CAZyme Information: MGYG000003984_01394

Basic Information

• Species: Mediterraneibacter sp900752395
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter sp900752395
• CAZyme ID: MGYG000003984_01394
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1764	MGYG000003984_20|CGC1	193748.2	4.5099

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003984	2095190	MAG	United Kingdom	Europe

• Gene Location: Start: 6852; End: 12146 Strand: -

Full Sequence      

MKKKIVSCLLAAAMVVSSGAAVPGFFFAPEKVQAEENDTKAGSENLALKGTAAASHAETD
STSAAKAIDGNKGTHWGTAPDRVTNEWIEVTLEKPTKVSEIKVFWERTGATGSHQNNIKQ
WKVDVKTMSGEYKNVYEKADEGTYAPSEQTITLEADKQEVVTAVKITVNKADKGPDDFWS
NIGLSEVEVYGEESDIEATENTNHVQGTGVTAEASTTEAGSLPVSNIKDGNNQTRWASDY
TDAKAQTVTVTFPKLTLVKELDFDLFTRNVAPMPSNVKSFDLIYTDAAGAEHTVKINNEK
SAESGKTGYVTNVQHIFETPVYMKSFKMANFDLQIDIEGTNGYNNISISEVRAYSNDQSE
TPQDQTLDEVVASIKGTKIAKDVKEFALPSVPEGFTIESNGADFEQIIGAADKETGKIPV
VHPMTDKEVKISFNVTETKTGTVKNTGDLVFTVEGTKDTSKAKNAKPSVIPEIQEWFSES
DQKVAVDTLTEVTYSDDSLKAIVDEFVADYKNFTGKELKAGKSSEGKANAFNFKKAAPDA
LLGDEGYTMDIKSDRIDVQSVSVTGNMYGMQTILQMYKGSEGSGYSIGTMRDYPRYETRG
FLLDVARKPVSLEMMQEITRTMRYYKMNDFQAHLSDNYIWLGEYGKNGTEENAFDAYEAF
RLESGLTNEAGESPTAKDYSITKEQFKKFIADERAVGMNIVPEIDVPAHALSFTKVWPEL
KVSNGIHNSNPLIDHFDLTNEAAVAKIKEIFDDYTKGTTPTFDKDTVVHIGADEFMADPK
SYREFVNEIIPYVDQTNTVRMWGGLTQIKDNPPTEINKDAIDGVQINLWSKDWADGIDMY
NMGYDLINTIDDFGYLVPNGDYKRLNAYGDLLNIDRIFKDFEVNKVRTQNGAYKAVPSGD
DQMLGAAFALWSDNIDKKASGLSESDLYWRFFDAMPFYAEKTWAATGQEKGTSAALTSLA
EKMGTGPNTNPYYQENKKGDDYEKYEFADMKDSSENKRDLKEGKGAEVKDGVLNLGDEES
YVTTPIEQLGNGNVLSFDLELSKPSKPGDILFETDSAYGTHDIRVMENGKLGFTRELYDY
YFDYELPVGKKVNLKIVSTQQKTELFVDGVSAGTAVGKFVHNGQVKKDGITNATFALPLE
RIGSETNALAGKIDNVVVSVLNTEDKYNKKDWKITASSEYSANKENEGEVVKAFDGKSVT
KWHSEWQAGEGETNERLHDGAPSGQGTVDTVYAQAEFDKGYEIDKIAFTPRTDQPSGYVT
KADLYIQTEKDGEMKRVVTDAQFAADKTQKVFHFDKQTVYGFKFVAKASNDGWVAVSEFN
IGDEIAGLSKNTIFVNAEKGGKAEIVGAEAGKPFEADNGTKVTVKATPDKDYHFVGWYHS
SDAETPVSTEAEYEFTVSGNYALTAKFEKDNVTPPVETKDVTSIDKPEKVTVEEGTTFED
LQKDLPKTVTVHFGEGEKAETAEVEVTWEKGDYKGEADKTYTLSGTLGTLPENVTNTKGL
KAEIEVEVTKKEVTPPVETKDVTSIDKPEKVTVEEGTTFEDLQKDLPKTVTVHFGEGEKA
ETAEVEVTWEKGDYKGEADKTYTLSGTLGTLPENVTNTKGLKAEIKVEVTKKEVTPPAEK
EEYKITAKANDPKMGTVELKSADGKFTEGTEVTAIAKAKKGYEFVNWTVNGKEVSKDAVY
KFTAEKDMDLEANFQKVKGEDSNPDKDSNKGTSGDNKGTSGDNKGTSGDKAVQTGDKAGS
PVVPIAGLMLAAGAAVAALRKKED

Enzyme Prediction     

EC	3.2.1.52

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	592	945	5.9e-53	0.9703264094955489
CBM32	53	174	5.6e-16	0.8548387096774194

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	2.17e-116	597	944	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	8.26e-26	599	943	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.
pfam00728	Glyco_hydro_20	5.95e-23	596	915	1	321	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
pfam02838	Glyco_hydro_20b	1.10e-21	466	592	1	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
COG3525	Chb	1.93e-19	540	951	201	621	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTQ18922.1	0.0	40	1487	31	1451
ALE12005.1	0.0	40	1487	10	1430
ADO53681.1	0.0	40	1439	31	1405
ADP36558.1	0.0	40	1439	10	1384
BAI94822.1	0.0	40	1439	31	1405

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	2.64e-89	369	1144	2	720	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	3.76e-21	455	944	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	5.33e-16	539	774	72	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]
6YHH_A	8.85e-15	506	720	64	247	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
6Z14_JJJ	2.70e-14	540	731	254	456	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	4.52e-95	365	1161	20	756	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
Q9HGI3	1.40e-17	544	951	128	553	Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA PE=1 SV=1
B2UQG6	3.03e-15	539	774	91	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
P43077	6.68e-14	536	951	102	513	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
P49008	7.27e-14	477	778	44	339	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2

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
0.000490	0.998737	0.000200	0.000236	0.000170	0.000147

TMHMM  Annotations     

start	end
5	27