CAZyme Information: MGYG000002340_02980

Basic Information

• Species: Intestinimonas butyriciproducens
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Intestinimonas; Intestinimonas butyriciproducens
• CAZyme ID: MGYG000002340_02980
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1715	MGYG000002340_1|CGC18	182449.45	3.9805

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002340	3376471	Isolate	not provided	not provided

• Gene Location: Start: 3110203; End: 3115350 Strand: +

Full Sequence      

MRTGMQKGSSRLVAMLLCLVMLFGMLPMSALADEGTGTPPVQTETPVSTPEAAPEGSPAS
TAEVSPEISPTPAPEASPEVSPTPTPTPSTEVPMDEVLDELETVETPPAAVSSVENGFGH
KILHLDCGRKYFTKEWVIALIHEMTAAGYNELELDFSNNEGFRFALDDMFVTFMTESGEE
KTIDLTPALGGDTDGSDTKSPWLTQADMDEILSVARGEDVAIVPLLNSPGHLGRILDTVA
PEYRYQNSNSLDITSDDAKAFGIALVQKYAAYFADEGCEYFNMGCDEFANDLYSSGGMGF
GHLVSAGRYGDFADYVNSLAGVLKSLDLTPRAFNDGIYYNNDTSVSFDQDIQVCYWSSGW
NGYAVASAATIVEEGHAVINTNGDYYYVLGKSDKFDGDKTGSGADSFRNYTFMGTTFDED
ESLVIGSMFCIWCDYPAAESETEIAANVRQALRVMGGRMDKKSGASVTSATVSNEAVPGG
FNADGTIYAVLAYTYELGELTVGAPTVNAGGSLTLTWSEPLITATGDVAALALPAVTYTV
SRDGTVLGATDATTYTVENARAGAYTVSAALDGDAAAPVSSAVTVTQEQLDAAAIQNGTI
TGGGTADAYELSDVSNGGQYLIVYQSDSTSGYALKNDGSAVPVTIADGRVVSEVTEDMLW
TYTEESSFIWTNYYLSSGGKYLYPSRDGIITSSQSSITLSGQNSTGTYTISGSYSRYLQY
NRGNFSAARNSSSTLYFYEYTAGTEAWHVDTEALDAKLAALAAEGLQADDYTSASWSAYT
AALDAAQNLTPNTTAYPSAETAQAAQDAIDAALSALNTAYAGLVRVERVTITIHCVDGSG
NRVAADTTVRLEKGVSQTITAPAIANYTATGTTSVTQTWTADSEVTFTYLLTPTGDPLTI
EYWITNVVVTGSNGVTSKEITVAEAYGAEGVEVAPTYAPTTGTSSTFGDMVYWKSVRLDS
AHKQTSDSGDDETASGTDLTKVRYYNDSWQYYTTSDEWKSFAEGDQLVAYYLQKTEVTQE
ITTLTKDWGYGIPSEDTSGQNGQVALSFAVVYPDGSLSPATESLIYANCTTIFNYWSNRD
IGIIAPQSNADYDIEKITVTRGSRHSNTSSNTWGASDSIDWNKVTDSEGTQWYDETTAWD
DSMETSPAVYGSDGYVWSRKNTAFLILIYLKPRVTDTSLTVRYVDDTDTSEIYSYPVAVT
NGITFLNGLKNTGTVQSGTITLDDGAYITNSSGVDQTFNKNLATIPNLAGKYASGYYQYV
SADVSEDGKTLTLHYQPSAEVLTFVVDFGLPLNITPNDLGLENADAVTGLTCNTSKGTYG
IFSSSGTTVTYTPNETIDGAESVVLTIHYSGSTVTKQIRVLPASVVYYEDSFATYDSSWS
GTGTLAGTAQTAEKLGAKQNLYGYDPAYTSGTGFSMGSAHTVTVNAANDSATASFSFKGT
GFDLISRTDSDSGVIFIEAMGTRGTTKRLIVDNYYGYDFVNGAFVTADKGSIEQVPVARM
AGLPYDTYDVTVTMVYHQKLNHAGDSSYSFWLDGIRVYDPMGSSYSAYASDSEAAPQYVE
LRKSLLNAAALTSGAVVQGTTFIDGKGETAVLADYESYGPNNEVYLSKGQSITFTLGSVD
FADIQLGASLTGSAASTITVNGTTIQLDSATNLYYSIKNAIGADKVVTITNTGDGMVALT
NLKATGGTATLNLYSSQAAVGKVLAAMQMPGTGNQ

Enzyme Prediction     

No EC number prediction in MGYG000002340_02980.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	111	443	3.9e-45	0.9287833827893175

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	4.87e-65	120	456	2	320	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	1.90e-22	125	435	6	279	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.
COG3525	Chb	3.45e-18	118	449	261	604	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam00728	Glyco_hydro_20	6.08e-13	118	435	1	320	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06569	GH20_Sm-chitobiase-like	2.73e-11	118	387	5	315	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. 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
ALP95510.1	0.0	1	1715	1	1715
QBB67228.1	0.0	1	1715	1	1718
QMI85631.1	3.03e-62	121	451	36	381
QMW75670.1	1.07e-57	109	443	27	367
QPS13996.1	1.07e-57	109	443	27	367

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4AZB_A	1.68e-54	121	438	8	343	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
2YL5_A	2.04e-54	112	443	2	340	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	2.04e-54	112	443	2	340	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
4AZG_A	2.09e-54	112	443	3	341	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]
2YLA_A	5.07e-54	112	443	2	340	InhibitionOf The Pneumococcal Virulence Factor Strh And Molecular Insights Into N-Glycan Recognition And Hydrolysis [Streptococcus pneumoniae TIGR4],2YLA_B Inhibition Of The Pneumococcal Virulence Factor Strh And Molecular Insights Into N-Glycan Recognition And Hydrolysis [Streptococcus pneumoniae TIGR4],2YLA_C Inhibition Of The Pneumococcal Virulence Factor Strh And Molecular Insights Into N-Glycan Recognition And Hydrolysis [Streptococcus pneumoniae TIGR4],2YLA_D Inhibition Of The Pneumococcal Virulence Factor Strh And Molecular Insights Into N-Glycan Recognition And Hydrolysis [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P49610	6.61e-49	121	438	188	523	Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 SV=2
P49007	9.84e-08	123	246	332	457	Beta-hexosaminidase B OS=Pseudoalteromonas piscicida OX=43662 GN=nag096 PE=3 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
0.000880	0.997657	0.000672	0.000259	0.000275	0.000229

TMHMM  Annotations     

start	end
12	31