CAZyme Information: MGYG000000287_02286

Basic Information

• Species: Robinsoniella sp900539655
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella sp900539655
• CAZyme ID: MGYG000000287_02286
• CAZy Family: GH136
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2433	MGYG000000287_29|CGC1	267312.93	4.9079

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000287	7249439	MAG	Sweden	Europe

• Gene Location: Start: 2162; End: 9463 Strand: -

Full Sequence      

MGKRLKLWKRILSIFLAVTLSLSSFIISAGAEEMSYKEIPENTAGETSAVNPNEKEQTLI
EEAENAQLNEPGDFSDDNDSASHGGKHIRTQNAGDIIVSPGDTDYYLDSGTSQNGDGSQE
SPFNTLFEINRREFAPGDHIFIKRGSVFKGQLYPKGSGSADKPILLDAYGEGEKPLIDGD
GRYGGQQEYGAEGPFGEAAAAVYLHNSQYWEISDLKVTNWDEDTANRERSGIRIEASGGG
IFRHIYIKNCEIFNVRGYRGQDSIWDVDPVGGGTTFFGSRTTHRTGGINFCSYTGRENNA
SDKTNPGKISDSEPTIFDDVLIEGNNIENCDANGITTTNVKGEMDNRDYRHKNVVIRGNS
ITNVQRAGIVPLYTDGALVEHNKVDTFQQTTEGYGCGIWCDRANDMVFQYNEVCNGQNTM
DGMAFNLDDMTENGVIQYNYTHNNVGGGTMLHVRTNSYNRNNTIRYNLSVNDTHNYAPHQ
AIVVCVGEDAKTKIESARVYNNTFFNTRTVRPVYKGDEIAFENNIFYLVNKGMKNKTDAY
DVGSKTIFNHNLFAGVHPQDEPSGNENISTAMPGLAGVLVEKDGDQYLPKGIEEAMAAAM
LAHASQALNAGIVMEDGVEEDLYGNPVTAGEAPNIGVYNGVSVEKTEYEDFSDITEVSGE
PSEFDDFTIEYVEGEDERVSKNAAFKTNPGGAHGGFHISSDEDGASAEYTFTGKAISVYT
KSGGAAGVANIYLDGQKAATDDQYEGRETFGRMAFTRTFAESGTHTIKIERSGMKNPSSS
GTNLNLDYFKVFKESQPVVPEKELIKMDASGFIAEAESVEEDEGPASCAIDGNSNTYWHS
NWSGTAAMQPDFEEGLRNGFTIDLGRNYNIQKLEYLPRQDQNNGTITKYRLFYSKTEDGE
FIPIPRGIGYWEGDSTLKSITFEKVNARKIQIRAYDAVSDSSGKNLITAAEFYVYRWKED
GGPVTPPDRSFHVPPAWNQGDTHITLPKVADGWEIELFGSDRKEVVGLDNSVTRPLEDVT
VNLLYKLTNRATGEVLETNVNAQITIPAAPMEDFVSGSNEKPGVIPALREWKGASGEIKL
TNTSRIVVDSESFRQDDAAHVKENLSKTDNFYTQVNMFKEDLKAQTGLDLPIVTDQEPGT
ADLYFTAQGAPASLGAEGYMIEFGGQNGDGGSVIVRAPQKTGILYGGITILQILKQNTAL
SLPRGICRDYPAYEKRGYMLDAARIYLPLEYLEDTLKQMAWYKMNTFSVHLNDCENWGNL
ELGQERYSAFRLESNVPGLTAEDGSYTKDEFREFQYDAVDLGINVIPEFDTPGHSLAFTR
VWPELAREDNAKYLDVTNPQVLEKVKALFDEYILPQDGKEEVFIGPEVNVGTDEYKTNGL
PESDRARYKEAFRGYIDQLLQHVKNRGKEPAFWGCLRENAGTTPVTTDALMYAWYWDYSE
ALKALEAGYRVLTMDEMETYIVPGGGWYVNQYGRGEHLYNTWLPNDNRAWDISFSGDRAP
APKGHPRVVGGQFAVWNDWIGNGISTGDISFRIQYNIPAIAQKSWSVDESNASMNYTEFK
RLGEIIGDAPGSDFLYRNNRFTEDKILDLGEEDDISNQADMQLHPVNVGSDAQGKDGAGI
RFNGEDSFIESDVDSTGFDWTVGMWINPDEGNAADAVLMEGKTGTLKLKQGKTGKIGYSV
GNYDHYFHYRLPEGRWTHIALTGDAYGVKLYANGIFIDELKDKPWPNLNFDSNFAKPSGQ
PNFIPTYFETLMLPTSVLGSKTNAFKGVADDFRIYNRVLEADEILEMTNMKGDASRALAA
QVNEANKLLDSGRLSEDPEAKAAMLNAVKAAANVLANPAFTEEQIKSAAQALQAEVEKAP
ADPADINLMADAYAATSVECHAGFGPEKMVDGDDALESRLATKRGVEEVPVEFILAGEKT
FNTLVIKEGLGPITGETLAAQIKGYEVQVAKNGKYEDLLSAVDQSAGIVGEKLTIDLGRD
VTASKIRVIFKVNPEAGINIKEAELYRLLKPQPYVNETARDVVNYLGIPERLELTDTHLP
ISEMPGAYSSRIIASGNSDIIGLDGTVVREDTDQTVAILMEVTKRKGTNTILEKAVMPYT
VVVAGLQTPAVMYRVTFHANGGTAVNPASIETESGKAIGSLPSTTREGYEFQGWFTAQTG
GTKVTEATVVTSDMTLYAQWKKMMQPQPQPQPKPEVSFTKTEYSLYATQTIKTSVNANAA
AGVVTGYKSSNTKVAVVTLAGVIKGIQKGSATITVYTSGKGTATVNVTVKTPKVTLTAKK
AKIQAGKSTKAITVKRKIKTDKVVKFTSSKKKIASVNHKGKIKGIKAGKTRITVFMKSGA
RASCVLTVQKAPVRTTKIKVPKKVTIKVKEKQKIEVVRKPVTAADKIDYRSSDSKIAKVD
KKGIITARKSGSCNITVTCNKITKRIRVIVERK

