CAZyme Information: MGYG000001374_01105

Basic Information

• Species: Mediterraneibacter torques
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter torques
• CAZyme ID: MGYG000001374_01105
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1669	MGYG000001374_2|CGC4	184458.27	4.4518

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001374	3092406	Isolate	not provided	not provided

• Gene Location: Start: 248308; End: 253317 Strand: -

Full Sequence      

MHNVKKSFKRLLAVSLCASCVLSNGMLSLAEGAEDKAVNLALGCQATANAQYNQNGNDMS
ASKAVDGNDETRWSSEGAAPGWLQVDLGEQKSFTQFRILSEGGTGVTVGKQLIGKFKIEG
SNDNSKWTLIHQSEDKQAEGFPQDTVVTLEKPVSYRYVKLTVESLKTGAFDSVSIREFEI
RDKEETTPEKPQDPEENVALKKTAAADSTEDNSLIAAKAFDGNTKDRSSRWSSAVADAPH
WIYVDLGKEMDVKTVCIFWETRKATDYKIQIANTAEAPAESDWKDVKHVQDRPKALKDAI
VLDKVEKARYVRLYINSFTKNDPDNEGASWNSISIYEMEVYGGEPKVDIEEGISVDTPKK
GDKKLTVHIPEETKTEKVTYNGTDYEQVVDADLNLYQPVVDTTVKVSFKIENKENGSYRF
KEIPVTVPGEYETKEGDNAAPDVLPEIREWKGNAGTFAPNAGSRIVIKDAELQEMADAFA
KDYEAIMGQTLPVVTADSANAGDFFFALTKEGKGLQEEGYLMTVDEKTAVEAETTTGAFW
ATRTILQSLKANGNIPQGVARDYPLYKVRGFILDVGRKTFTMDWLEDTVKQMSWYKMNDF
QIHLNDNLIPLEHYSQIGEDPMQAYSAFRLESDIKEGGKDGLYKADLTSKDVFYTKDEFR
NLIQESRVYGVDIVPEIDTPAHSLALTKVRPDLRHGTYGRDNDHLALKEKYDESLEFVQS
IFNEYMGKDLSDPVFDKDTVVHVGADEYTAAPEAYRKFADDMLKYVQDSGRTPRIWGSLS
TIKGETSVRSEGVQMNLWNFGWANMDKMYEQGYDLINCNDGNYYIVPNAGYYYDYLNEDT
LYNLAINSIGGVTIPAGDKQMIGGAIAVWNDMTDYLENGVSEYDVYDRIDNEIALFGAKL
WGKGNKDLSAAKEDYAALGTAPRTNFTYETEKNEEGAAVHYPMDNMKDASGSGQDLKEGK
NAAIESVDGRNALKLEGKESYVSTDLATAGLGNDLRVKVKRTTDGDEEQILFESSYGTIK
AVQKETGKVGFTRENHDYSFNYKLPVNEWVELEFKNEQNKTYLYVNGELRDVLGDDERVE
GRPLLATTMFPIERIGSTKNAFTGYVDDVRLGTNADFASTMPLDYAVLTANQVIGKTENA
QLAQLVKEAEAIFAAYNPDASAINDLAAEIKAVLDDSDYKEADYSRIETLKKTIPSDLSP
FTEESAAWLEYVLSQIRTGLPEEMQSTVDGYEKMLADALAGLTLVEERNVNYVDNAKLTA
TASSHQDNGSAPDKALDGDTNTIWHSKWDITTMPHWIDLEMEEPMAVDGLTYVPRQTGTN
GNVTKYEIQISNDGTNYTKHAEGTLKNNADTKVIDFNKVTTKHVRLVYLEAANNNGAAAE
LKLHQADVPADIEGLTAVITEAKAIKNEGFTKESWDALQNKIAEAEELASAENADANDVE
IMKRELSKAMTSLILEDKVTSDPEPGKVDKSKLQELYNKYKGIKADGYTAESWTAFAEAR
TEAETVLANEKATQEKVDKAAENLEKAFKSLKKEETKPDPDPTPDPDPGAADVSGLKNLY
EAYKDIKSDGYTAESWAAFDKARAEAEKILANPNATQDDVNAAKAALEAAYKGLVPKTQP
NPTPGGNGGNVGSTAVVTGDSANIAGYLTVLLAAGGIAVVTFFRRKRVK

Enzyme Prediction     

No EC number prediction in MGYG000001374_01105.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	560	888	1e-58	0.9436201780415431
CBM32	49	179	4.4e-26	0.9354838709677419
CBM32	1259	1380	7.3e-25	0.9274193548387096
CBM32	202	338	2.9e-20	0.9435483870967742

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	2.02e-130	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	1.90e-29	440	562	1	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
pfam00728	Glyco_hydro_20	4.25e-29	566	889	1	335	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	7.63e-25	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.
pfam00754	F5_F8_type_C	7.84e-25	1259	1367	1	111	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCL58378.1	0.0	1	1614	1	1553
QWT17580.1	0.0	9	1438	15	1455
QPS14026.1	2.61e-299	38	1667	43	1523
QQY27155.1	2.61e-299	38	1667	43	1523
QMW75640.1	2.61e-299	38	1667	43	1523

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	6.12e-123	382	1098	33	721	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	9.43e-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]
3GH4_A	3.60e-22	432	787	30	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]
4A41_A	8.17e-22	1255	1383	29	159	CpGH89CBM32-5,from Clostridium perfringens, in complex with galactose [Clostridium perfringens],4A44_A CpGH89CBM32-5, from Clostridium perfringens, in complex with the Tn Antigen [Clostridium perfringens],4A45_A CpGH89CBM32-5, from Clostridium perfringens, in complex with GalNAc- beta-1,3-galactose [Clostridium perfringens],4AAX_A CpGH89CBM32-5, from Clostridium perfringens, in complex with N- acetylgalactosamine [Clostridium perfringens]
2J7M_A	6.95e-21	1261	1384	14	148	Characterizationof a Family 32 CBM [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	4.44e-127	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	8.92e-19	1194	1384	572	766	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
Q0TR53	8.92e-19	1194	1384	572	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	1.12e-15	437	692	135	380	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	6.52e-14	555	816	100	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
0.000296	0.998363	0.000761	0.000207	0.000177	0.000150

TMHMM  Annotations     

start	end
1644	1663