CAZyme Information: MGYG000003147_00301

Basic Information

• Species: Robinsoniella sp900555455
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella sp900555455
• CAZyme ID: MGYG000003147_00301
• CAZy Family: GH136
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2414	MGYG000003147_1|CGC9	263629.78	4.9837

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003147	4940098	MAG	United States	North America

• Gene Location: Start: 370606; End: 377850 Strand: -

Full Sequence      

MQYAKGMKMGKEQKLWKRLLSIVLAVTLSLSSFTIPVSAEGTSNDTRAKDTTNEASVEGT
TNIASAEVIAGEAREEGITGEPSENNPNAREQSYIVEAENAQLKEPGDFSDDNDTASHGG
KHIRTQKIGASVTLTFTGTGIRFYTKKGSGAGVLQVEIDGGLHGKADEYVNGSPQFQSKT
YEALNLSEDNAEHKIVLTTTSENPNDINGSPWFNFDYFEVIQSEGGGAGDIMQSPGDTNY
YLDSQASQNGDGSQESPFNTLDEINRREFAPGDHIFIRRGSVFSGLLYPKGSGSEEKPIL
LEAYGEGEKPLIDGGGRYARQQEYGAEGPFGEDAAAVYLYNSQYWEISDLRVTNWDEDAA
NRERSGIRVEAGGGGVFRHIYIKNCEIFDVRGYRGQDSIWDVDPVGGGTTFFGSRTTHRT
GGINFCSYTSRENNASDKTNPGTVTDNEPTIFEDILIEGNNIENCDANGITTTNVKGEMD
NRDYRHKNVVIRSNSIKNVQRAGIVPLYTDGALVEHNKVDTFQQTTEGYGCGIWCDRAND
MIFQYNEVCNGQNTMDGMAFNLDDMTENGVIQYNYTHNNVGGGTMLHVRTNSYNRNNTIR
YNLSVNDTHHYAPHQAIIVCVGEDANTKIEAAKVYNNTFFNTRTVRPVYKGDEIAFQNNI
FYMVNKGMKNKTDAYDVGYNTTFNKNLFAGVHPKDEPAGNGNLTAAMPGLSGVLVNKDGD
QYLPKEMEEAIAAARLAHNSEALNAGVAIEDGAAVDLYGNPVIAGEAPNIGAYNGESVEK
TEYEDFTDITEAPGEPSDIENYTIEFVEGEDERVSKSAAFKTNPSGAHGGFHISSDEDGA
AAEYTFTGKAISVYTKSGAAAGVANIYLDGHRVATDDQYEGTETFGRMAFTRTFTESGTH
TIKIERSGMKNPSSSGTNVNLDYFKVFKESQSVVPDRSFHVPPTWNQKDSHITLPEVAEG
WKIELFGSDRKEVIGLDKSVTRPLEDVTVNLLYKLTNQATGEVLETNVNAQITITAAPME
DFASGSNGKPDVIPALREWKGASGQITLSNGSRIIVDAENYRENDAVHVKANLSKTDNFY
NQVNMFKADLKAQTGLDLPIVTDQEAGIVTGQEPVGEDIYFTTQSAPESLGAEGYVIEFG
GQNGDGNCVIVRAPHKTGILYGGITILQILKQNAALTLPKGMIRDYPAYEKRGYMLDAAR
IYLPLEYLEDTLKQMAWYKMNTFSVHLNDCENWGNLALGQERYSAFRLESNVPGLTAEDG
FYTKDEFREFQYDAVDLGINVIPEFDTPGHSLAFTRVWPELAREDNAKYLDVTKPQALEK
VKALFDEYILPQGGEEEVFIGPEVNVGTDEYKTNGLPEADRTRYKEAFRGYIDQILKHVK
NRGKEPAFWGCLRENAGTTPVTTDALMYAWYWDYSEALKALDAGYRVLTMDEMETYIVPG
GGWYVNQYGRGEHLYNTWLPNDNRAWDVSFAGDRAPAPKGHPRVVGGQFAVWNDWIGNGI
SSGDISFRIQYNIPAIAQKSWSVDESNGSMSYAEFKQLGEIIGDAPGSDFLYRNNKFTED
KILDLGETGDMASQANMELQPVNIDSSAQGKDGSGIRFNGKDSYMESNVESTGFDWTAGM
WINPDEGNAADTVLMEGKTGTLKLKQGMTGKIGYTVGKYDHYFNYRLPEGRWSHIALTGD
AYGVKLYVNGIFIDELKDKPWPNLNFDSNFAKPSGQPDFIPAYYQTLMLPTAVLGSKTNA
FAGVADDIRIYNRVLGADEILEMANVSGDAQGALAAIVNEANALLDSGRLSEDPEAKAAM
LNAVKAAVNALGNPDFTEEQVRSAAQALQAEVKKAPADPAAINLMTGAAAETQVECHPGF
GPEKMLDGDDALDSRLATKRGVEEVPIEISLTGEKTFNTLVIKEGLGPITGETLTAQIKG
YEIQAFKNGAYESLMSARDEASGIVGEKLTIDLGQDVTASKVRVIFKVNPTAGINIKEAE
LYRLAKPQPYVNETARDVVSYLGIPERLELTDTHLPVSEMPGAYSPRIIASSDPDIIALD
GTVAREDADQTLTVLMEVTKRKGTNTILEKAVMPYTVVVAGIKIPAVTCQVTFHGNGGAV
PNPASKEVLAGEAIGNLPETTREGYEFLGWFTAQTGGTKVTEETVVNSSMDLYARWREIT
VQQPQQPQKPQQPHPEVSFAKKEYSLYATQTVKTSVNANVAAGAVTGYQSSNTRVAVVTS
GGVIKGIKKGTATITVSTSGKGTASVKVTVKTPKVTLTVKNAKLQEGKTTKAITVSRKIK
TDKIVKFTSSKKKIASVNRKGRIKGIKAGKTKITVFMKSGAKASCILTVQKAPVKTTKIR
VPKKIILKVNKKQKIDVVRKPVTSADKIDFRSSNSKIAKVGKKGVITAKKAGSCNINVTC
NKISKKIRVIVERK

