CAZyme Information: MGYG000004184_00701

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; QANG01
• CAZyme ID: MGYG000004184_00701
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2165		238132.72	4.5033

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004184	2370952	MAG	United Kingdom	Europe

• Gene Location: Start: 2194; End: 8691 Strand: -

Full Sequence      

MLHKRLKKRLSSCLAAVLAVTCMFSSIPVQAANTRAADNRVNLALGITYETNATDADYNE
AYPDFDHVKMTDGQMASSVWSGASVGFKNLKRGDPATDIPLTLTFDLGGEKDVNAVLFSG
WDSNNDGGIRNPVHYVIKYWADGAWQVLHEQSHGRVDPNGGHAYFEFGYTIPDNGSVKAS
KIMLEITNDPETLVAFLDEVQILAPAEQGGGSTGTPGNLAKGKSYEVTGTSDWISEDKNY
GDPTGRKLTDGVIHTDDSSFQTGDALVGYKVNDAEHQDFIVDLGEEKEVSGYAIHGWCIN
DYAWLIWNLRHYSVSYLDGNGDWQILVNTEDRLPRQDDTASCYTWKGDFDTPVTTSKIKF
SLQCWSTGLFLSELEVFGTQGGEPEEPDTYDNKALNRPYTKSEPYSENGSILYPDTGDSE
LTDGKVGGDSYGDAGWVGFAGQDNEKFVQVDLGKPYDIDKVEFSYCVDSGAGINPPSSTK
VTYSLDGVTFYDFVTFQNLSPASGAHTVSLKGEPVVARYVRYNFTKTGSWLFVSEVAAYG
TAASLDPKMPYLAQNLSAEKQLYFGNDADLTVSAIIGTPGTVTYEWTKDGNPLEETGATL
SLKNVQAADGGVYQVSVVNELNGEKYVAKSTPCTVSVTEVQDAKTLLDVFKTKTPVIEGG
KVVIEDSQSSLYKVVIGGSDRETIIDLDGNVYEPLFDTTVNLVYKAVSTTDETDFANADY
NVQVVVPGKYKKGTGDNKAPSTLPSIREWKGNTGKFEMTDSTAIIANTAVEKAVAQKMVT
FFKDVLKKDVSIKEGTPAKGDVQLKIDSSIPEMGAEGYYMDVTDTVVVRAPQQTGLLYGA
ITVVQSLYSDKEKTFIPKGIARDYPAYKVRGAFLDVARMAYPLDYLEEITKYMAWFKMND
FHLHLNDKADQDYKSFRLESDLKNLTSTDLYYGKEEYKEFQDMAADWGVNIISEIETPGH
ARAFRDVPGIKMTTDGEHLDLSDRQTVETIKGLFDEMLDGDDPVIRNPVVHIGTDEYYAG
TSEQLNEYVYELTQHLAAKGVNMRFWGAFLNNAGVPAGVSKTIPGSQCNIWASSGEWSDT
LSPTQMMEYGYDLINSNGYNLYMVPGGQEYSDSLNHAALFNNWDVNHFDLAGKQTNIMPL
GHPQVLGADFLIWNDRGTSNCGFSIFDVFTRFQNGTTIVAEKTWHGPKDEDQDYNDFAKR
DKMFKDIVGGANPTRKVNSETQTPVDIDFEDTNGNTAYDMSDNQLDATVTNGSFVEDNGS
TVLSFDGNGSMSLPVQSIGFPYEASFDLKVTKAPAANTKLFSSQDGTFYLNINGTGKMGF
KRDGFKVITPGKDVRFDWEGYTFLFDYKLPLNTWTKIKIKSDKQFTYLEVGGTTYKAQAT
VTKTPGKPNKPLDESSISMFSTEKMFEGMTCMVDNLVVKNPELKDNSERNPNLAFECDVT
TSPLEDGSMYGRNFYPGALTDGIKDDVNTRVSFDPSSATTWAIVDLGKVRDVNLIKLFFF
ESCPEYKISISEDGDHWTEVLHETNGVHGRPESVDVEVDIPFETQKARYVKYEGLQKWQS
QWGGYHGGLSEMEVYNMKADYDVIVKETTNGTVNVDKIYANEGDEVTVTVTPAEGYKLDS
LTVNGKAVAVEGGTYTFTMPAKNVTIAANFVSATKPTFSVTMDSMQNGTVTADKTTANEG
DKITLTVRPANGYQLKEIKANGETITPVEGVYSFVMPAKDVTVTAVFEKIPEVKYNINIA
ETTNGTVSSDKQTAAKGETVTLTVTPANGYLVKSVKVNGSTVEAVGGVYSFVMPAKDVNV
EAVFEKIPENQYKVTVLPSENGTVTADKQAAAEGETVTLTVKPASGYSIGFVKVNGEAIT
PVNDVYRFVMPGKDVEVTASFEQGETYKIIVEQLNGGVIVPEKTTAKAGETIHLTVVPDF
QYAVSFVWCNKQELVSKDGKYSFVMPAQDVRIYAYFIYMGGSGGSIGGGSSGGGSSKPSK
PVKPTEPTWEEVDGVWKLKGTDGEYLTGWQKVDSKWYYLGTDGVRATGWQKVDNKWYYLK
SDGVMATGWLKLGNTWYYLNAGGVMQTGWLYNGGVWYYLYSWGGMANTSWVQIGNTWYYF
RGNGAMFTGWLQQGTTWYYLKDSGAMATGWNWVGNKCYYFNASGKMAQNTTVGGYKLDAS
GAWVK

Enzyme Prediction     

No EC number prediction in MGYG000004184_00701.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	861	1186	1.7e-51	0.9762611275964391

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	3.00e-82	868	1184	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.
NF033838	PspC_subgroup_1	2.10e-63	1977	2164	474	683	pneumococcal surface protein PspC, choline-binding form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
NF033930	pneumo_PspA	2.28e-62	1977	2164	433	660	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
NF033840	PspC_relate_1	6.30e-44	1977	2165	501	648	PspC-related protein choline-binding protein 1. Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC.
COG5263	COG5263	1.05e-34	1989	2164	175	313	Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQV05909.1	3.04e-155	368	1575	470	1543
QMW75624.1	4.17e-150	218	1575	335	1549
QQY27139.1	4.17e-150	218	1575	335	1549
QPS14042.1	4.17e-150	218	1575	335	1549
QTY17007.1	1.19e-149	617	1551	17	942

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	2.51e-72	655	1372	11	678	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	3.62e-30	740	1184	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]
6YHH_A	3.58e-17	816	1184	92	476	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
3GH4_A	7.95e-15	731	1046	30	375	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]
7BWG_A	4.31e-14	740	1112	20	402	AGlycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5],7BWG_B A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	3.65e-75	641	1372	20	700	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
P43077	8.28e-17	802	1208	95	531	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
P96155	2.42e-14	741	963	140	373	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
Q7WUL4	1.93e-12	756	1200	21	462	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
B2UP57	4.07e-11	802	1055	44	335	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

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
0.000694	0.998079	0.000528	0.000262	0.000223	0.000182

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004184_00701.