CAZyme Information: MGYG000002014_00926

Basic Information

• Species: Merdibacter sp900754715
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Merdibacter; Merdibacter sp900754715
• CAZyme ID: MGYG000002014_00926
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1944	MGYG000002014_31|CGC1	213898.01	3.9498

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002014	2253473	MAG	Spain	Europe

• Gene Location: Start: 14685; End: 20519 Strand: -

Full Sequence      

MLRKISKIILSALMALSVISWSDIRASAQEENLALNRPVTVSGVEGGVQDDGTLTYPQFD
PSNLTDGNASTRWSSDEALTSINLEDNPDQNVWAMVDLGEEKEIGTIVMKWQNANSRDYD
VQVSSDAQQWTVLHHYVDPDNDGRDYTETLSLDAPVSARYVRIYARLGTIIASIANMQCP
TISLYELEVYPYSDEATLNDVLASVLEQPAQADGDMIALPQVPEGYSVRLYATSNPAVVS
ETGKIITPLEDMNVNLFYEVSDTEGNVLQGDDPKKVTIAGQYAPQESINEKPDVIPELRE
WKGDTGSFVFNGRIVIEDARLQQTAEQIAMYLKEMSDLDCVITQDEPQAGDIVLQLDESS
VLGEEGYAMDIGDILTVSALSEKGILYGGTSISQILSQDEDHDEIPKGQVRDYPQYAVRA
VMLDVARQYIPLDYLSELTRYAGYFKLSEFRNHINDNGGEQTAAFRVESKVYPQLNEGLP
KDQVYSQEAYKAYQKDAKRYGVDVVTEIDTPAHAGAFANIDESLLMDGYHIDLRTEEAYQ
NAVGVMKNVFDEFLDGEDPVFQNGKFHIGTDEYDKSYSEVVRRYMNELIEYVNGKGYETR
FWASLGTNGFAGETPVSTDVIAHMWSHSWASFDEMKDAGYRFINNADGILYIVPWAGYYN
NYLNIASLYDTWEYSNLNGGHYLQTGHPQLLGGEAALWYDMKVGASEFDIFDRQRDQVML
MAEKGWYGEDDDETSDEFMERVEALGTHAPNANPGRYVESESSLVASYDFDDIADGIAED
ASGNGYDAEVHDLYAKDDALRLKGEGYLSLPFDTLGYPYTLQCDITIDSATGENALLFSG
KDGKFYYNYDGTGHFGYERKGYAYLIDADIPLGVTFAMTIVCDETNTSLYINGMFVGSGE
YYQVSGASSQGSSTFVMPTEKIGEGIYGTMDDLKLYNYAMSAAQVAGASESEDSGNIALH
KNVEVSGVEGGYNEDGTLVYPQFDPSNATDGSESTRISLNTDDDAWVSVDLEKPYLLDRV
IIRFNELPNAYAIQVSEDGQSWTQVAEYRDLNGGAKQTMTVNFDHLVKARYVKYQQLERF
TYGPTGGRYSGNFTELEVYGYDTERFVQFIAEAQERLSSCDDGSAFAQSVYTDLQTLEAM
LETGPVSTMNQLANMISDKLTMLKNDSAPQAVPDKSALQALLEETLDENEYSEQSWNKYA
QTLDYGSTIYYHAGADQALVDYACARIEEAKAGLSMRNYITISSNKSVYQDYALSRLIDG
DTSSMTWLQNNQAQGDHIQFSFREPLALSQIDIYSVNAGSDILHHGRVEISADGNSWQSI
AEIGENEHEVVTLEETPVMAVRITVTQAAEYWWKITEVMFNEAQIQDKAVLEEELNKQVD
LSLYSEASVQAYEAARAQAEAVFADEQATQPQIDTAAAQLVAAREALEKKLDKSALGSLL
GTKLEADAYTPSSYAEYEEAYLNAQDVYDDANATQNEVDQAAWKLQEAVSRLVIADFKDE
LNDLIAQASAWNEDEYTANSWTPFMEALDQAKETAADEQATKADADEAAAALRAAMDALQ
RKASEAAMAALQDIVDQAEALQNDELNDLIANANALLADSDNASATALVSALLDLSEAMQ
ALNVGESTDALKADLEATIQFINANILPNVDNVRPGKVQALKDAITAAQDVLDNEEATAD
QLKQANRTLTKAAQELWQIVSKNELNAMITAANGYAEGSYTAESIAALQDAITAAQSVAD
NDDATTAEVTEAITSLADAIAGLEKIVLDTSALAHEIELAEAILANIDDYVPGTVEGLQE
KVDAAKTALDAMTQEEIDAATQTLREARLRARTKADKSALDELIETANAMTLGGYGRAQV
LAFRQALVQAQQISIKEDATQEEVNEATETLNTAMREMMESTASAGTDSEAAKTMAELQT
GAFALLLMTSALMAWMLKRRNVRS

Enzyme Prediction     

No EC number prediction in MGYG000002014_00926.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	412	727	3.7e-45	0.9673590504451038
CBM32	56	174	3.8e-23	0.8467741935483871
CBM32	981	1078	5.5e-19	0.7580645161290323

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	2.73e-77	418	728	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.
cd02742	GH20_hexosaminidase	1.64e-31	419	726	2	302	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.
cd06562	GH20_HexA_HexB-like	5.13e-27	416	698	1	297	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.
pfam00728	Glyco_hydro_20	2.18e-24	416	726	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
pfam02838	Glyco_hydro_20b	1.81e-21	291	412	1	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SDT48132.1	3.94e-252	199	1363	33	1195
API91270.1	3.90e-221	212	1900	55	1873
QTY17007.1	5.29e-220	212	1900	55	1873
QMW75624.1	2.96e-211	32	1293	483	1742
QPS14042.1	2.96e-211	32	1293	483	1742

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	6.58e-61	209	928	11	724	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	4.86e-27	282	726	23	474	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	3.69e-18	291	742	38	505	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]
7BWG_A	3.49e-13	365	746	87	499	AGlycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5],7BWG_B A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5]
1HP4_A	9.16e-12	363	572	96	320	ChainA, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1HP5_A Chain A, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1JAK_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],1M01_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],5FCZ_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus],5FD0_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	4.02e-64	209	928	33	746	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
Q54SC9	2.82e-13	352	572	95	314	Beta-hexosaminidase subunit A2 OS=Dictyostelium discoideum OX=44689 GN=hexa2 PE=3 SV=1
E9DFH0	3.84e-12	364	728	121	539	Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 SV=1
P49008	6.39e-12	281	575	21	338	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UP57	8.28e-11	383	572	77	279	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
0.000428	0.998135	0.000894	0.000192	0.000176	0.000160

TMHMM  Annotations     

start	end
1920	1937