CAZyme Information: MGYG000003087_01992

Basic Information

• Species: Merdibacter sp900543035
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Merdibacter; Merdibacter sp900543035
• CAZyme ID: MGYG000003087_01992
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1693		185447.93	3.88

Genome Property

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

• Gene Location: Start: 799; End: 5880 Strand: +

Full Sequence      

MLKKTMKLLLAGGMALSMLPVQAQPLFAVEAPVNLALNKVATSSENETDYYTAAKAVDGI
VNRDVSDKKQQSRWATNTHSDGKAMWLKVDLGEAQTFQSFVLAWERTNITGYEIQVSDSG
ADDSWETVYTKAGDEGISGINENIHLEEAVTARYVRLYIDGYNGGDNNWRSVSVYDFQIY
ENEIPSTVLPDENYSLEGTATASDYEPTTGDTQRAEMAIDGNKLTRWATNSSSAIAERTL
TVTLPASQWVQYFRIIWERLNIESYHIDVAADDSDNFTTVYSTDTPITKTNELITLEKGV
WAKQIRLVVDGYNGGDINWPNVSVAEFESYAMEPAQISEGASAEEVASMLDAPVINEDGT
ALTMPEVPENFTVEFLADYEQVIDRDGNIYKPLTGKTIKGVYKVTKADGTHAESDEFTLE
VSGQYADEGENAKPIVIPELAEWHGTSGTFVPTEASRIVIDANASDIATAAAEALQADYA
DESGMTMEIVKDGTPQAGDFYFVADAESMLDEEGYLMEIGDYVTVKAEQATGAYWSTRSI
LQILKQNDGTMPKGITRDYPKFEVRGFMLDVARKPASMETLQFVVKEMAYYKMNDFAVHL
NDNLIFYEDYENAEEARDLAYTGFRLESDIKEGGNGGLNKADLTNKDMYYTKAEFRDFIL
DSRAMGVNIVPEFDTPGHSGAFTKVRPDLMLDHVVTGNANRAGEQFNLALEKYDESLAFV
EALWDEYLTDDMFDESMTVHIGTDEYYGDKNRFRVFSNDLINYVQGKGRTVRMWGSLSQM
PGEAEVASEGVQLNVWSTGWANPTDMYNAGYELINTVDGMLYMVPAAGYYFDYLNTQNLY
NNWKPNTMGSTTIPAGSDQMLGSTFAIWNDSIDTRANGISELDVYDRFADAIPTLASKNW
GEADDLTYAEMEAAADALGEAPNNNPYHEETAEDGEYMEYEFSAGSELEDSSANDRDLSN
ETNVTIENGELQLNGGESYVETPITKLGTGNTLEFDITLDEEPEAGSILFEADTEGNEDY
AHSIRIMDDGRLGFTRELYDYYFDYTIPVGETTHIIISTDGTKTTLIVDGETYAAVGTYR
NRQTDGEVRVDDITIATFVLPLQRIGSKTNAIDATIDNVVVSEGAYEDPTILDSSTFTVT
SDNENPPAGSEGPVELAFDGDTSTFWHSNYTPYQELPATVEIDMNAVYNIDKFSYLPRQS
GTNGIITEYSLYYKLNADDEWTALVENGTWAGNSSLKTARFDAVEARYLRFVATEGMSDS
GRMFASAAEFYVHKVYEEPSEPGNPASDVALQALSNMVEKANALGSDDAALQAAIKAAQA
ILDKEAPTATEVVTALLNLSEAMQALNTDESVDALREDVQATIDFINENILTNVDNVRPG
KVDALEAAVEAAQKLVDDPDTTADELKAANKAMTKAAQELWEIVTKAELEALIEAANGYL
DGDYTAESLEALQTAIEAAQTVAINDDATTSEVTDAITSLANAIASLEEITLDTSALAHE
IELATEMAANIDDYVPSTVEGLADKLADAQNVLTNATSQEEIDAATETLREARLNARTKA
DVSALEELAAYVNSLDLSGYSQLSVQRLQAALSAANTLMDDEEASQEAINLAEYTLQKAL
DELTQEEAEENIVPKPVGTQSGSAVQSTDADEQETTAADVTTSASASTSSYALIFTLLAA
GGILLITHKKRQR

Enzyme Prediction     

No EC number prediction in MGYG000003087_01992.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	556	901	8.3e-60	0.973293768545994
CBM32	1141	1271	1.9e-21	0.9435483870967742
CBM32	41	177	3.7e-21	0.9274193548387096

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.37e-126	563	901	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	1.05e-31	565	901	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	3.73e-28	562	877	1	326	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	8.99e-24	494	1013	187	717	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06563	GH20_chitobiase-like	2.00e-22	562	876	1	324	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
QPS14026.1	0.0	33	1490	43	1475
QQY27155.1	0.0	33	1490	43	1475
QMW75640.1	0.0	33	1490	43	1475
QQV05894.1	0.0	33	1490	43	1475
QTU82680.1	7.63e-293	28	1346	29	1307

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	1.19e-116	344	1107	1	720	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	1.74e-27	433	919	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]
4A41_A	1.44e-25	1132	1272	25	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	2.05e-21	1136	1273	10	148	Characterizationof a Family 32 CBM [Clostridium perfringens]
2J1A_A	2.10e-21	1136	1273	11	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	1.53e-122	340	1107	19	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
Q8XL08	2.66e-20	1121	1297	613	787	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
Q0TR53	3.49e-20	1121	1297	613	787	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
P0DTR4	4.32e-17	1119	1273	499	644	A type blood N-acetyl-alpha-D-galactosamine deacetylase OS=Flavonifractor plautii OX=292800 PE=1 SV=1
P96155	1.63e-13	510	692	205	384	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI 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
0.000275	0.999062	0.000173	0.000175	0.000159	0.000143

TMHMM  Annotations     

start	end
1664	1686