CAZyme Information: MGYG000004799_01051

Basic Information

• Species: Schaedlerella sp900765975
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Schaedlerella; Schaedlerella sp900765975
• CAZyme ID: MGYG000004799_01051
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1596	MGYG000004799_32|CGC1	177101.83	4.6143

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004799	2888994	MAG	China	Asia

• Gene Location: Start: 1710; End: 6500 Strand: -

Full Sequence      

MHKVKKSFKRLLAVSLCASCIMSNGIVSFAEESSTKVTNLALGCQATANAEYNQSGNDMS
AAKAVDGNDESRWSSEGAAPGWLQVDLGAQKTFSQFRILSEGGTGATAGKQLIGKFKIEG
SNDKSKWNLIHQSEDKRAEGFAQDTIVTLDKPVTYQYVKLTVESLKTGAYDSVSIREFEI
RDKVAITPEKPQNPEENVAQGKNAAADSTEDGNLTAAKAFDGNTKDRSSRWSSAVQNAPH
WIYVDLGKEMDVKTVRIFWETRKATDYKIQIANTTEVPQESEWQDVKHIQTNPKALKDTI
TLDEVKKARFVRLYINAFTSQDPDNESASWNSISIYEMEVYGGAPKVDIEEGISVDTPEK
GAKKLTVHIPEETATEKVTYNGTDYEQVVDEKLNIYQPVVDTTVKVSFKIENKENGSYRF
KEIPVTIPGEYQVADGDNAAPDVLPEIREWKGNAGTFTPSEESRIVIQDASLQETADAFA
KDYEAVIGKRLPVVTGTSANAGDFFFALIKEGKGLQKEGYRMTVDEKVAVEAETTTGAFW
ATRTILQSLKAAGNIPQGIARDYPLYKVRGFILDVGRKTFTMDWLEDTVKQMSWYKMNDF
QIHLNDNLIPLEHYSQIGEDPMQAYSAFRLESDIKEGGKDGLYKADLTSKDVFYTKEEFR
DLIQESRVYGVDIVPEIDTPAHSLALTKVRPDLRHGTYGRDNDHLALKDKYDDSLEFVQS
IFNEYMGKDLSNPVFDKDTIVHVGADEYTAAPEAYRKFADDMLKYVQDSGRTPRIWGSLS
TIKGDTSVRSEGVQMNLWNFGWANMDKMYEQGYDLINCNDGNYYIVPNAGYYYDYLNEDV
LYNLAINSIGGVTIPAGDKQMIGGAIAVWNDMTDYLENGVSEYDVYDRIDNEIALFGAKL
WGKGNKDLSAAKEDYAALGTAPRTNFTYETAKNEEGAAAHYPMDDLQDASGNGHNLQDGK
NAAIENIDGRNALKLTGKESYVSTDLTTVGLGNDLRVKVKRTTDSEEEQILFEGSYGTIK
AVQKGTGKVGFTRENHDYSFNYKLPVNEWVELEFKNEQNKAYLYVNGELRDVLGDGERVE
ARPLLATTMFPMERIGSTKNAFVGYVDDVRLGTNAEFASTMPLDYAVITANQVMGTANNP
ELTQLMKEAEAIFAAYNPDALKINELAGKIQTVLDNSDYEQADYSRIESLKKTIPSDLSP
FTEESVAWLKYVLSQIRTGLPAEMQSTVDGYEKMLADALAGLTLVEGRNINYVDNAQITA
TASSHQDNGSAPSKVLDGDTSTIWHSKWDITTMPHWIDLEMAEPTPVDGLTYVPRQTGTN
GNVTKYEIQISDNGTDYTTHATGTLKNNADTKIIEFDKVTTKHVRLVYLEAANNNGAAAE
LKLHQANVPADIDGLNAVIKEAKAIQNEGFTAESWKALQDKIADAESLAAMENADANEVE
IMKRELSKAMVSLVLDGKTTPDPEPEKVNKEKLEKFYKECLAFYKEENHSKENWKAYQDA
LAAVKAVLDNDKATQKEVEDALEQLVKITEKMNKELKDDSGTPQKPSNPSGTGGNQKPDK
NSPVKTGDGTPILFMAFMVFAAGAVLVIYGKRARKR

Enzyme Prediction     

No EC number prediction in MGYG000004799_01051.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	560	888	3e-58	0.9436201780415431
CBM32	49	179	7e-25	0.9354838709677419
CBM32	1259	1380	1.9e-23	0.9274193548387096
CBM32	203	338	1.7e-21	0.9354838709677419

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	2.75e-131	567	902	1	325	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.
pfam02838	Glyco_hydro_20b	1.41e-29	440	562	1	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
pfam00728	Glyco_hydro_20	4.73e-29	566	889	1	335	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	7.39e-27	569	888	2	293	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.
cd06563	GH20_chitobiase-like	1.89e-25	569	835	4	269	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
BCL58378.1	0.0	1	1526	1	1480
QWT17580.1	0.0	9	1468	15	1491
QPS14026.1	7.61e-282	3	1539	5	1406
QQY27155.1	7.61e-282	3	1539	5	1406
QMW75640.1	7.61e-282	3	1539	5	1406

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	2.04e-128	349	1098	3	721	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
3GH4_A	4.62e-23	434	787	32	386	Crystalstructure 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]
4H04_A	8.88e-23	441	905	34	484	Lacto-N-biosidasefrom Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4H04_B Lacto-N-biosidase from Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4JAW_A Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],4JAW_B Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],5BXP_A LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXP_B LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXR_A LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXR_B LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXS_A LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXS_B LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXT_A LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254],5BXT_B LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254]
2J7M_A	5.79e-20	1252	1384	5	148	Characterizationof a Family 32 CBM [Clostridium perfringens]
2J1A_A	5.95e-20	1252	1384	6	149	Structureof CBM32 from Clostridium perfringens beta-N- acetylhexosaminidase GH84C in complex with galactose [Clostridium perfringens ATCC 13124],2J1E_A High Resolution Crystal Structure of CBM32 from a N-acetyl-beta- hexosaminidase in complex with lacNAc [Clostridium perfringens ATCC 13124]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	1.29e-132	343	1098	19	743	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
Q8XL08	4.95e-17	1135	1384	494	766	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
Q0TR53	4.95e-17	1135	1384	494	766	O-GlcNAcase NagJ OS=Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) OX=195103 GN=nagJ PE=1 SV=1
P96155	1.06e-15	424	747	118	435	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	1.52e-14	515	816	55	365	Beta-hexosaminidase Amuc_2018 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2018 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000347	0.994735	0.004277	0.000242	0.000204	0.000174

TMHMM  Annotations     

start	end
1571	1590