CAZyme Information: HCAG_06040-t26_1-p1

Basic Information

• Species: Histoplasma capsulatum
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum
• CAZyme ID: HCAG_06040-t26_1-p1
• CAZy Family: GT15
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
461	CH476661|CGC1	52422.45	6.3208

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=CH476661:1378450-1380861(+)

Full Sequence      

MHLRRLLQAAATATCLAGVAVEAVDVNPLPAPADITWGTSGPIHISERLEFRGPNNYLLR
AAWRRASDAIRTIRWTPAVVEKPIPTFEPFPGSSKAQRDSVWPPQRSLVRMVNVKVKNER
AELQHGVDESYTLDIKERSHSIDITANTIWGAMHAFTTLQQIIIAEGYWRLIVEQPVSIK
DQPLPGPVKINRYPQMTKGAYSPREVYTPEDIRHIVQYARERGIRVVPETDMPGHSAKGW
EQVDPKMIACANSWWSNDVWALHTAVEPNPGQLDIIYDGTYKVVENVYKELSTQFPDNFF
HTGGDEVHPNCFNFSSIIRDWFAEDSKRDFNDLLQIWVDKAYPIFKDRPSRRLIMWEDVL
LGGMHAHTVPKDVIMQSWNLGPENIKKLTSQGYDVIVSSADFLYLDCGFGGWVGNDPRYN
VMFNPDPAHQTSTTLDLGGSWCAPYKTWQRLEIEEGKREVG

Enzyme Prediction     

EC	3.2.1.52:13

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	188	424	4.1e-52	0.6735905044510386

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119332	GH20_HexA_HexB-like	7.56e-89	187	451	46	278	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	2.21e-85	187	448	46	301	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
373334	Glycohydro_20b2	1.74e-41	28	162	1	133	beta-acetyl hexosaminidase like.
119333	GH20_chitobiase-like	8.12e-32	190	406	49	268	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.
119338	GH20_chitobiase-like_1	9.88e-29	188	406	47	248	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS66068.1|GH20	0.0	1	453	1	481
QSS57475.1|GH20	0.0	1	451	1	494
QSS67506.1|GH20	0.0	1	451	1	494
ABB18373.1|GH20|3.2.1.52	1.33e-181	16	461	14	506
QRD87688.1|GH20	1.27e-180	23	451	18	492

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5OAR_B	1.00e-158	109	451	5	391	Crystal structure of native beta-N-acetylhexosaminidase isolated from Aspergillus oryzae [Aspergillus oryzae],5OAR_D Crystal structure of native beta-N-acetylhexosaminidase isolated from Aspergillus oryzae [Aspergillus oryzae]
3NSM_A	3.47e-41	109	451	109	478	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]
3WMB_A	6.55e-41	109	451	109	478	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]
5Y0V_A	7.03e-41	109	451	109	478	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with berberine [Ostrinia furnacalis]
5Y1B_A	7.03e-41	109	451	109	478	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with a berberine derivative (SYSU-00679) [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9DFH0|HEX1_COCPS	2.35e-182	16	461	14	506	Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 SV=1
sp|Q8J2T0|HEXA_ASPOZ	2.25e-181	23	451	18	492	Beta-hexosaminidase OS=Aspergillus oryzae OX=5062 GN=nagA PE=1 SV=1
sp|Q9HGI3|HEXA_EMEND	4.62e-179	21	451	17	495	Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA PE=1 SV=1
sp|D4AYT4|HEX2_ARTBC	5.91e-154	11	451	20	507	Probable beta-hexosaminidase ARB_01353 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01353 PE=1 SV=1
sp|P43077|HEX1_CANAX	6.01e-95	16	451	15	455	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000909	0.999067	CS pos: 23-24. Pr: 0.9491

TMHMM  Annotations     

There is no transmembrane helices in HCAG_06040-t26_1-p1.