CAZyme Information: MGYG000003087_00969

Basic Information

• Species: Merdibacter sp900543035
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Merdibacter; Merdibacter sp900543035
• CAZyme ID: MGYG000003087_00969
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1850	MGYG000003087_18|CGC1	202381.82	3.818

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003087	2304658	MAG	Spain	Europe

• Gene Location: Start: 12940; End: 18492 Strand: +

Full Sequence      

MNKQKSSAIVKSLLAAAMLVPSFQVGTLAVSANEGTDTGGVSTLAETPMNMNLALNKSVT
ASAEYGSMPASNLTDDDESSRWSTEADATQWAVVDLGEIYQMNTFSMIWESDSVYASSYN
IYVSDDGESWGEAVVARTGNTARNCTESLAEPVSGRYVKLEVTAMHGYPSVSASDFKVIY
SDGETVPQDPYENVALNGTASSDSNEADGLNASKAFDGDRTTRESRWSSAVADGPHWLAV
DLGQTRNIKTVMLYWETRKATHYQIQVSDDGSDWRTVKEINDRPASTTDRIILDNTESAR
YVRLYIDSFTAENPDGDVTWNTISLFEMEVYGGEIQESASDIANQIEIADPQLGDETLNV
SYPETDRYTIEYKGTDYEQVVDENRHIYTPIVDTVVNVAFKITDNETGEYEFKEIGITIP
GTYTQEEGDNAAPDILPELREWKGSTGNFTVSDSSRIIYADEGLQAAAEEMAADYKDLTG
KDITVMQGTSEDVQAGDFYFALTDDTSMGLMEEGYLMNVEDAITVTAETQTGAYWATRTI
LQGLKLNNFETFPKGITRDYPLYEIRGYIMDVARRPFTMDFLEQVVKEMSWYKMNDFQVH
INDNLIPLESVSDPMSAYSAFRLESSIKEGDTLTDSDGNPVTLNGENLVYQQDLTSTDLF
YTKDEFRDFIQESRELGVNIVPEIDTPAHSLALTKVLPELRQGTSGRQNDHLNLIGESYN
ASLAFVQEIFSEYLDGSDPVFDAQTIVHIGADEYNASSQAYRMFVNDMLEYVEGTGRKAR
VWGSFTQAAQGEDINAEGVEINLWNFGYANMDEMYDDGFDLINCNDGNYYIVPNAGYYYD
YLPDSTMYNLAINTISGVTIPAGDPQMKGGAFAVWNDMTDYLYNGVSEYDIWDRISNLPL
FAAKLWGRGDMDLTQAQAASDALGEAPRTNFGYEVDSVSDEYVNMPMDTLDDTSDNDFTV
NEGENASIVEVDGKNALQLNGGTSYITTGLETAGLGNDLRVKVKRTSDSTDDQILFESPY
GSIKAVQGDTGKVGFTRELYDYSFNYTLPVNEWVELEFKNQQNVIELYVNGSLVDTLGDD
EQIQGRPMRATCMFPMAKVGSETDAFVGYVDDVRLGVNDDFASTMALDYAVETANAVMDA
ESSDVLQPLIDQAKELFTQYAPDAAAIESLTAQINDVLAGMDYEKADYSRVNAYLDLIDD
LSVFTDATVKTLEMAVEAVRENLPASMQATVDAYEAAIVNALNGLELKELSNTNYVDSSM
LEATASSYQHDGSDPENVLDDNPSTMWHTDWNVTTMPHWIDLQISEPTVVNGLYYLPRQS
GSNGNATSYQVQVKNAEGQYETVAEGTWSSNSSAKEVTFDAVETTNVRLVYVKAVNNNGS
AAEIKLMLANVEPDVEGLQAAIEKASAVTNNNYTEATWNALQAKIAEAEELAAAEDPDAN
EVEIMKVELVAATMALRLSDTIVDEEPASDAAIQALRDMVEKAIALGSEDEALNAAIEAA
QAVLAEEEPTVTEVVTALLNLSEAMQAVNAGESVDALREDVQATIDFINENILNDVEGLR
PAKVQALKDAVAAAQTLVNDPMATADALKAANKAMTKAAQELWEIVTKAELEALIEAANG
YLDGDYTAESLDALQAAIESAQTVAINDDATTAEVTEAITNLSNAIAGLESIRLDKSALE
HEIELVSEMVANLDDYIASSVEGLADKLADAQNVLENATTQAEIDEATKTLREARLNART
KADTSALEELIAYAKSLDLSGYTTESAQAVIQNLARAENLITDPEITQEEVNNMVETLQA
SVDNLVEVNNSTSAEDTTNTAAAMQTGLFAGLLAVSAGLVLMMRRRRTER

Enzyme Prediction     

No EC number prediction in MGYG000003087_00969.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	556	906	4.3e-58	0.973293768545994
CBM32	200	328	3e-25	0.9274193548387096
CBM32	57	166	4.7e-22	0.8629032258064516
CBM32	1263	1384	4.4e-17	0.9354838709677419

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.02e-108	564	907	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	2.19e-32	565	907	1	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	4.42e-29	563	906	1	342	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.
pfam00728	Glyco_hydro_20	3.26e-24	563	906	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
pfam02838	Glyco_hydro_20b	4.24e-24	432	559	1	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCL58378.1	0.0	25	1459	9	1422
QWT17580.1	0.0	2	1459	6	1472
QPS14026.1	1.10e-252	78	1605	79	1475
QQY27155.1	1.10e-252	78	1605	79	1475
QMW75640.1	1.10e-252	78	1605	79	1475

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	6.12e-100	342	1101	3	720	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	1.54e-23	433	893	34	464	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]
6YXZ_JJJ	1.85e-21	225	705	65	454	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]
6Z14_JJJ	1.85e-21	225	705	65	454	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]
3GH4_A	3.82e-20	433	782	39	375	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	1.77e-103	337	1101	20	742	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
P96155	2.01e-14	429	699	135	380	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
Q2MGH6	5.62e-13	1205	1415	1440	1656	Endo-alpha-N-acetylgalactosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=SP_0368 PE=1 SV=1
B2UQG6	3.28e-12	503	753	89	327	Beta-hexosaminidase Amuc_0868 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0868 PE=1 SV=1
P29767	2.70e-11	1256	1386	51	183	Sialidase OS=Clostridium septicum OX=1504 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
0.000268	0.998955	0.000200	0.000195	0.000180	0.000156

TMHMM  Annotations     

start	end
1821	1843