CAZyme Information: MGYG000001004_01029

Basic Information

• Species: CAG-56 sp900539525
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-56; CAG-56 sp900539525
• CAZyme ID: MGYG000001004_01029
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1574	MGYG000001004_19|CGC1	174206.16	4.7813

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001004	2903340	MAG	Austria	Europe

• Gene Location: Start: 32598; End: 37322 Strand: -

Full Sequence      

MRAKKAVFAGVLASVMLCQTISAPWLAGTGALHAQAAAANVVLNKTATASGVENDSAVWT
ADKAVDGDSSSADSRWSSARMRPTGTGTEQTPQWLKLDLKADTTEVESIKIKYYLKVWST
QYKIQTSATGEDGSWEDVYTQAQRADSNDTDVIDTIEASAMTKTTLKRYVRFYFEKLNAN
AAGVAVSVREIEIYGTQGGTIDTVTSAQEALNAVPALTVSETDTALQIPSVSDAYEIRVY
GSEVDRVIGDDGTVSPLHIGERSMNVILQATSKSDPSDTAKKNMTVTVPDNTGRFPELFP
QISDPNPMPDVLPTIQEWYGYNGDFTISEDTEIIYHDPANLGLAEVAAEMQADLKEICGF
VPEVRAGASGDSNDILLESLTEDTYGTGEEGYLLVTDDAGIHIFSAGKTGVLYGTVTVEQ
ILYQDQAHQTVPKGVIRDYPLYAVRGIMMDVARIPTRIQFLEDYTRILKWYKLNEMQIHL
NDNQWSDPPYSPDYNQWENVEASHRLYSDTFPSLAVQDSKFMTDRDYEGRYDYYYNVHTE
MKEKHGTAGELYYTKEEFKDLQKQAEARGIQVVAELDTPGHSAAYTKYVYKNQEEVIKSL
TEKGYLNRADYLDANGEVKAGASFYIHNPNNFELLALDDQSTDQTTRQNAVNAKIFMKAL
FDEYLGGDDPVFTGDAVSAGVDEYWDKNTGNNKDAFRRYMNYMYNLLGESENGYGKQVRM
WGAVMLMPGSTVINKDIVLDIWATYEDDPIARMNEGFRVINVPQPYLYTTPGRYHKDMIR
EEYIYYNWDPVIFNGNVRAEKGEPLLLGAKAALWGDENREGITEADLNERYLRLCAMVGE
KTWGGTKADDTFVDYSQTFNSLREGPGTQIANQIDSKSNVVLDYDFENVSKDGKTVYDAS
GNGYNGSITGGEVVEKEGQTWLRFDGNTTVETPLTSLGYPYTMSFDVYLDGTEENTKESS
LFSGYDGRLQVAGMDGKLSLNRDYFTQSFDYQVKNEEKHTITIVGTYQVTKLYVDGVFTK
ILYAAASDKDNGGAVGASTWADQDNNFRTTFVFPMNTIGKDFSGYLANIKAYNKALSTEE
LSAEESAGGEVDVARNRHAYADNGNSTFWGDEMRLYPAWKATDGDGHVTGATGVSTSNES
RWNSSDRDTDFLMVDLGENRSISKVVIDWEASRYAADYEIQVSGDRKNWKTVKTVTGNTS
ALTTDTFDAENARYVKMQGVHRRAGSNEYCIYEMKVYGTVDKSQLKKACEEKAEILAQKA
ISWENANVLYDGYVAAKAVLGDVMAGQEEVDAAVLALEQAEEAAKKEEAAEKQEAIAEAI
SKAAAVLKEKDSYDAASWQAFEKAYEAVVNASADLTAEELQTLLAALENAQKGLVRKPSG
PSNPEQPAKPAVALTAPKVTAVKSMETKVRVSWEKAEHAASYQLYRKTGSSVTKVGGPVT
GTTAYDTNPVGGKKMSYYVVALSGGQKEYKDSAAGSTKDITLPKATAKVTATQQKGQKAV
TVKWKKVKKASSYIIYRAENRKGSWKKIATVKKGISYRDKKKLKKGKTYYYRVVTVSAKT
YSPMKEAKKAVKIR

Enzyme Prediction     

No EC number prediction in MGYG000001004_01029.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	437	844	6.2e-47	0.9703264094955489
CBM32	1116	1235	2.4e-20	0.8548387096774194

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	6.63e-70	444	845	2	326	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	1.88e-28	445	844	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	4.64e-24	442	843	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
pfam02838	Glyco_hydro_20b	1.36e-19	309	438	2	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
COG3525	Chb	1.66e-19	244	768	71	534	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AXH51903.1	1.16e-248	40	1243	191	1274
AMN35076.1	6.34e-248	40	1238	191	1269
ASY50997.1	4.86e-247	40	1243	191	1274
AWS25495.1	4.86e-247	40	1243	191	1274
QQA11576.1	1.34e-246	40	1243	191	1274

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	7.93e-57	226	1064	19	724	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	9.82e-21	309	862	34	493	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	2.43e-15	390	584	37	196	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]
1M04_A	8.39e-14	388	749	96	455	ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]
1HP4_A	1.93e-13	388	600	96	276	ChainA, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1HP5_A Chain A, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1JAK_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],1M01_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],5FCZ_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus],5FD0_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	8.85e-60	226	1064	41	746	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
B2UP57	1.49e-14	390	584	58	217	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
Q5RC84	1.35e-11	390	857	114	499	Beta-hexosaminidase subunit alpha OS=Pongo abelii OX=9601 GN=HEXA PE=3 SV=1
P06865	1.78e-11	390	857	114	499	Beta-hexosaminidase subunit alpha OS=Homo sapiens OX=9606 GN=HEXA PE=1 SV=2
P96155	8.27e-11	372	587	194	376	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
0.004271	0.877831	0.116855	0.000518	0.000257	0.000235

TMHMM  Annotations     

start	end
7	29