CAZyme Information: MGYG000001304_00690

Basic Information

• Species: Erysipelatoclostridium spiroforme
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium spiroforme
• CAZyme ID: MGYG000001304_00690
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1847		206018.01	4.1472

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001304	2507485	Isolate	not provided	North America

• Gene Location: Start: 280124; End: 285667 Strand: +

Full Sequence      

MKGKERIAKRAFKVLVAATMVVTSTQFGSFAVQAEVERQNFALNQEASANYEDSAHGFDA
EKAFDGNDELSSRWAAKEGERTGWLSVDLGRERTFDEFRILAEKDAQKIGKFTIEGSHDG
NVYETIFQSEDKTNDGGYDVDYTVKLNAPVTYRYVKITVESLVAGAYPSLSLREFEVLGD
KVAETPMNENLALNKAVTASAEYGSMPASNLTDADKDSRWSTEKNATQWAYVDLGQTYEM
NTFAMIWESASVYASDYNIYVSNDPNNWGEAVVSRNGNTSASSTEFLQAPVSGRYVKLEV
TKQYGYPSVSCRDFEVMLTDGQQLPQDPQENVALNKDATSSSNETSGLNASKAFDGDHTT
RDSRWASALGNGPHWISVDLGEVRNIKTVRLFWETRKATDYEIQVSSTGEEDSWQTVKHI
ESRPAIKTDRIVLDEVVRAQYVRLMVNDFTAQDPDGGVEWNNISLYEMEVYGGIIEDSAS
DIANQITIEEPQKGDTELVVNYPETDKYLVEYNGTDFEQVVDENLHIYQPIVDKVVKVSF
KITDKETNEYEFKEIGITIPGKYQQEETDNPAPVILPELAEWKGFEGNFTVLPTSRIVYS
NADLKAAAEAMAEDYELLTGKAISVVQGDQPQAGDFYFVQTTDTSKGLMEEGYIMEVDDV
ITVTSETKTGAYWATRTILQALKQSDYTTIAKGETRDYPLYEVRGFIMDVARKTFTLDYL
KQLVKEMSWYKMNDFQVHLNDNLIPLEYYSQNGMDPMDAYSAFRLESDIKKGGNNGLNQA
DLTSTDLFYTKDEFREFIKDSRELGVNIVPEIDTPAHSLALTKVRPDLRNGTYGRENDHL
NLVSKYNESLEFVQSIFSEYMTEENPVFDSQTTVHIGADEYNASSQAYRKFVNDMLDFVE
GTGRKARVWGSFTQASQGEDIDAEGVEINLWNFGYANMDQMYEDGFDLINCNDGNYYIVP
NAGYYYDYLSDSTMYNLDINTISGVTIPAGDDQMKGGAFAVWNDMTDYLDNGVSEYDVYD
RIERGLPLFAAKLWGKGDMNLEEAKATSDSLGDAPGTNFGYEVESKEDAILNMPMDEYED
TSANDHQIEQGVNAQIETVDFKNALRLNGGQSYISTDLETVGLGNDLRVKVKRTSDSTEE
QILFESPYGNIKAVQKDTGKVGFSRERFDFSFNYTLPVNEWVELEFKNQQNRISLYVNGE
LVDTLGDDERIEGRPMLATTMFPIQTIGSKTNAFIGYVDDLRLGKNDTFASTMALDYAIW
NGEAVLTNMANEQLRTVIDEAKSVLTEYAPSKATVDSYVSQINDLLSQMDYKKADYSRLN
AYLALTKDLSEFTDESVASVNQVIEGIRLNLPVQLQSTVDAYEKALVQALDNLELKDKTD
PNLVDSSKLTATASSYQQDGSNPSNVLDGSTSTMWHSAWNITTMPHYIDLEIDESTEIKG
LIYTPRQSGSNGNLLEYQIQVSDNGVDYETIATGTLENNAQAKTINFAPVTTKHVRLVYV
RAVNNNASASEISLIQAKVNPDIEGLQAIIDNAKSMSNVGYTDETWTAFQDVIKEAEALV
NLENPGANEVEAMKQTIASSIVALRLSEEELVVADKTALQIAVDLADKVTDKDLENVVPV
VAEEFKAALQEAKEILADETASQEDVNASFDRLASVMQKLEFYKGDKTALKAFIDDVSNL
DSTKYSTDTWAAFEKELNEAIAVYEDLNAMQEEVNNAHKELVTAFLNLRLIPDKSLLEEL
INKAEGLNSTNYTKATFDGLKDALNEAKAVFNDPNATQEQVNNAKDVLEKAINSLEVITT
VDNTPSTPVDNGDTTSVKTGDTTNLWYSLATLTLASVALYGSKKRKK

Enzyme Prediction     

No EC number prediction in MGYG000001304_00690.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	696	1035	3e-61	0.9703264094955489
CBM32	47	176	1.6e-23	0.9516129032258065
CBM32	336	468	4.2e-22	0.9435483870967742
CBM32	197	303	2.3e-21	0.8629032258064516
CBM32	1391	1512	7.3e-20	0.9274193548387096

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.47e-118	702	1035	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	3.76e-35	704	1035	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	7.69e-30	701	1022	1	334	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.
pfam00728	Glyco_hydro_20	8.28e-28	701	1022	1	335	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
pfam02838	Glyco_hydro_20b	8.70e-25	572	697	1	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCL58378.1	0.0	155	1804	1	1565
QWT17580.1	0.0	190	1561	40	1454
QPS14026.1	5.23e-291	218	1751	81	1502
QQV05894.1	5.23e-291	218	1751	81	1502
QMW75640.1	5.23e-291	218	1751	81	1502

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	7.37e-105	482	1229	3	720	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
3GH4_A	1.81e-24	573	909	39	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]
4H04_A	6.95e-21	573	1052	34	494	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]
2J7M_A	3.78e-18	1379	1520	6	146	Characterizationof a Family 32 CBM [Clostridium perfringens]
2J1A_A	3.88e-18	1379	1520	7	147	Structureof CBM32 from Clostridium perfringens beta-N- acetylhexosaminidase GH84C in complex with galactose [Clostridium perfringens ATCC 13124],2J1E_A High Resolution Crystal Structure of CBM32 from a N-acetyl-beta- hexosaminidase in complex with lacNAc [Clostridium perfringens ATCC 13124]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	2.34e-109	474	1229	17	742	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
P49008	5.67e-16	575	880	37	335	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q0TR53	9.01e-16	1255	1520	532	764	O-GlcNAcase NagJ OS=Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) OX=195103 GN=nagJ PE=1 SV=1
Q8XL08	9.01e-16	1255	1520	532	764	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
B2UQG6	1.08e-12	641	880	89	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

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
0.000756	0.998226	0.000283	0.000260	0.000232	0.000194

TMHMM  Annotations     

start	end
12	34