichoderma harzianum OX=5544 GN=chit42 PE=1 SV=1
E9ERT9	7.13e-29	22	411	30	384	Endochitinase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=chit1 PE=3 SV=1
A6N6J0	3.71e-28	43	411	50	390	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 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
0.000766	0.998245	0.000273	0.000257	0.000227	0.000204

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001514_05045.