CAZyme Information: MGYG000001091_01186

Basic Information

• Species: Citrobacter_A sp009363175
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter_A; Citrobacter_A sp009363175
• CAZyme ID: MGYG000001091_01186
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
287		32254.69	4.8605

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001091	4193018	MAG	Sweden	Europe

• Gene Location: Start: 1628; End: 2491 Strand: -

Full Sequence      

MFIQSAMEIVQKYGLDGIDLDWEYPVNGAWGLVASQPADRENFTLLLKELRQAVGNQKLV
TIAVGANAESPKSWVDVKAIAPLLDYINLMTYDMAYGTQYFNANLYDSKDWPTVATADKY
SVDFVVNNYLAAGLKPQQMNLGIGFYGRVPKRTVEPGIDWTKPDAQKNPVTLPYFGEPEI
TLFKSLGVDLTKDTYVKYNDIVKTFLNDPQKRFTEHWDAQAMVPWLSVQSADGKPLFALS
YENPRSVAIKAEYIKKRGLAGAMFWEYGADDNNQLAKQLAESLGIQH

Enzyme Prediction     

EC	3.2.1.14

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	2	277	4.4e-56	0.6925675675675675

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	8.31e-70	2	270	113	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	5.91e-59	2	270	95	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	2.94e-53	2	270	92	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	1.96e-51	2	271	100	342	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	9.60e-44	2	284	155	437	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFS72142.1	1.10e-210	1	287	131	417
AKE58689.1	2.35e-205	1	287	131	417
AMG94376.1	3.19e-203	1	287	131	417
AUO64755.1	7.47e-202	1	287	131	417
SAZ89220.1	2.04e-199	1	287	131	417

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QOK_A	1.37e-178	1	287	134	420	ChainA, Putative chitinase II [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]
4NZC_A	9.65e-162	1	285	114	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]
6HM1_A	1.03e-161	1	285	111	395	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A	1.15e-161	1	285	114	398	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	1.27e-161	1	285	117	401	Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	5.60e-33	1	283	182	451	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q9W092	3.80e-28	2	271	147	390	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
Q91XA9	4.07e-23	2	271	119	366	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
Q6RY07	4.90e-22	2	271	119	366	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
Q11174	3.32e-21	1	273	157	402	Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 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
1.000052	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001091_01186.