CAZyme Information: AO090003000988-T-p1

Basic Information

• Species: Aspergillus oryzae
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus oryzae
• CAZyme ID: AO090003000988-T-p1
• CAZy Family: AA5
• CAZyme Description: Has domain(s) with predicted catalytic activity, hydrolase activity, hydrolyzing O-glycosyl compounds activity and role in carbohydrate metabolic process

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
205	Chr2_A_oryzae_RIB40|CGC24	22559.91	8.3485

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AoryzaeRIB40	12364	510516	274	12090

• Gene Location: location=Chr2_A_oryzae_RIB40:4778854-4779549(+)

Full Sequence      

MAYDIHGLWDAHGKEVGPHALAHTNLTEINMGLELFWRNNINPARVVMGLGFYGRSFTMA
DPNCMEPGCLFKEGEAPSGECTNVPGVISATEIHGIIKKGATVTFYKDAAVKVATWNTNQ
WVSWDDVETLKLKIDFANKRCLGGTMVWAVDLDDGTLVEALGNASGKKKQWTSDGIFKPM
PCFGKNWPKGSNKTWIGKKEKPKKG

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	1	155	7.5e-25	0.4391891891891892

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119351	GH18_chitolectin_chitotriosidase	3.50e-31	1	154	186	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.
119357	GH18_zymocin_alpha	3.49e-30	1	153	183	345	Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
214753	Glyco_18	4.14e-27	1	153	182	334	Glyco_18 domain.
395573	Glyco_hydro_18	2.80e-22	1	153	173	307	Glycosyl hydrolases family 18.
225862	ChiA	2.33e-12	1	161	249	432	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAE58097.1|GH18	3.36e-159	1	205	1	205
QMW28376.1|GH18	1.78e-153	1	205	204	408
QMW40447.1|GH18	5.08e-153	1	205	204	408
UDD56387.1|GH18	6.68e-153	1	205	212	416
QRD82868.1|CBM18|GH18	1.04e-151	1	205	326	530

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Y29_A	9.42e-20	1	154	196	352	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 [Ostrinia furnacalis],5Y2B_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with HEPTA-N-ACETYLCHITOOCTAOSE (NAG)7 [Ostrinia furnacalis]
6JAV_A	1.03e-19	1	154	196	352	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a piperidine-thienopyridine derivative [Ostrinia furnacalis],6JAW_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a napthalimide derivative [Ostrinia furnacalis],6JAX_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with chitooctaose [(GlcN)8] [Ostrinia furnacalis],6JAY_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a dipyrido-pyrimidine derivative [Ostrinia furnacalis]
6JM7_A	1.33e-18	1	154	191	351	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
6JM8_A	1.33e-18	1	154	191	351	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
1LG1_A	7.43e-18	1	154	189	343	Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q13231|CHIT1_HUMAN	5.81e-17	1	154	210	364	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q91XA9|CHIA_MOUSE	5.89e-17	1	156	210	368	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q9W5U2|CHI10_DROME	1.50e-16	1	154	2098	2254	Probable chitinase 10 OS=Drosophila melanogaster OX=7227 GN=Cht10 PE=2 SV=2
sp|Q6RY07|CHIA_RAT	2.02e-16	1	156	210	368	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q95M17|CHIA_BOVIN	6.91e-16	1	156	210	368	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000060	0.000009

TMHMM  Annotations     

There is no transmembrane helices in AO090003000988-T-p1.