CAZyme Information: MGYG000002014_00267

Basic Information

• Species: Merdibacter sp900754715
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Merdibacter; Merdibacter sp900754715
• CAZyme ID: MGYG000002014_00267
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2008		220439.02	3.9302

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002014	2253473	MAG	Spain	Europe

• Gene Location: Start: 32387; End: 38413 Strand: -

Full Sequence      

MERLRKACKSLLAAALLLTGIPLGMAGQPLTARAAGDDGTFRIATYNIAAKGGAVSAIGS
LIKEENIDVVGFQEVDKNTGRNQVDMLKEIADTAGYDYSFRKAIDYSGGEYGIGIASATA
ILDESGAALETGGYEGRTWQRVEIEIDGKDVAVYNTHLTWEDPAIRAAQMEAVLDAMEAD
DTEYQLLTGDFNAQESNDEFDVFLRDYNIANGLDGEWLDTYIPEDATMKTNAIDNIIASR
NIDIQNVEAVEETEIGSDHKILIADCKLLEEKQVSCQLLGRYISKAQDLVQMSDRYTEAS
LQQLEEALQEAYMADCSTQEKVNAATDALMAAIDRLELLPADPSKPVAWWDFDGDEPLKD
KTGRGNDGVEKGTVSYVDGLENLGNALSTADGYVSVAKVSDDLNLGTEDMSVGFWYKATN
PGTWSAVLGDKNWSSGANPGFAVVQGQGQFYTTYAANGHSQQENIVSGTASKVYDGKWHY
ITAVLDRDGDSMLYVDGQMIASTSIASTADMDATVSTPFNIGADGVGGYRINSLIDEVKV
YRSVLSQPEIEAEYLKNRDKTEEAIDDMVTQTEQYLENLVIDPAETTQLESFTSEDGKVV
SHIFCSENDIIIDDEGRILRQPLVDKKVQISYIVQENKDGVAYDEGTMVENKWIVVKGET
TSGSNPQPEVVPTMQEWRGDDGGAFSLNENTRIVVSAEDMDVLGDAAEITKSDLEEMFGI
NAEITSDAPQAGDIVLALTDSGIETEDEEILELIAQSYRMDVGEYVTVEGPAYKGVFFGT
RSVLQALLTSGNDTIAYGTAVDYPNYPIRQFMLDVGRKYFPMWYLEDLVKYASWLKLTDF
QCHLSEDTFNDYSAFRLESDIPHLTSTDGYYTKDEYREFQKHAENYGIRVITEIDGPAHA
RRFIELGSYEDAPDKYKDLGLDGTHFNLSEEGGARERVLNLMDEVLEEYLGGDDPVVITD
AFNVGMDEYFGDQNDLRAYAVHMYDQVVNKYGKTAFGWDSNASLPNDIYTKEDYPIDDVR
ICYWKWEEVDGGVKALMDAGYKVVNGDHRWYIVPGAQIGFWDYANEERLYNELSAGSMVG
WYGGGMIFPEGHPNIVGGTMLLWNDRGMFAGYTVNDIFARQRSQYPYLAQTYWYGREDET
FEEFTAKVDAIEVGPGLQNLYEDIDSQSDLVYDFDMETLEDGTLKDNSGNGYDAKVTGAV
LSEGPDGSQLTFDGDDYIEAQHKGLNWPYTAVFDLTIDEAQTGDITLFEEIMPEQECVKK
DGNLTGQEKRVIIMQEQEDGTYRLTYSREGFDYAHNYVFEKGKPYRIVFSSDESAPTGGE
FEKWNQPNRMYVNGELVSTLQGPQKPADFNGQWWVDSASMNMPLQKIGQGLVGSLDNFKL
YDRLLSDEEIKALGGFESGEPQPGSDNLALHKEATASSSKNSSFDPSYATDGSQDTRWGS
NYNSSVNDPFDKQEWIQIDLQETYALGEVRLYWQDAYAQEYTIQLSDDGSSFTDVKTITG
SDGGEDIITLNGEQGRYLRILCTRAVPSDDGWQWNYGYSLFEVEAYEAEQIDADKTALNE
AIADAQALNADEYTTSSWNAVSAALENAMNIAADTSADQNTVDQAAAALNDAVAALQVKA
SEAAIQALREMVDKANALGAEDETLNAAIAAAQALLDDAEDAGSSAVVSALLDLSEAMAN
LNTGESSDKLREDLKATIDFINENILTNVDNVRPAKVTELKTAVAEAYQVYMNEDATADE
IRAAIRTLSEKAQELWLIVSKAELNALIESAEAISADGYTDLTYRALQAAITAAKSAAAN
DNATTSEVAQAITDLASAIAGLETITLDTSALEHEIELVTEMVENIANYVPSTVEGLQDK
LNEAKAALEATTQEEIDAATKTLREARLNARTKADVSALEELIAYVNSLELSAYTSASAQ
PVIQDLARAKAMLMNAEVTQEEVNDMVETLQASVDSLVEVSAESTTTAGNENADTTNTAA
AVQTGLFAGVLAIAACALFVIRRRKMSE

Enzyme Prediction     

No EC number prediction in MGYG000002014_00267.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	801	1134	1.6e-43	0.9703264094955489
CBM32	1412	1543	4.5e-24	0.9435483870967742

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.28e-67	807	1135	1	326	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	5.87e-25	808	1107	1	280	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.
pfam00728	Glyco_hydro_20	1.43e-22	806	1071	1	293	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	1.17e-21	806	1051	1	265	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.
pfam13385	Laminin_G_3	1.30e-19	391	550	4	150	Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQY27138.1	2.69e-230	595	1868	365	1668
QMW75623.1	7.27e-229	595	1868	365	1668
QPS14043.1	7.27e-229	595	1868	365	1668
QQV05909.1	1.06e-178	1	1868	1	1942
QMW75624.1	1.92e-165	1	1885	1	1885

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	5.04e-45	611	1167	39	581	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	5.20e-23	667	1151	33	493	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]
2RV9_A	7.96e-21	1407	1546	7	135	Solutionstructure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis]
4ZXE_A	8.20e-21	1407	1546	8	136	X-raycrystal structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5. [Paenibacillus fukuinensis],4ZXE_B X-ray crystal structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5. [Paenibacillus fukuinensis],4ZXE_C X-ray crystal structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5. [Paenibacillus fukuinensis]
4ZY9_A	2.83e-20	1407	1546	8	136	X-raycrystal structure of selenomethionine-labelled V110M mutant of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis],4ZY9_B X-ray crystal structure of selenomethionine-labelled V110M mutant of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	4.53e-48	611	1167	61	603	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
P43077	4.75e-09	743	1044	97	405	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
Q54468	6.34e-09	754	901	285	454	Chitobiase OS=Serratia marcescens OX=615 GN=chb PE=1 SV=1
Q8WSF3	1.42e-07	700	1061	151	541	Probable beta-hexosaminidase fdl OS=Drosophila melanogaster OX=7227 GN=fdl PE=1 SV=1
Q04786	8.20e-07	757	1003	266	574	Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex 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
0.000355	0.998901	0.000181	0.000219	0.000174	0.000151

TMHMM  Annotations     

start	end
1979	2001