Enzyme Prediction     

No EC number prediction in MGYG000003147_00301.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH136	238	773	3.3e-101	0.9918533604887984
GH20	1185	1522	3.8e-59	0.9673590504451038

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.25e-87	1190	1521	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	1.32e-39	1189	1522	1	344	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	1.93e-37	1192	1522	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.
COG3525	Chb	8.02e-34	1028	1533	128	625	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06563	GH20_chitobiase-like	1.54e-33	1189	1522	1	343	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
AYE35145.1	2.68e-150	231	862	29	682
AZS13470.1	1.90e-149	924	1755	173	930
SYX85460.1	1.09e-148	904	1767	206	990
QQA10987.1	2.73e-144	943	1775	349	1115
QDM43686.1	4.39e-144	956	1753	256	973

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	7.95e-67	938	1553	6	576	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
7V6M_A	2.58e-29	236	779	8	581	ChainA, Fibronectin type III domain-containing protein [Tyzzerella nexilis]
4H04_A	3.01e-29	1029	1494	33	448	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]
3GH4_A	1.07e-26	1021	1537	30	503	Crystalstructure of beta-hexosaminidase from Paenibacillus sp. TS12 [Paenibacillus sp.],3GH5_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GlcNAc [Paenibacillus sp.],3GH7_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GalNAc [Paenibacillus sp.],3SUR_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NAG-thiazoline. [Paenibacillus sp. TS12],3SUS_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-NAG-thiazoline [Paenibacillus sp. TS12],3SUT_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc [Paenibacillus sp. TS12],3SUU_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-PUGNAc [Paenibacillus sp. TS12],3SUV_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-DNJ [Paenibacillus sp. TS12],3SUW_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-CAS [Paenibacillus sp. TS12]
3RCN_A	1.23e-24	1090	1437	49	408	CrystalStructure of Beta-N-Acetylhexosaminidase from Arthrobacter aurescens [Paenarthrobacter aurescens TC1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	1.08e-70	938	1553	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	1.33e-22	1151	1437	221	528	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
P49008	7.27e-20	1103	1522	82	504	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UP57	7.25e-19	1156	1422	76	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
Q641X3	1.59e-18	1112	1541	87	502	Beta-hexosaminidase subunit alpha OS=Rattus norvegicus OX=10116 GN=Hexa PE=2 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
0.001039	0.997743	0.000402	0.000287	0.000262	0.000221

TMHMM  Annotations     

start	end
20	39