CAZyme Information: MGYG000001018_01782

Basic Information

• Species: Mediterraneibacter sp900751785
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter sp900751785
• CAZyme ID: MGYG000001018_01782
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1651	MGYG000001018_117|CGC2	180225.63	3.8452

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001018	2841260	MAG	Sweden	Europe

• Gene Location: Start: 23349; End: 28304 Strand: -

Full Sequence      

MRKTRKCFKRVSACALSAAMVFTMATPFAPLTAEAAGEDPVNLAIGATATANDSETSDYT
ADKAIDGIVNRDAPKPQSRWATNTSSAQTPKILTVDLGETKTFQSFVIAWERTNITSYEI
QTSDTGGSDASEWTTVYEKEGSDQISALDENIHLAEPAEARYVRLYVDGYDLNPGSWQSV
SVYEFQVYENEIPDELLTEENYNLEGTAEASDYEPTEGDTQAASMAIDGDQTTRWATNPS
NDGVARTLTVTLPASQRVQFFRIIWERLNIESYKIEVAESDDAEFTEVYAKTEPITATNE
VISLDAPVWAKKIRLTVDGYNGGSNDWPNVSVAEFESYAVEPAQISEDATPEEVADLLGA
PTINEDGTALVLPEVPEGFTVEFLADYEEVVGKDGTIYTPLTEKTVKGIYKVTKGEESAE
GSAEHTVVIPGKYDSEGVNAKPTVIPELAEWYGKDAEGSFTVGGRILVSEGASEFMDAAE
ALAEDYEAELGTAMTVETGDAPQAGDIYFISDETNGLGEEGYIMDIGEYVTVSAENATGA
YWATRSILQITELNDETMPYGITKDYPKYEVRGFMLDVARKPISMETLQDIAKEMAYYKM
NEFHLHLNDNLIFYEDYASAEEARELAYTGFRLESDVLEGGNDGLNQADLTNEDLYYTKA
EFRDFILSCRSMGVNITPEFDTPGHSGAFTKVRPDLMLQNIVSGAANRAGEQFDLSPEKY
DESLAFVESIWDEYLTEDMFDQSMTVHIGTDEYYGEKNRFRMFSDDLIEYVQSKGYTVRL
WGSLSSMPGEADVRSEGVQMNVWNTGWANPTNMYNEGFELINTIDGQLYMVPAAGYYFDY
LNTQNLYNNWTPNNFDGTVIPAGSEQMLGSTYAIWNDSVDTKANGISEVDIYDRFADAVP
TMASKNWGEAQDQTWAEMEATVDELGDAANSNPYHEASADENGEYMSYEFDDTTDSSANG
RDLAEPVNAEIADGSLKLNGGESYVSTPIDKLATGNTLEFDITLDTPAQAGDILFEADNE
GSNGDYVHDIRIMDDGRLGFRRELYDYYFDYKLPVGETVHLSISTNGTSTTLTVNGTTYE
ASGVYRNRQTDGEVRVEGITRATFLLPIQRIGSETNAIEAVIDNVTVKQGAAVDYNKSAW
SKVEVDSETVYSSTEGLFEYAFDGNSGTIWHSNWQGASDKLKPQGTFDEIGGVIDLGQKY
TINQFKFTPRSGTNSGQVTKADLYVKANEGDDWNKVAEDAEFADDATTKTFYFDEQEVQY
VWFVAKESDDGWVAVSEFDIANAPAQSYNVYVEAQEGGTVSGGAKGIAENTEITVTAEAD
KGYTFAGWYDAVTGTKVSDNAEYTFAVTENTALTAQFTKNEEPDPEPGEEISTAVLEYAI
ELAADVNTDGVIDAVKTNFENALKTAEDVLAKVQAGDTSVTQSDVDSAWQNLIKAMQYME
FKSADKKDLAAVIAAAEDINSRLDQYLETGKDAFTSALATAQEVYEDELASQDEVNSAWI
NLLNAMADLRFIPDKGLLEDLIAQAEALNEADYEAQSFAVMRTALAAAKEVFADENATED
DVNSSVEALEDALAQLTASSDGTQAGGNDQQSGNTGNGGQTSGSSSSGSSNTSGSKAVKT
GDTATVFPFAAAAAVAAAAAVAVIRKKEEEK

Enzyme Prediction     

EC	3.2.1.52

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	563	907	1.9e-60	0.9703264094955489
CBM32	48	186	2e-21	0.9435483870967742
CBM32	211	336	3.8e-17	0.9516129032258065

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.13e-130	570	908	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.
cd02742	GH20_hexosaminidase	1.08e-33	572	908	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.
pfam00728	Glyco_hydro_20	2.38e-29	569	884	1	326	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	1.62e-23	436	988	118	694	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06563	GH20_chitobiase-like	3.43e-21	569	840	1	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
QQY27155.1	1.14e-314	41	1515	43	1484
QPS14026.1	1.61e-314	41	1515	43	1484
QMW75640.1	1.61e-314	41	1515	43	1484
QQV05894.1	4.48e-314	41	1515	43	1484
QTQ18922.1	8.45e-269	31	1416	27	1436

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	2.15e-112	352	1113	1	720	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	6.86e-27	441	926	33	494	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	1.80e-19	459	880	47	475	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	1.57e-16	485	926	50	499	AGlycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5],7BWG_B A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5]
6JE8_A	1.39e-14	556	752	77	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	7.32e-118	352	1113	23	742	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
P49008	3.20e-17	427	696	26	282	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UP57	8.51e-14	556	752	98	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
P96155	1.20e-13	517	698	205	383	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
Q7WUL4	8.04e-13	518	922	80	463	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 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
0.000424	0.998699	0.000204	0.000259	0.000212	0.000176

TMHMM  Annotations     

start	end
13	35
1625	1644