CAZyme Information: HCAG_05925-t26_1-p1

Basic Information

• Species: Histoplasma capsulatum
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum
• CAZyme ID: HCAG_05925-t26_1-p1
• CAZy Family: GH92
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
360		40472.01	4.8441

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HcapsulatumNAm1	9402	339724	89	9313

• Gene Location: location=CH476661:964962-966044(+)

Full Sequence      

MNRLHIHATDSQSWPLDIPSMPELAAKGAYHPSLILTSSKLSDIQMYGLERGVSVFLEID
MPGHTGSIGYAFPELVSAFLANEWEKYALQPPSGQIKLNSSDVDKFLDELMADLLPRVSP
FTRYFHTGGDEFNLNTYLLEEAIGSSKEEVLRPLLQAVVTRLHTAIRKAGLTPIVWEELV
ADWDLSLSPSPTEKTEIIVQAWRNSTAVKYLLDRGYRTIFGSGDAWYLDCGQGTYVNPKR
SSTAIKEPFLDWCSPKKNWKHMYMYNPLEGISEDLHHLLEGGETHMWSENVDPVALDMMV
WPRAAAAAEVLWSGPRTANQIQDASYRLSEWRERAVVDLGVGASLAQMTYCLMREGSCEL

Enzyme Prediction     

EC	3.2.1.52:9

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	1	314	9.6e-65	0.8664688427299704

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119332	GH20_HexA_HexB-like	2.85e-123	1	336	32	345	Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
395590	Glyco_hydro_20	5.19e-76	1	314	32	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
119338	GH20_chitobiase-like_1	1.22e-33	1	328	32	311	A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This subgroup lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
119336	GH20_SpHex_like	1.39e-33	1	319	32	321	A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases.
119333	GH20_chitobiase-like	1.41e-33	1	315	32	345	The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS66188.1|GH20	2.62e-269	1	360	243	602
QSS57609.1|GH20	1.51e-268	1	360	243	602
QSS67367.1|GH20	1.51e-268	1	360	243	602
ABU87865.1|GH20	7.81e-195	1	360	244	603
AAL14649.1|GH20	1.14e-183	1	296	244	539

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WMB_A	1.06e-53	1	358	218	570	Crystal structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with naphthalimide derivative Q1 [Ostrinia furnacalis],3WMC_A Crystal structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with naphthalimide derivative Q2 [Ostrinia furnacalis]
5Y1B_A	1.17e-53	1	358	218	570	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with a berberine derivative (SYSU-00679) [Ostrinia furnacalis]
3NSM_A	2.06e-53	1	358	218	570	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 from Ostrinia furnacalis [Ostrinia furnacalis],3NSN_A Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with TMG-chitotriomycin [Ostrinia furnacalis],3OZO_A Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with NGT [Ostrinia furnacalis],3OZP_A Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with PUGNAc [Ostrinia furnacalis]
3S6T_A	1.13e-52	1	358	221	573	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 V327G complexed with PUGNAc [Ostrinia furnacalis]
5Y0V_A	1.66e-52	1	358	218	570	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with berberine [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4AUH6|HEX1_ARTBC	1.86e-186	1	360	244	605	Beta-hexosaminidase ARB_07893 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07893 PE=1 SV=1
sp|Q9SYK0|HEXO2_ARATH	2.74e-66	1	359	202	571	Beta-hexosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=HEXO2 PE=1 SV=1
sp|Q06GJ0|HEXC_OSTFU	1.51e-52	1	358	240	592	Chitooligosaccharidolytic beta-N-acetylglucosaminidase OS=Ostrinia furnacalis OX=93504 PE=1 SV=1
sp|P49010|HEXC_BOMMO	3.03e-50	1	358	242	594	Chitooligosaccharidolytic beta-N-acetylglucosaminidase OS=Bombyx mori OX=7091 PE=1 SV=1
sp|E9DFH0|HEX1_COCPS	2.79e-45	1	360	208	587	Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000065	0.000000

TMHMM  Annotations     

There is no transmembrane helices in HCAG_05925-t26_1-p1.