CAZyme Information: MGYG000001709_01884

Basic Information

• Species: Collinsella stercoris
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella stercoris
• CAZyme ID: MGYG000001709_01884
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1631		177133.47	4.3652

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001709	2399821	Isolate	Japan	Asia

• Gene Location: Start: 11600; End: 16495 Strand: +

Full Sequence      

MRKHRWKGGLVASGLAALCAAAMVLPAQPVFAAEENLALNKPVTTSAEHQNLPASRLTDG
NKDPKKGRWSAEQGPTQWAYVDLGASQEMNYFELTWESNTEYATDFNIYVSDSKDDWGEP
DKAVKGNTSGVSTIKLDAPVTGQYVKLEVTKVSAYPNVSCSELEIRNIAGEAPEKPAEAT
NLALKKPTKASKDYHNENGARAVDGKKKNSKADRWMTETKPSVDKPMWVYVDLGKSETVN
HFELYWESAANYATDFNLYVSDSTTEWGEPVKAVKGNNQGQTSVTLETPAKGRYAKLEIT
AETSGWGASCMEFEVWNEVPPAPEKQPADYLNDIVVKPVTAESTELEYTLPTDLPAGYKI
KYNGTDYEQVIGLDGKIYRPISDVTVKASFKIENEKDKSDYAFKEFDVTVPGSMTAGTNP
APQVLPELREWVGGEGQFAASAAKRVVYGSESLKAMAEDFAADFQAITGVKLSVASGSSA
AAGDIFFTLGADAAKGLGDEGYLLDAKADRITVSAEEVAGANWGGKTILQGMKTGANNFP
VGMSRDYPLYKVRGLILDVGRKTFTLDWLKQMTKQLSFYKMNDFQIHLNDNFIGLENLED
PMKAYSGFRLESNVKKGGNGGKNQADLTSTDVWYSKADFKEFIEHSKDLGVNIIPEIDTP
AHSLALTKVRPDLRTGTSGRQNDHLDLKNQYNESIGFVQDIFNEYLDANNDGATAADDVF
ADADVIHIGADEYSADANAFRRFNNDMFKYVEDHGKIARVWGSLTSIAGDGSVKVPGVNE
DGQRRQINLWNFGYANMDKMYEDGFELIDCNDGDFYIVPNAGYYYDYLSYDHCYNDPLNA
VGRVSIPAGDPQIAGGAFAVWNDMCYVSENGMSEYDIYDRIDGALGAYAANSWGKGALSA
ADSQALYAKIGDAPNTNFGYEAAADENGMYAQWNMEGTLADSSDMNRDLENGKNAELAKV
DGKQALKLNGGESYVSVKDDALTTLGLGNDLRVKVKRTSASTDEQVLFESEYGTIKAVQK
GTGKVGITRENRDYSFNYTLPVNEWVELEFKNEFEVTTLYVNGEKIETIGATGEGSRNKL
KATCMFPVNKIGSTENAFEGYVDDVRISTAKEFASTMELDYAVLTAESVLAAQDVPGLRE
LLDQAYALFLNPNPAQADIDGLVTKIEALLTGEDGKPSYEMADYCRLDAYAQLQLDGDAA
ALLNGLFTEESVAGVQAAWAQVREDLPKSMQSTVDAYENAIVNALNDLELRTGGDLNFVD
PASLKAVASSEQGGAEVAAKVLDGNVGTMWHSKYSENKLPISITLSSETPMSVDGFVYTP
RQSGANGNMQAYDIEVSQDGKTFTKVASGTVKLDGVNPVSLKFDRQDNVKAVKIVWTKSV
GNFASAAELRLMDAAAAPDFAGLQTLVDAAKAIKQDGSCKHDAFTDATWDALQAKVAEAE
KVIADKSGDVNSVFALMGELGKSIVSLRLDAKVVDPGADEFTVTVDDRIPGHEDLVIVVK
KGDKVPVLPMPEFAGYLFDGWYTDGVDGTWKNEWDFDAPVTSDLVLSAKWVENRDAPVDP
GVDTPEPPVDPEKPTDPEKPVNPGKPNADNPNPGVGLPQTGDSSMLLIGGIAAAAVVLLV
VGVIMRRRNSR

Enzyme Prediction     

No EC number prediction in MGYG000001709_01884.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	543	881	2.1e-54	0.9495548961424333
CBM32	44	163	1.6e-20	0.9193548387096774
CBM32	189	314	3.7e-20	0.9274193548387096
CBM32	1268	1389	1.1e-18	0.9112903225806451

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.54e-108	551	894	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	3.77e-34	553	894	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	7.38e-26	550	881	1	335	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	1.74e-22	553	761	4	224	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	1.97e-21	496	762	202	487	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCL58378.1	0.0	24	1469	21	1421
QWT17580.1	0.0	19	1556	23	1581
QPS14026.1	1.37e-195	36	1134	44	1135
QQV05894.1	1.37e-195	36	1134	44	1135
QMW75640.1	1.37e-195	36	1134	44	1135

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	3.18e-100	325	1102	1	726	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	1.57e-26	406	879	23	464	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	1.45e-21	410	769	28	383	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]
6YXZ_JJJ	7.04e-20	149	678	18	454	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]
6Z14_JJJ	7.04e-20	149	678	18	454	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	6.00e-102	325	1102	23	748	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	2.93e-14	499	839	128	468	Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA PE=1 SV=1
Q7WUL4	2.59e-13	498	780	80	330	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
B2UQG6	2.14e-12	484	732	85	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
P0DTR4	8.88e-12	1246	1391	495	643	A type blood N-acetyl-alpha-D-galactosamine deacetylase OS=Flavonifractor plautii OX=292800 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
0.000391	0.998761	0.000203	0.000267	0.000189	0.000156

TMHMM  Annotations     

start	end
9	31
1603	1625