CAZyme Information: MGYG000000670_01829

Basic Information

• Species: Faecalibacillus sp900544435
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Faecalibacillus; Faecalibacillus sp900544435
• CAZyme ID: MGYG000000670_01829
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1945		218234.15	4.5101

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000670	2790604	MAG	Kazakhstan	Asia

• Gene Location: Start: 4016; End: 9853 Strand: -

Full Sequence      

MKKSKKILATLIATMTAVSQIVPTIKVQAATDSIRLATFNIAANKKPDVVKLNELLKNNQ
VNVVGLQEVDVNTTRNPYDMLEKFTEQGDYEYSYFQKAIDMKDGVGEYGIGLLSNLELSN
STGGSLNSEGINEARAWQKSEVEFNGKVIAVYNAHLTHESVDARAKQLLELKQTMDQDPT
EYKVAFGDFNVDQSHDEIYPFLEDYNIANGKDGKWYDTYNGVDASMKTNAIDNIITSRNM
EISHITMVETSLSDHNLFYADAKLLDHDVTSREYLDLVIKQANDLDEDQYSNATYKVLDE
KLTAGELLDENASQEQINQAIKDIQDAQENLKVKYENLALNKNVNVSGLEVNDGRFTAAM
AVDGVVSKTSRVSFAKDKDEQWLEVDLGKVENISHFVINYESQAPAFKIQVAGEDKVYQD
VYEVSGLDGQISNIQNITVDPVDARYVKYVQLKRWKHSGNGKYYSGSIYEFEVYQKDPNA
KNYDNLALKKDVSVSGLEVNDGRFTAPMAVDGVVSKTSRVSFAKDKDEQWLLVDLGGRKT
VSEFVINYESCPPAFKIQVSTDGVHYKDVYKEENLADGGPSAVKEIQIDATKARYVKYVQ
LKRWKHSGNGRYYSGSIYEFEVYKERNHATASEVLKAASKEAPQIDGNKLVLPTVPEGFE
ISLYGCDNKQVVTMDGTVIQPLEDMNVNVLYQVKNLKDDSDVATSEEDIKFVVPGKYSKE
ESINAKPNVMPGLREWKGNEGEFTLTKDSKIVVKDESLKATAKQIQFYLKEMVKKNLAIV
SSGETTGDIVLTKDSSLDVLGKEGYTLDINDLIEIKSNYETGILYGGISITQILSQDEGK
NNIAKGIARDYPKYEVRAGMLDVARTYIPMDYLKEMTIYMAYYKLNEVQVHVNDYWGATG
YSAFRLESTTYPMITSTDGSYTKEEYKNYQKEMKNYGIDVITEIDTPYHAECFRSIPGAK
MLKTGALDIREQSSYDIIENLIDEYLDGDDPVIESDKFHIGTDEYDKNYSEQMRKWTDHF
IKYVNNKGYKTRLWGSLGSRGFNGTTPVSNDATVNLWAPYWADVKETYASGYDIINTCGG
WLYIVPGANAGYPDRLNISTLYDKFDVNNFSPSRNAGQGTAIMPVAHPQTKGAQFCIWND
MTSYGGGFTWFDIYDRFKDAVMITSEKTWYGEKTDGQTAAQFVERVNKLNSVVPGANPGR
VVESADKNVTTIDFESVKDNKAIDLSKNGYDATLKNVTIEKGNGGHVATLNGNGYVSLPY
QTIGYPYTVMMDVKLDSNTPENTEIFSGSDGVMYANVDGTGKIGYKRSGYTFTFDYELPK
DKWFNLALTCDQKNTTLYINGKAISTGINMKTAINNRKDSSTFVLPVEKILNNAKGSVDN
IKIYNQVSSASEIADELGYISLENLALHKNATASSVYPGSNKTPDLAVDGDNSKSADNRW
SSKRATGNGSNEDSGQHGTKEQYLTVDLGDVYKVDKVFISWEGAYATNYTIQGSLDGENF
FDIKVVDDGKGGEETHDDLGNKETRYIRILCRQAKTANYGYSIYELEVYQSANEELRKLA
QAGKDQLSQFEVGNKNGNIAKKDYEELEKAYKDYLDLAQGEKISDEEIGRLLKEVTELNS
SIESYVIYSKDELNDLYQAMKAYKEKDYTKDSFVGFDDQLNALKEVIDQADDYQKVNDAL
KQLKELNSTLVKLDRSKLEKIIKEYQELKEEDYTVDSWQQMKEVLDAAQAVYNNSSLNQE
DIDQAVASFDGVQLVQRGNVEKLEELLSSIKESDYTVASWSQFDSIYQEAKQMVNDSCNV
DQKAVDEMIEKVKDAMELLVKAGNIDDYQDAVDKVSDKVGQLDQSKYTKESWDKLQETLQ
KAKDLATKEDVSQEELDNMLASLNDAYDALKEAKTDSVITDTDTNDKTNTTDKNTTKTGD
DVSLFGYVGLLCIALLGFVYSKRFE

Enzyme Prediction     

No EC number prediction in MGYG000000670_01829.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	848	1169	3.4e-48	0.9703264094955489
CBM32	1412	1547	1.9e-22	0.9274193548387096
CBM32	500	621	2.9e-17	0.8870967741935484

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	4.67e-104	855	1171	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	7.08e-30	857	1140	2	278	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	5.37e-26	854	1138	1	317	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	4.75e-23	854	1138	1	316	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.
COG3525	Chb	2.63e-21	696	1140	102	589	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW75624.1	0.0	1	1945	1	1946
QPS14042.1	0.0	1	1945	1	1946
QQY27139.1	0.0	1	1945	1	1946
QQV05909.1	0.0	1	1943	1	2018
QTY17007.1	1.11e-278	613	1570	21	981

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	5.79e-63	635	1378	12	726	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	2.32e-24	717	1169	23	474	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]
3GH4_A	8.57e-18	725	1075	37	411	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]
7CBN_A	2.79e-17	776	1140	57	457	Crystalstructure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835],7CBO_A Crystal structure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila in complex with GlcNAc [Akkermansia muciniphila ATCC BAA-835]
6JE8_A	1.60e-13	784	955	18	199	crystalstructure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEA_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEB_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	1.44e-66	631	1383	22	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
B2UQG6	1.60e-16	776	1140	76	476	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
E9DFH0	6.81e-15	803	1117	122	475	Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 SV=1
B2UP57	9.67e-13	784	955	39	220	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	3.41e-12	789	1004	95	314	Beta-hexosaminidase subunit A2 OS=Dictyostelium discoideum OX=44689 GN=hexa2 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	0.999061	0.000182	0.000168	0.000169	0.000149

TMHMM  Annotations     

start	end
1922	1941