CAZyme Information: MGYG000001328_02935

Basic Information

• Species: Clostridium tertium
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium tertium
• CAZyme ID: MGYG000001328_02935
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1616	MGYG000001328_3|CGC44	179827.43	4.4209

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001328	3807822	Isolate	not provided	not provided

• Gene Location: Start: 2774624; End: 2779474 Strand: -

Full Sequence      

MRNKRYNISKRILPLFIAFTMMFSFVPVRAEENTTEVKRENLALGKSATASGYEGGSTFT
ADKVIDGKVDRPADINKAGSSRWASNLNAVNPWITIDLNEVKAFDEVVIEWERRNVNSYK
VEVSNDNITWANIHKSTTKNELREVLDVGSQKARYVKITIENYSSTQEGSNIIWNTVAMY
EVEIYNNKPEEPEVPEVPEVIVPAAGENVALSKNATSSSNETNTLTPDKAVDGLKSKASR
WASAVSSNPQWITVDLGAKTQIENLVIEWERKNATEYRVQVSDNNENWTDIYAAKSAPTK
NRQEINLDKAIATRYVRVYVDKHIADADGVNWNNVSIYEIEIYNGGIPKGFDEITNSINV
RELTIDDEVLPMPEVQDGYEISFVGADYEEVIGSDMKINRPLVDTKVRVNFEVKQGDKKA
YTPDIEVLVPGAHEATGNNAPTVIPELREWLGGSGNFEINNGSRIVIAPSSEAELIESMN
VFAEDYKDVVGREIEVVVSDSPKNGDFYFELNNKRPELRTEGYYMEIGDFVKVESNEAEA
AFLSTRTILQILKQNGTTIPQGITRDYPLSDVRGFMLDVGRKPITLDFLYDTVKLMSWYK
MNDFQVHLNDNYIFLEDYSKNGEDPMDAYAGFRLESDIKEGGNNGLNKADLTSKDTFYTK
DEFRTFIKDSREIGVNIVPEFDTPAHSLSFTKVRPDLKMGNVGRQADHLDVTNPGSLEFV
KGLWDEYLDGENPVFDSETIVNVGTDEYDAKYTEEFRKFTDDLLGYMQDEKDRTVRLWGS
LSARPGNTPVRSENVQMNIWNNGWSDPSDMFKAGYDLINTEDGKLYIVPDAGYYYDYLNS
SYIYNNYEVSKFGNGDVIPAGSPQMIGGTFAVWNDMVDKKANGIVELDIYDRILPAVQAI
SEKMWGLAEDKTYAEFQEVAAKVSNAPNSNPRYKVESKTEKVLDYNFKGASKGIVPDNSG
NGYNSVALNNSTIKNGVLKLNGSNSYLENSIENIGPNYTVSLSVKRDENSNNEEQVLFES
EKGSFKAVQKETGKVGFSREFYDYSFDYELPKGEWVDISIVGRMTKTELYVNGEYVDEVS
KTSEARHNGTFVFPLEKVGSETKAFNGEIKSLKVYNVANNVADETVIPQETMKASATSEH
PNVGSEGLASFAIDGKPGTIWHTNYDTPVQLPQSITLDLGKAYTINKFSYLPRSNGGNGT
ITKYELQVSTNGTDFTTVSDGSWAKDATLKVVNFDEVPNVTHVRLVAKEGAGGFATAAEL
NVHKVKEVTPEPKPEVDKTALKTTIDYANEVVAEGLLNGVVPVVVKDFNAALEEAKAIYE
NEDSTEEEVDEVFKRLVNVIWMLEYKQGNKEALKALVDSAKGLVEKVYTADSWAVLQVAI
EAADAVLADENAMQEEIDEILDSLKSAVDGLVKIEVKKEALENLVNKLEKLDKKVYTEST
WTPFENALKTAKEVLANTDAIQEEVDSAYNTLLKSSLDLRLIPDKSKLEDLINKAKAVDL
SKYTEKSANELKIQLARASEVFANEEATQEEINKATRSLDTALNDLIAKGDENGGSENNG
NGNGSGTETPSDSNKTPDNGGKLPATGVESGPWTMVAFISIIIGSALIYRKRYNRI

Enzyme Prediction     

No EC number prediction in MGYG000001328_02935.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	571	905	2.3e-57	0.9495548961424333
CBM32	213	340	3.1e-26	0.9435483870967742
CBM32	1134	1259	1.1e-23	0.9435483870967742
CBM32	47	168	1.4e-20	0.8870967741935484

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	3.80e-132	572	906	2	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.
pfam00728	Glyco_hydro_20	1.44e-31	573	905	4	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	3.10e-29	573	906	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	4.64e-27	573	916	4	353	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.
pfam00754	F5_F8_type_C	1.04e-21	214	340	1	127	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
AYE33718.1	0.0	10	1551	11	1675
QAS61873.1	0.0	10	1551	11	1675
ATD55826.1	0.0	10	1551	11	1674
SLK21750.1	0.0	10	1551	11	1674
QBJ76126.1	0.0	10	1551	11	1674

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	3.19e-134	353	1112	2	734	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4A41_A	1.00e-48	1125	1262	23	159	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]
2V72_A	5.44e-30	1124	1264	8	143	Thestructure of the family 32 CBM from C. perfringens NanJ in complex with galactose [Clostridium perfringens]
4H04_A	6.30e-26	441	923	34	490	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	3.48e-23	1131	1263	10	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	3.89e-140	353	1114	24	753	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
P0DTR4	2.40e-25	1125	1272	507	653	A type blood N-acetyl-alpha-D-galactosamine deacetylase OS=Flavonifractor plautii OX=292800 PE=1 SV=1
Q8XL08	6.40e-21	1123	1267	620	771	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
Q0TR53	6.40e-21	1123	1267	620	771	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
E8MGH9	4.37e-16	1137	1475	1520	1871	Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 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
0.000314	0.998861	0.000291	0.000171	0.000169	0.000146

TMHMM  Annotations     

start	end
12	29
1590	1609