CAZyme Information: MGYG000000151_00848

Basic Information

• Species: Clostridium paraputrificum
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium paraputrificum
• CAZyme ID: MGYG000000151_00848
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1687		189693.9	4.3434

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000151	3486414	Isolate	United Kingdom	Europe

• Gene Location: Start: 252406; End: 257469 Strand: -

Full Sequence      

MKFKRIINSLLSAAMIVNLIPFNAMTVSAKTSPNVNLALNKNVIASAEYSTMPASNLTDE
DEGSRWSSESKPVQWAYVDLGQEEELNYFRMIWESNENYASSYNIYVSNDINNWGDPVAV
QAGNTTKISENLLEESVKGRYVKLEVTEQKGYPNVSCSDFKVMLKDSSMPDEQDPSENIA
LGKEVFVSDSETSSLSGDKAVDGDTTSKGSRWSATGKPAWIYVDLGKKQDIKTINLFWER
RNATKYEIQIADTLSNPMNDNDWKTVQSFTENPSRKDQKIILDKVYNARYVRLYINEYTA
DDPDGIVTWNSVSLYEMEVYGGDTKKSISDIVNSINIESPKKGDKKLDISNLPNEDGFIV
EYNGTDYEQVIGEDLTIYEPITDVTVNVSFKVTNEETKEYKFKECAIKVPGKYTNEEGEN
VSPVVIPELREWKGSKGNFTISNSSRIIVPSELKEMAETFAEDYKAMSGKTLKVVSGVTP
KAGDISFTLTKDQSKGLQDEGYLMDISDYITVEAETETGSIWATRTILQILKQNNNITIP
KGVTRDYPLYEVRGFILDVGRKTFTMDYLEQIVKEMSWYKLNDFQVHLNDNLIPLENYSS
AGKDPMEAYSAFRLESDIKEGGNNGLNKADLTSTDMFYTKNEFNEFIKTSRIYGVNIVPE
IDTPAHSLALTKVRPDLRHGTWGRDNDHLALKTKYDECLEFVKSIFDEYMMGEDPVFDDQ
TIIHVGADEYNADKESYRKFADDILEYVQDTGRTARIWGSLSQCRGTTPVRSEKVQMNLW
NFGYANMDEMYEQGFDLINCNDGNYYIVPNAGYYYDYLNDNTMYNLPINSIGGVTIPAGD
DQMIGGAFAVWNDMTDYLDNGVSEYDVYDRIGVAMPLFAAKLWGKNDLSLDEAKEKINEI
GEDPRVNFDYDVETKSENIAQYNMDDLKDSSSNGYNLASGSNAEIKEEDGKNVLELKGNE
SYVQSKLNTVGLNNDLRVKVKRTSNSKEEQILFESEYGSIKAVQKDTGKVGFSRENYDYS
FNYELPVNEWVELEFKNELNQISLYVNGNLVDTLGDGEKVEGRPLLATNMFPMQYIGSKT
KSFIGYVDDIRLAKNAEYASTMELDYAVWNASEYLKENKNHKLSALIKDSKKIFTKYNPT
SQEISEKANEINAILKDLDFEKADYSRVNAYLSLIPEDLSPYTEESVNVLLFVKNSIRGD
LPASLQSTVDGYEKLLASALNGLVAKPIKNVNYIDNSIIKATASSYQKDGSDPKNVLDDN
TGTMWHTDWNVTTMPHWIDLEMDEPTKVNGLTYVPRQSGLNGTITKYEIQVSDDGVNYTK
VKEGTLARNSEAKIIEFDAVTTKHVRLVALEAVNNNGTASEIKLYAVDVKADLEGLNKLI
AQASAIEDQGFTVDSWKTLQDKIVEAKALVDSEEPNANDVEIMKTELSVAMVSLILEDNT
VEVDKSQLEDLYNKVKSLEKDDYTEESWSLFIKALEKAKSVLNDDLATQEAINNAFNELT
DAYDKLVKTTPEEEISKDDLQAFLNKIEGLDTSKYTQASLKVFENAVKNAQLVLDNTNAS
KEEIEAAYNNLADALSKLEVKVDKTRLIKLYNKLIKLEKGNYTDGSWNNLKNALDSAKTV
IENKDATTEEVEKAIAELENAFNNLKQIEGQSVATGDNANIGLWFALLVISVAGACFVVL
KKENKIS

Enzyme Prediction     

No EC number prediction in MGYG000000151_00848.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	544	885	8.6e-59	0.9762611275964391
CBM32	1241	1356	5.2e-23	0.8790322580645161
CBM32	46	150	1.3e-20	0.8064516129032258
CBM32	190	317	2.1e-19	0.8951612903225806

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	2.75e-120	551	884	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	2.15e-28	553	884	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.
pfam02838	Glyco_hydro_20b	1.61e-27	423	546	2	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
pfam00728	Glyco_hydro_20	3.08e-27	550	872	1	336	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
pfam00754	F5_F8_type_C	4.44e-23	1240	1360	1	123	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCL58378.1	0.0	27	1585	27	1559
QWT17580.1	0.0	35	1419	39	1455
QPS14026.1	0.0	64	1585	81	1480
QQV05894.1	0.0	64	1585	81	1480
QMW75640.1	0.0	64	1585	81	1480

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	7.15e-123	331	1087	3	726	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	1.30e-27	423	891	34	489	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]
4A41_A	1.29e-22	1221	1366	12	161	CpGH89CBM32-5,from Clostridium perfringens, in complex with galactose [Clostridium perfringens],4A44_A CpGH89CBM32-5, from Clostridium perfringens, in complex with the Tn Antigen [Clostridium perfringens],4A45_A CpGH89CBM32-5, from Clostridium perfringens, in complex with GalNAc- beta-1,3-galactose [Clostridium perfringens],4AAX_A CpGH89CBM32-5, from Clostridium perfringens, in complex with N- acetylgalactosamine [Clostridium perfringens]
3GH4_A	1.51e-21	423	858	39	477	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]
2J7M_A	3.79e-21	1239	1365	11	148	Characterizationof a Family 32 CBM [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	5.61e-128	319	1087	17	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
Q8XL08	1.04e-17	1230	1365	620	766	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
Q0TR53	1.04e-17	1230	1365	620	766	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
P49008	3.85e-16	425	734	37	340	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q8J2T0	5.27e-14	491	885	114	519	Beta-hexosaminidase OS=Aspergillus oryzae OX=5062 GN=nagA 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
0.000260	0.999083	0.000183	0.000166	0.000148	0.000132

TMHMM  Annotations     

start	end
7	29
1661	1680