CAZyme Information: MGYG000003087_00968

Basic Information

• Species: Merdibacter sp900543035
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Merdibacter; Merdibacter sp900543035
• CAZyme ID: MGYG000003087_00968
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1753	MGYG000003087_18|CGC1	191345.64	3.935

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003087	2304658	MAG	Spain	Europe

• Gene Location: Start: 7459; End: 12720 Strand: +

Full Sequence      

MTIGENIVLNKETIASSTANGLGPELVVDGNTAAPQWNSSDMKNWGAASDTSKDEVEQTP
QWIVIDRGEDAEPANITQIKLWYNARVWPMEYQIYTASASDLETGDTVDLSRWDEVVSVD
RPSSASGTSGQVVNGAGQNIADTNENSDTITAETVPALDADVQLQRYVLIYFAKVNAQAP
GNNINLREIQIFDDTQIVDVQAALDSISASDLIIAEDQVTLDPAAQMQGVEFYVRGSDLE
RVVDNEGRLSGANIGDREVTLLVGVRETRDPDNKAEKNLKVIIPDQSDAYPQSYFPAVDT
QNEKPEVIPTIQEWYGYQGEFKLDAQSRIIYHDEANVGLERAAENMKADLLEITGLDLPI
IAADASAAGASDIYLASVSEDSYDVGDEGYLMITDDNGLRIYSPTYIGCLYGTISVEQIL
YQAEDHLSVPKGIARDYPAYEVRGIMLDVARTPYRLQQLQDYTKVMLWYKMNEYHLHIND
NDNCNITGSVEDHSGFHRLESDVFPSLKSEVKHAGIPEELVNADYYLHNEDYQGNPTYTK
EEWRTLKETCTDLGINMITEIDLPGHSLLYNKYAEENPDNIPQLEGGIKYTANALSTNGG
AELLDLTGENAERALWFAQTLWNEYTDPDQEGGPVIYGDVVHIGADEYWDHSTAGIRDKF
ALFADSLRQVIQGNLGSDTKIRMWGAGSVMFSTADSVLEDVDLASNYQLDVWYHGYEDAK
ARIAEGFEVINCRDAYLYGNPGRSNRDVPNAEYLFNEWNPAMFTDNTPQPGTGSNPLLGE
PNLLGAKTVIWGDQSQEGMTERDVNQRVLRAVSIVSEKTWGATDEEDTFEQFERRAARLA
EGPGTQIAMQVDSASSLVLDYDFDHLSADGMTVYDTSGNGYDGTLSEAGTVSEDGYLRFE
GGKLSTPLKTLSYPYTVAFNVRVNAEQAAKNTTASSIFSGYDGQLQIAGTDDGSLSANVN
YFTRDLDYQIPTDGTEISVMLVGTFQGTKLYINGELQTFLSQKSDQDGVAPGNVSTMYAS
FPLPLEKIGEGLYAELADLEVYDRAFSSEEAASYYTEEWQEPINKTNVAQGMYAGGTSRT
IGDGTGYDNSDGRVRVAFKAVDGDAFELANDPADQMDVSTTDIYSYWKGNSADSALSVDL
GEVREISEIQIQWRYGGKGRDFDIQVSDDGINWESVSSIRNNQDFLSVIALDAPIDTRYV
RMQGIASNSVSGYMIQEFLVYETADKTSLGQLLDEAEKIVNDKELGFETQNETDRELFAA
VVQARAVRYHAQMSVSDVGKATARLRAALDAQATEQQVTVTFDTNGGSQVDPQTIEKNST
VHRPDDPVKEGFVFTGWYIDKECTEKFDFDALITEDLTIYAGWDKQQLPEDPASDAAIKA
LQTMVDKAVALGSDDEALQAAIEAAQAVLNEETPSATAVVTTLLNLSEAMQALNISESTD
TLRADVQATIDFINANILNDTEGLRPAKVQALRNAVQAAQDAVDDPEADADQLKAANKAM
TKAAQELWEIVTKAELEVLIEAANGYLDGDYTAESLEALQTAITAAQAVAANDDATTAEV
TDAITNLSNAIAGLESITLDTSALAHEIELVTEMVANIDNYVPSTVEGLADKLADAQAAM
NATTQEEIDAAAAVLREARLNARTKADVSALEELIAYVNSLELSAYTSASAQPVIQDLAR
AKAMLANEEVTQEEVNDMADALQASVDNLVEVNNSTNAEESTNTAAAMQTGMFAGLLALT
GGMLAVARRKKRN

Enzyme Prediction     

No EC number prediction in MGYG000003087_00968.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	434	821	1.5e-43	0.973293768545994
CBM32	1099	1218	1.6e-18	0.8145161290322581

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.36e-67	441	821	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.
pfam00728	Glyco_hydro_20	1.13e-22	440	820	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	3.70e-20	443	821	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.
pfam09479	Flg_new	2.19e-18	1299	1361	2	64	Listeria-Bacteroides repeat domain (List_Bact_rpt). This model describes a conserved core region of about 43 residues, which occurs in at least two families of tandem repeats. These include 78-residue repeats which occur from 2 to 15 times in some proteins of Bacteroides forsythus ATCC 43037, and 70-residue repeats found in families of internalins of Listeria species. Single copies are found in proteins of Fibrobacter succinogenes, Geobacter sulfurreducens, and a few other bacteria.
COG3525	Chb	3.46e-18	386	914	204	703	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AXH51903.1	1.13e-175	6	1226	191	1273
ASY50997.1	4.10e-174	6	1226	191	1273
AWS25495.1	4.10e-174	6	1226	191	1273
AMN35076.1	5.68e-174	6	1221	191	1268
QQA11576.1	1.09e-173	6	1226	191	1273

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	2.27e-47	223	845	20	571	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	8.58e-21	304	820	33	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	1.74e-13	293	579	26	295	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]
6JE8_A	3.28e-13	388	647	37	258	crystalstructure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEA_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEB_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835]
7BWG_A	7.09e-13	305	839	20	498	AGlycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5],7BWG_B A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	1.49e-50	223	845	42	593	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
P43077	5.94e-16	387	820	111	505	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
P96155	3.60e-15	292	567	128	371	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	1.97e-12	388	647	58	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
P49008	6.68e-09	387	568	110	273	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000037	0.000010	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
1725	1747