CAZyme Information: MGYG000001310_00596

Basic Information

• Species: Mediterraneibacter lactaris
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter lactaris
• CAZyme ID: MGYG000001310_00596
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1347		148341.76	4.2977

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001310	2729735	Isolate	not provided	not provided

• Gene Location: Start: 8233; End: 12276 Strand: -

Full Sequence      

MKKKKDMKKPLLAAVLACSMVQIPAIPVAAAAPENLALNQTVTASSYEQPTNNPEKTSPS
KAVDGDLTTRWGTAQNLAANEWINVNLGSSKQIQQININFERTDDAQNILGYKVEIANGN
DTYTEIYRKEEKAKQKEVIKLTSPVSATDVKVTILSADAGTINWVNVGINEIGIYGSINN
DYSLSDVAGMITGGTTIAADVADFPMPTVPEGFNIRINGADFEQIISRDGKIVHPLTDKT
VKVSYVITKEETGEELVTDDFTYTIAGQHTTNAAKNTKPSIIPEIAEWYSDSTDSVATDS
ITAVTYDNNALEDVVNEFIADYKDFSGIELQKVKGNAKANAFNFSLSAPDELLGDEGYTM
NILSDRINVASESTVGNMYGMQSILQMYKSNPDAFSIGTMRDYPRFSTRGFVLDAARKPV
SMDMLKEISRTMRYYKMNDFQVHLSDNYIWLEDYGKLDQENQAFDAYDAFRLESSLTNDA
GESPTAEDYSFSKKEFKEFIQTERAVGVNIVPEIDVPAHANSFTKVWPELKVTNKTSSTS
ANRPLIDHLDISKTETVQKIEEIFDDYTHGSDATFDSETTVHIGADEFLDNYSAYRNFIN
TIIPYVKQTNTVRMWGGLTWIKDNPITQINADAIDGVEMNLWSKDWADGIEMYNMGYDLI
NTIDDYGYMVPDGSKTRANSYGDLLNTSRIFSSFEPNKLRSSSGYVAVPSGDDQMLGAAF
ALWNDNIDKRASGLSESDLYWRFFDALPFYAEKTWAATGQEKGSADALNTLATSMGTGPN
TNPYYQESSVDNIYESYDFNSGKGLDDTSENDRDLTLASDSTAKVQNKALVLSGDKSYVE
TPIEQLGNGNALSFDITLSSEPESGDILFESDAAYGTHDIRIMSNGKLGFTRELYDYYFD
YTLPVGEKVNIKIVTQQQVTKLYVNGQFVSNATGEFNHNGTTKKSGITNATFALPLQRIG
SETNAVQATIDNVNVTAADMYNKSKWTGTTNSETTYNNVEGLLRYAFDNDYTSRWHSNWK
GATDKLTGSNSFYAEINFGQKYTINQFSFTPRTDTASGYVTKADLYIKANDSDEWTLVAQ
DQTFAADAAQKTFTFNAQEVQYVKFVAKASSDGWVAVSEFDIANTAQNPDQPEADKTALQ
ELVNQAVTDFTGYTSESVTAYKVALDNAKEVLTNEDATQAEVDEAIAALTNAVLVTDKSK
LQEKIDQAVTDFDGYTADSVAAYKAALARLNEVLADTDATPAQVSEAIAAFDLARLVKDT
SDDGKKDDDKKDDDKKNDDKKDDNKKDDSKKEDGTNDNSSSTNGKADKKDTASKAAKTGD
ASTALPYMLLMLASGSAVVILKKKKEQ

Enzyme Prediction     

EC	3.2.1.52

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	402	757	8.6e-55	0.9703264094955489
CBM32	42	161	9.4e-20	0.8870967741935484

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	6.11e-112	408	756	2	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	5.71e-31	409	755	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.
COG3525	Chb	1.63e-26	352	772	202	626	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam00728	Glyco_hydro_20	5.28e-23	406	736	1	340	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
pfam02838	Glyco_hydro_20b	5.11e-19	278	402	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
VEG17438.1	0.0	12	1124	14	1285
BBA57859.1	0.0	12	1124	14	1285
ALE12005.1	0.0	21	1124	1	1264
ADP36558.1	0.0	21	1124	1	1264
BBA55782.1	0.0	21	1124	1	1264

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	2.35e-91	197	961	12	720	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	1.49e-25	267	756	22	475	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]
7CBN_A	5.71e-18	326	587	54	308	Crystalstructure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835],7CBO_A Crystal structure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila in complex with GlcNAc [Akkermansia muciniphila ATCC BAA-835]
7DUP_A	8.62e-16	306	587	33	316	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
6YHH_A	2.10e-15	318	587	64	317	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	3.78e-96	197	961	34	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
P43077	1.20e-18	355	763	111	513	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
B2UQG6	3.28e-17	326	587	73	327	Beta-hexosaminidase Amuc_0868 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0868 PE=1 SV=1
P13670	4.18e-16	319	558	247	491	N,N'-diacetylchitobiase OS=Vibrio harveyi OX=669 GN=chb PE=1 SV=1
Q9HGI3	1.32e-14	355	764	128	554	Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA 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
0.000644	0.992365	0.006234	0.000266	0.000231	0.000215

TMHMM  Annotations     

start	end
12	31