Enzyme Prediction     

No EC number prediction in MGYG000000287_02286.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH136	103	638	3.3e-102	0.9918533604887984
GH20	1208	1546	6.3e-59	0.9703264094955489

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.96e-87	1214	1545	1	324	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	8.58e-41	1213	1546	1	344	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	1.07e-35	1216	1546	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	1.28e-34	1213	1561	1	355	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.
COG3525	Chb	7.56e-29	1064	1556	136	624	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYE35145.1	4.65e-151	105	791	38	749
AZS13470.1	5.98e-148	829	1780	68	931
SYX85460.1	1.84e-147	829	1780	123	982
QDM43686.1	2.19e-145	829	1780	117	976
ASY51670.1	4.80e-145	830	1774	219	1093

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	3.64e-73	970	1577	6	576	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
7V6M_A	2.40e-37	103	644	9	581	ChainA, Fibronectin type III domain-containing protein [Tyzzerella nexilis]
7V6I_A	1.98e-30	103	636	14	605	ChainA, Lacto-N-biosidase [Bifidobacterium saguini DSM 23967]
5GQC_A	1.30e-29	103	636	18	593	Crystalstructure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_B Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_C Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_D Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_E Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_F Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_G Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_H Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQF_A Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, lacto-N-biose complex [Bifidobacterium longum subsp. longum],5GQF_B Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, lacto-N-biose complex [Bifidobacterium longum subsp. longum],5GQG_A Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, galacto-N-biose complex [Bifidobacterium longum subsp. longum],5GQG_B Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, galacto-N-biose complex [Bifidobacterium longum subsp. longum]
6KQT_A	4.13e-27	105	472	247	617	CrystalStructure of GH136 lacto-N-biosidase from Eubacterium ramulus - native protein [Eubacterium ramulus ATCC 29099]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	3.59e-77	970	1577	28	598	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
P96155	2.35e-22	1175	1461	221	528	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	3.03e-18	1119	1446	33	355	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
P49008	1.36e-15	1117	1546	72	504	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P06865	3.12e-15	1209	1546	163	486	Beta-hexosaminidase subunit alpha OS=Homo sapiens OX=9606 GN=HEXA PE=1 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
0.000517	0.998614	0.000337	0.000183	0.000165	0.000152

TMHMM  Annotations     

start	end
7	29