CAZyme Information: KFA48029.1

Basic Information

• Species: Stachybotrys chartarum
• Lineage: Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
• CAZyme ID: KFA48029.1
• CAZy Family: AA9
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
754		82976.72	4.3695

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SchartarumIBT40293	11453	1280524	0	11453

• Gene Location: location=KL651577:195375-197639(-)

Full Sequence      

MRFCISTVALLRLPILVRSLQLLPPVLQATGGEDGSWQLASSPRVIYIEEGIASEADTDG
LTLIPPSGSAFASLFRENIGTVTGDEWSLEIVQSLPRNASGILLGSFTGDDISTVTYENG
IATSEGYEIVVSSSSVFIGGTGARGMWWGTRTLLQQLMISGDSSLAAGRYVDAPAYATRG
FMLDAGRKWYAPGFLKELCSFASFFKMSEFHYHLSDNYPLNRGRNESWQDVYSHFSLLPE
DESLLGIIHDRENETLSRADYADLQSHCAAYGVAVIPEIEAPAHSLYLTKWMPELSLGRR
DLLNLSHPDTIPTVQRIWAEFLPWFDVKEVHIGADEYDRTLADDYINFVNEMSRFVNDTA
GKRVRIWGTPTDEPVENITIANDVVVQHWQYGQSDPLQLVEHSYDIINSQDWWAYMSMKN
DHMPILPARYPQFFNESRVLEFANQDGWQWSPADFNHVNTTLQVADEDVHNKGAIMAAWN
DNGPDASTQLEAYYAMRRGIALVGARAWSGSRGPELVEGDVASSIDFYSPLAPGQNLDRV
LPAPENISGPLLSWSRNGNSSEGMQLGQGSKGLNYTLSLVVNGPFTLSGPDDTLTLNDDG
SLVFEADGYEYPLRHVSEQAGLELDPGHPGRIWVNVTSSTHEVVTVPVGSPSNITIATDA
EHGSVAWIDGSFAGRFEVFVFGGRNTQFSWSQMAFVAPLSQARGGLHELTVYDEFIIQRN
GQPETVPGNGAAESLLPSRRVMAAVVSIVVALLV

Enzyme Prediction     

No EC number prediction in KFA48029.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	172	510	4.7e-53	0.9703264094955489

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119334	GH20_DspB_LnbB-like	7.65e-95	178	510	2	326	Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. 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.
119331	GH20_hexosaminidase	6.29e-34	179	509	2	303	Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) 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. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself.
395590	Glyco_hydro_20	6.93e-28	176	510	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
226056	Chb	5.49e-20	111	418	192	537	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
119333	GH20_chitobiase-like	2.47e-17	176	442	1	293	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
UQC90187.1|GH20	0.0	15	711	477	1173
EAA64130.1|GH20	0.0	9	699	9	708
CEI70263.1|GH20	0.0	10	732	12	733
QPC80002.1|GH20	0.0	10	737	12	742
QKD58866.1|GH20	0.0	10	709	11	703

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	7.48e-33	111	416	146	469	Crystallization analysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
3GH4_A	3.99e-17	68	454	80	449	Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 [Paenibacillus sp.],3GH5_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GlcNAc [Paenibacillus sp.],3GH7_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GalNAc [Paenibacillus sp.],3SUR_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NAG-thiazoline. [Paenibacillus sp. TS12],3SUS_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-NAG-thiazoline [Paenibacillus sp. TS12],3SUT_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc [Paenibacillus sp. TS12],3SUU_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-PUGNAc [Paenibacillus sp. TS12],3SUV_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-DNJ [Paenibacillus sp. TS12],3SUW_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-CAS [Paenibacillus sp. TS12]
6Z14_JJJ	8.92e-13	106	315	236	469	Chain JJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]
6YXZ_JJJ	8.92e-13	106	315	236	469	Chain JJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]
7DUP_A	3.93e-12	97	336	50	316	Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B2UPR7|H2136_AKKM8	1.85e-34	111	416	168	491	Beta-hexosaminidase Amuc_2136 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2136 PE=1 SV=1
sp|Q7WUL4|HEX20_CELFI	5.12e-14	122	421	79	379	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
sp|Q9HGI3|HEXA_EMEND	4.73e-13	152	416	157	449	Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA PE=1 SV=1
sp|P96155|HEX1_VIBFU	1.10e-12	152	428	235	540	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
sp|D4AYT4|HEX2_ARTBC	5.84e-12	148	515	161	564	Probable beta-hexosaminidase ARB_01353 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01353 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.930741	0.069274

TMHMM  Annotations     

There is no transmembrane helices in KFA48029.1.