CAZyme Information: MGYG000003148_00712

Basic Information

• Species: Faecalimonas sp900551895
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Faecalimonas; Faecalimonas sp900551895
• CAZyme ID: MGYG000003148_00712
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1611	MGYG000003148_3|CGC2	179126.61	4.5639

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003148	1849841	MAG	United States	North America

• Gene Location: Start: 172978; End: 177813 Strand: -

Full Sequence      

MKKWKKKVLALALSMSLAVTGNVTIFAETKAPKASDNLALNRPVTTSAAPLDQFKAEYLT
DADESTRWSSEAKPEQWAYVDLGEKKSMNYFSMLWESDSQYVTDFKIYVSDSTENWGEPV
AEKSGNTKRKSEVKLEKAVEGRYVKLSVTGVTPYPSVSCCDFQVKLVDDTTDPEPEQPQE
PQDPQKNVAQGQPAFSDSFEADNLKVDKAFDGNTKDTRWSSAANLNPHWIYVDLGSVKDV
KTIKLYWETRKATTYRIQTATTLSNPMKDSDWKDVKVMNDRPANKVEKITLDKTEQARYV
RLMIDKFTAEDVDGGATWSTISVYEMEVYGGEPKASMDDLAKQIQIKEPERTDKKLEVTL
PTSDDYEIKYNGTDYEQVVGPELEIYQPLVDTMVKVSFKITDKKDEKNYAFEERNVVIPG
KLAEEEGDNKAPNVLPELREWKGTTGTFAPTAESRIVIKNDELKDMADTFAKDYKEITGK
DIKVVTGEAKAGDFEFALTTDKTKGLQKEGYLMNITDKVTVEAETATGAFWATRTILQSL
KLTNNIPKGQTRDYPLYEVRGFILDVGRKTFTMDYLQQVVKEMSWYKMNDFQVHLNDNLI
GLENVKDPMKAYSGFRLESDIKEGGNGGKNKADLTSKDVFYTKDEFRNFIEESRTYGVNI
VPEIDVPAHSLALTKVRPDLRHGTSGRQNDHLNLVTKYDESLEFVQSIFGEYMTGTKPVF
DKQTTVHVGADEYTADGNAYRKFANDMLSYVKDSGRTARIWGSLSSITGDVDVQSEDVQM
NLWNFGWANMDKMYEEGFDLINCNDGNYYIVPNAGYYYDYLNNDTCYNLPINTIGNVTIP
AGDEQMIGGAFAVWNDMTDYLNNGVSEYDVYDRINEPMALFGAKLWGKGDMNTNQALDLS
KKLNDAPQTNFGYETAKDSEGAIVNYPMDDKTDYSVNKHNLTEGKNASIENVDGKNALKL
NGKESYMNTEVGTAGLGNDLRVKVKRTSDSTDEQILFESSYGSIKAVQKETGKVGISREN
FDYSFNYELPVNEWVELEIKNKQNKVELYVNGELKDVLGDGEQIEGRPMLATTMFPIDTI
GSKTKAFEGYVDDVRVGKAVESTYTSTIALDRAVWTATEVAKDNDALKPLLDEAKQLLTK
FNPTEAEVTDLVNRINEVLSSSEFKKADYSRVEKYLALVPEGETERSVFTEESLANLDYV
VSTIRYDLPASMQDVVDGYEKALAKALQELEIIKESNINYVDNKTVKVTACSEQGGGEAA
AKAIDGDENTMWHTKYDELNMPHWIDLEMKEPTAVKALTYVPRKSGDNGKLIKYEIQISD
NGKEYTPIKEGTLKDRNKTQVIEFEAVTTKHIRLVYKESVGNFGSAAELRLHAANVKADV
DGLNALITEAKAMNNNDKTYTADSWDALQAKITEAEELAKSENPDANDVEVMKKELRKAM
TSLVLEGKGETNDGKDALREAVEKYSKYDEKDYTADSWKVFADALADAEKVLADKNATEK
QIQDALDALKTAADALVPVDNGNDGGSGNDGGSGNNGGNGNNSGSGNNSGNGNNGGNGNN
SGNGNNGGNSNNKPSGTKPPKTADATPIGLWLALLVVAGGSIFFSKKRKHS

Enzyme Prediction     

No EC number prediction in MGYG000003148_00712.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	552	886	1.8e-59	0.9673590504451038
CBM32	1249	1369	4e-22	0.9193548387096774
CBM32	51	150	1.5e-20	0.7741935483870968
CBM32	200	326	1.4e-19	0.8790322580645161

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.02e-119	558	887	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	2.90e-28	560	887	2	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.
pfam02838	Glyco_hydro_20b	3.12e-28	431	553	1	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
pfam00728	Glyco_hydro_20	4.32e-27	557	874	1	335	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	9.22e-26	557	732	1	175	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCL58378.1	0.0	1	1521	1	1491
QWT17580.1	0.0	37	1417	40	1450
QPS14026.1	8.23e-282	1	1516	1	1401
QQV05894.1	8.23e-282	1	1516	1	1401
QQY27155.1	8.23e-282	1	1516	1	1401

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	5.36e-115	361	1091	22	726	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	2.99e-28	432	872	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]
4A41_A	3.01e-24	1246	1373	30	161	CpGH89CBM32-5,from Clostridium perfringens, in complex with galactose [Clostridium perfringens],4A44_A CpGH89CBM32-5, from Clostridium perfringens, in complex with the Tn Antigen [Clostridium perfringens],4A45_A CpGH89CBM32-5, from Clostridium perfringens, in complex with GalNAc- beta-1,3-galactose [Clostridium perfringens],4AAX_A CpGH89CBM32-5, from Clostridium perfringens, in complex with N- acetylgalactosamine [Clostridium perfringens]
2J7M_A	1.37e-23	1240	1372	5	148	Characterizationof a Family 32 CBM [Clostridium perfringens]
2J1A_A	1.41e-23	1240	1372	6	149	Structureof CBM32 from Clostridium perfringens beta-N- acetylhexosaminidase GH84C in complex with galactose [Clostridium perfringens ATCC 13124],2J1E_A High Resolution Crystal Structure of CBM32 from a N-acetyl-beta- hexosaminidase in complex with lacNAc [Clostridium perfringens ATCC 13124]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	3.13e-120	357	1096	40	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
Q8XL08	1.25e-21	1110	1372	485	766	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
Q0TR53	1.25e-21	1110	1372	485	766	O-GlcNAcase NagJ OS=Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) OX=195103 GN=nagJ PE=1 SV=1
P49008	5.36e-17	429	680	32	282	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UQG6	1.18e-15	430	732	28	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

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
0.000290	0.998933	0.000247	0.000178	0.000162	0.000143

TMHMM  Annotations     

start	end
1588	1605