CAZyme Information: KIX05982.1

Basic Information

• Species: Rhinocladiella mackenziei
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Rhinocladiella; Rhinocladiella mackenziei
• CAZyme ID: KIX05982.1
• CAZy Family: GH43
• CAZyme Description: Beta-hexosaminidase [Source:UniProtKB/TrEMBL;Acc:A0A0D2FV73]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
630	KN847477|CGC16	71052.80	6.1184

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RmackenzieiCBS650.93	11418	1442369	36	11382

• Gene Location: location=KN847477:1146042-1147982(-)

Full Sequence      

MLFRIGAMLLCVTTSRAIWPQPADMTSGTNVLWLDPAAKATFRCDGAELALCDDFLGFGN
NRLLNLMNDAFQFFQDLLDWFPFSLGNKCGHDAQSPLTEVSIVRRAVRETIASTHKSRFV
PWKFHKRKSDFEPGASAPRHYLSTLQIVQNGCPETRTFHPATFFAGDESYEITVDNVTAI
IKANCTIGTLRGLQTFQQLFFAHSTFSGSYLPHTPVKIVDRPKWPHRGLSIDIARNPFHP
RDLIRTIDAMFMAKMNRLHVHATDSQSWPLEIPSLPELAKRGAYQPHLVWTASTLEEVQR
YGALKGVSVFVEIDMPGHTASVAHAYPDLIAAFSELDWSTFAAEPLSGQLKLNSSAVFKF
VSDVLQDLLPRTSDYTRLYHLGGDEVNRAAYLLDDTVRSDDPQVLQPLLQKLIDHVTGIV
TQHGLQPIVWEEMLLDWNLTLPSLQNGDQSTSTLVQVWRNSERIEEVLKRGHRAIFGDYH
YWYLDCGYGIFLDPYPTGKSPPGVPFNTSGGSSSKLKPPYLDYCGPFHNWRHMYMYNPLA
NISDDLQHGIEGGEVLMWSEQTDSIDLDTKLWPRAAAAAEVLWSGLREETMLEDASKRLG
EWRERGVTDLGIRMSPVQMTWCLMEGACNL

Enzyme Prediction     

EC	3.2.1.52:9

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	219	585	2.7e-77	0.973293768545994

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119332	GH20_HexA_HexB-like	1.92e-133	224	607	1	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	4.59e-101	225	585	2	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
119333	GH20_chitobiase-like	1.57e-54	225	585	2	344	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.
119336	GH20_SpHex_like	5.84e-46	226	599	3	329	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.
119338	GH20_chitobiase-like_1	1.42e-41	224	599	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABU87865.1|GH20	1.55e-196	17	630	19	603
QSS57609.1|GH20	8.53e-196	1	630	1	602
QSS67367.1|GH20	1.21e-195	1	630	1	602
QSS66188.1|GH20	6.88e-195	1	630	1	602
CBX95932.1|GH20	8.84e-164	15	630	15	613

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WMB_A	3.23e-66	99	628	66	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	3.66e-66	99	628	66	570	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with a berberine derivative (SYSU-00679) [Ostrinia furnacalis]
3NSM_A	1.68e-65	99	628	66	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	1.79e-65	99	628	69	573	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 V327G complexed with PUGNAc [Ostrinia furnacalis]
5Y0V_A	5.10e-65	99	628	66	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	3.00e-189	16	630	17	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	2.10e-77	167	629	115	571	Beta-hexosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=HEXO2 PE=1 SV=1
sp|Q06GJ0|HEXC_OSTFU	1.36e-64	99	628	88	592	Chitooligosaccharidolytic beta-N-acetylglucosaminidase OS=Ostrinia furnacalis OX=93504 PE=1 SV=1
sp|P43077|HEX1_CANAX	9.58e-61	167	630	111	555	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
sp|P49010|HEXC_BOMMO	1.87e-60	129	628	116	594	Chitooligosaccharidolytic beta-N-acetylglucosaminidase OS=Bombyx mori OX=7091 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000368	0.999610	CS pos: 17-18. Pr: 0.9684

TMHMM  Annotations     

There is no transmembrane helices in KIX05982.1.