CAZyme Information: MGYG000000244_01120

Basic Information

• Species: Catenibacterium sp000437715
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Catenibacterium; Catenibacterium sp000437715
• CAZyme ID: MGYG000000244_01120
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1202		134743.79	4.8266

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000244	2463343	Isolate	China	Asia

• Gene Location: Start: 32408; End: 36016 Strand: +

Full Sequence      

MPASYLIGNNKMNKNNMKRVLMSVMLVSSMTLSSGAIVAKAYNGTSAITERTMTNEQLVA
ATTPILQSYTKDASDKTWVMTKDSKFVIVASEANLKNERLAEIVKLVNSEFMAKQIVSSD
AQAMLYNQDGAPTDITIDIKPVSEITDKTTSKEAYKITIDDTGIHLTGASETAVLYGLRT
IEQLAIANNNNLAYGEIVDYPNVAERRIHVDMARKYISKEWFIRQIREMSYFKMNAIQMH
FSENLGFRIECETDPSIVSEQHLTKADVREILAEAKKYGVKVIPSFDSPGHVDQILRAHP
EYGQVDAYGNNYKSGLDVTNPEAIKYIYSLYDEYMELFEGCTDFHIGGDEYMEFDRAPFT
TQYKSVLDNYARENIDPNATWKDVIAKYINDLAEHVHEKGFTPRIWNDGIYYGENSYYGK
KQMIQMHKYIGIDFWSQMSWNSSIAKLQTFLDKGHDTVYNVNASFFYYVLRPSMPNDGRK
QHSFDNLNSDKLIFDQWTPGKFQANTIADDNPAIKGASLAIWCDKADVCDEDTITEDISN
EMRALATKAWNTKSNSIISHDQFKSNYAKLGHVAAFDKGSTLPDSGSILPADSLGKVTIK
YVDQDGKDIKSPVTRYGNVGDEYNFTAEKIYGYRLVSDKDSATGTYSKKGDTFTFTYEIY
TDKTDLKAALDNALDENDYIGATFGEYKAALDEAQKLYDDKKALQQDVDAILIQLNNAKK
KAIKRAYYPLWVEVENPMADNGYASGYAEYLEAVKNGKKVLYGEEVTDEAVKTAYDELVA
ARNGLMKRDGNVPSVQASDGYWSLGVSPSDKYSYDKMLDGNRDTFAWFNDAQKVGKHITF
TFANKVNMSGIKISAPERPGSDIIKNADIMVSEDKENWTTVGNLKMDANTLEQTFTFDKQ
PVKYVKLEMKEASDSWYKIAEVQFIYEQVAENTELKDLLKEAYGQDLTDKTTESVDAFLE
ALIEAQKAYAKEDLNNEEVMNALRTAMQNLKVVSKVNKAELKGTVTKAEAIPEETLNKAV
KKARDAFVKALEDAKAVVEKKDASQEKVNEAAKKLEDAIKGLDVHKGDTTTLDAKLAEIE
ELDEKKYTADSWAKLMAVVEEAKGLDAENATQKDVDEVVAKLTKAVEALEEKVVIEPEKP
ETKPEIKPETKPEVKPEVKPTTKPEDKKDDTVKTGDPTSLFGLVSAMALSLAGYVSVKKK
KD

Enzyme Prediction     

No EC number prediction in MGYG000000244_01120.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	204	552	2e-64	0.9554896142433235

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	3.73e-64	205	550	2	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.
pfam00728	Glyco_hydro_20	6.50e-37	206	550	4	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	6.67e-32	153	524	206	589	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd02742	GH20_hexosaminidase	6.75e-32	206	550	2	302	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.
cd06570	GH20_chitobiase-like_1	3.49e-25	206	350	4	157	A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase 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 subgroup 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCL57158.1	0.0	11	1139	4	1133
ASK64148.1	3.01e-225	53	593	29	577
APC47599.1	8.83e-224	55	597	31	581
AYV34923.1	2.27e-191	64	585	43	564
BCL57159.1	5.48e-179	11	1200	4	1144

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4H04_A	2.74e-42	33	572	11	495	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]
6JQF_A	1.00e-25	130	552	142	548	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
2YL5_A	8.54e-22	263	570	92	364	Inhibitionof the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis [Streptococcus pneumoniae TIGR4],2YL5_B Inhibition of the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis [Streptococcus pneumoniae TIGR4],2YL5_C Inhibition of the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis [Streptococcus pneumoniae TIGR4],2YL5_D Inhibition of the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis [Streptococcus pneumoniae TIGR4],4AZC_B Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZC_C Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZC_D Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
4AZC_A	8.54e-22	263	570	92	364	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
4AZG_A	8.63e-22	263	570	93	365	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZG_B Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZH_A Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZH_B Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZH_C Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZH_D Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	1.30e-27	130	552	164	570	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
P13723	1.32e-21	153	559	101	477	Beta-hexosaminidase subunit A1 OS=Dictyostelium discoideum OX=44689 GN=hexa1 PE=1 SV=1
B2UP57	7.38e-21	149	422	54	347	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
Q54SC9	1.35e-20	153	473	109	410	Beta-hexosaminidase subunit A2 OS=Dictyostelium discoideum OX=44689 GN=hexa2 PE=3 SV=1
P49610	3.31e-20	263	570	714	986	Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 SV=2

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
0.004686	0.992723	0.001466	0.000655	0.000241	0.000190

TMHMM  Annotations     

start	end
20	39