CAZyme Information: MGYG000000134_01495

Basic Information

• Species: Longibaculum muris
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Longibaculum; Longibaculum muris
• CAZyme ID: MGYG000000134_01495
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
879	MGYG000000134_7|CGC5	100485.17	4.8417

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000134	3162983	Isolate	Canada	North America

• Gene Location: Start: 146255; End: 148894 Strand: +

Full Sequence      

MRTSEKSYDGKYSIKVGNYKPENEHEVPIWSYNYGKGSVNVVIDNVKPNTTYEVTTHYFN
DTGVKMSTGVLDVDGSYSADYPWKLASNIKTNNQKSTSWQTNVHTIKTGPRTDQIYAFAY
MEWTGNEKGAGVFYFDDVEIKELETNAKDITTIAYEEKTDGFPNTVPAVQNFEQTKGTFK
LTKRNQVFSTDQYSKAKTEYLAKSMKEKGLIDKYTIRAIDDVKDAKGITLIKKPIQFKLS
DTIQKQKCKKDTYQIDITEDKVMIYSDYIEGIQNGSMTILQAFTQRDSLNCGTVEDYTDQ
NVRGLQVDSGRRYYSIDWLKNQIEQMAYYKQNVLQLRLKDNEGIRFDSKVAPELVDRKGG
FWTQSEIDELVNHAKKFNINVIPEVDFPGHSGQEADYHSDWKITKVCSNLDFSKAEVREY
IFSIYQEAADMFHADTIHIGGDEYFQTSGWNQDITGEQKLTAWAQEVTGNPKADHNDALK
LFFNEAAKPFLEKGINVLVWNDNMFSFNSAVDLDKRITIDFWAGSIYGSIIASDAIKAGY
NVMSSSASNYHDLWPQQNQDKLDRPAPKNLYENFTRYTYSKAAFNYPFYNRDEILTEGLD
QAQGQVFPIWDDAHGYVPEYVLSRTLFPRYAGFAYKTWGAEYENKLTYDEFERLAYAVES
PRPDLLGKQVEKNYTALDYKTIVQTIKDGLAKIKTENPIIQNNIKELSQLLNQKIDKTLY
TVEEVENLIRKYENVEYVADTGKVTIQYVDENNKDLCDPIIIQDEVGKDYVTEAKEFEGY
TLKQTPNNAKGMIERDDQIVVYVYQKNQTPVDPDKPNEGDQTTPTPVDPNKPSGGNQTQG
TDTVKTSDETTILTTVTVALIALGGIYLTLRTQKRKMNS

Enzyme Prediction     

No EC number prediction in MGYG000000134_01495.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	301	640	6.4e-58	0.9554896142433235

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	2.15e-43	302	639	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.
pfam00728	Glyco_hydro_20	5.79e-42	303	638	4	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06562	GH20_HexA_HexB-like	4.84e-36	303	647	4	331	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.
cd02742	GH20_hexosaminidase	6.31e-34	303	639	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.
cd06563	GH20_chitobiase-like	1.00e-33	303	655	4	357	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
QMW74199.1	4.82e-318	1	739	53	789
QPS12532.1	4.82e-318	1	739	53	789
QQY28682.1	4.82e-318	1	739	53	789
QQV07490.1	4.82e-318	1	739	53	789
QNS02236.1	2.88e-98	7	640	73	688

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6YHH_A	1.54e-22	251	568	92	431	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
7DUP_A	2.65e-22	251	679	79	529	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
7DVB_A	1.10e-21	251	679	79	529	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_C Chain C, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_D Chain D, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
4H04_A	1.74e-21	163	638	34	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]
6JE8_A	3.89e-20	251	556	37	357	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
P43077	8.83e-20	219	638	79	505	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
B2UP57	2.52e-19	251	556	58	378	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
B2UPR7	1.78e-18	250	612	181	538	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
Q7WUL4	5.86e-18	251	526	82	392	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
Q54SC9	7.29e-18	251	560	109	426	Beta-hexosaminidase subunit A2 OS=Dictyostelium discoideum OX=44689 GN=hexa2 PE=3 SV=1

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
1.000049	0.000007	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
851	870