CAZyme Information: MGYG000001373_01858

Basic Information

• Species: Faecalimonas sp000209385
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Faecalimonas; Faecalimonas sp000209385
• CAZyme ID: MGYG000001373_01858
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1627	MGYG000001373_1|CGC17	180454.23	5.0365

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001373	2218229	Isolate	not provided	not provided

• Gene Location: Start: 1896803; End: 1901686 Strand: -

Full Sequence      

MKKWKKKVLALALSMSLAVTGNVTIFAETKAPKANDNLALGKTVTASSDHANFPKSNLTD
ENQESRWSAEAAPEQWAYVDLGAKKSMNYFSMLWESDTEYGTDFKIYVSDSTTDWGKPVA
EKTGNTTRKTEVKLDHTVEGRYVKLSVTKVSKYPNVSCCDFQVKLVDDTTEPEEPEKPQK
PQNPQENVAQGKTAVADSVEANNLTVDKAFDGNTKDTRWASAMNSNPHWIYVDLGAVKDV
KTIRLFWETRKATNYRIQTATTLSSQMKDSDWTDAKVMNTRPASKTEKIVLDNKVQARYV
RLMIDKFTAEDVDGGATWNTISVYEMEVYGGEPKAGMDDLAREIQIKTPERTDKKLQVTL
PTSEDYTIKYNGTDYEQVVGPNLEIYQPLVDTVVKVSFKLTDKKNDKNYMFEERNVVIPG
RLAKEEGDNKAPKVLPELREWKGSTGNFTPSASSRIVIQSDALKDMANAFAKDYKEITGK
EISVVKGEAKPGDFYFTLTTDKTKGLQKEGYSMEIADKVTVEAETTTGAFWATRTILQSL
KLTNNIPKGQTRDYPLYEVRGFILDVGRKTFTMDYLQQVVKEMSWYKMNDFQVHLNDNLI
GLENVKDPMKAYSGFRLESDIKEGGNGGKNKADLTSKDVFYTKNEFRDFIEESRTYGVNI
VPEIDVPAHSLALTKVRPDLRHGTSGRQNDHLNLIGDKYNDSLEFVKSIFGEYMTGANPV
FDKQTTVHVGADEYTADGNAYRKFANDMLGYVKESGRKARIWGSLSTIKGNVDVQSENVE
MNLWNFGWANMDKMYEEGFDLINCNDGNYYIVPNAGYYYDYLSNETCYNLAINTIGGVTI
PAGDEQMIGGAFAVWNDMTDYLNNGISEYDVYDRIKEPIALFGAKLWGKGDMNTNQALDL
SKQLNDAPQTNFGYETAKDKEGAIANYPMDDKSDYSANKHNLVDGKNVEITNVDGKSALK
LNGKESYINTGVGTVGLGNDLRVKVKRTSESVDEQVLFESSYGSIKAVQKETGKVGISRE
NFDYSFNYELPVNEWVELEIKNVNNMKNNRIQTRIELYVNGELKDVLGDDEQVEGKSMIA
TTMFPVDTIGSKTKAFEGYVDDVRVGTAVEGTYTSTITLDRAVWTATEVAKDNEALKPLL
EEAKQLLTKFNPTKAEVENLTNRINEVISSTQFKKADYSRVDKYLALVPEDLSAFTKESV
DNLKYVIGSIRRDLPASMQDVVDGYEKALAKALKELKIYEAANVNYVDNRTVKATACSKN
GSEGPDKAIDGNKNTIWHTNYSGEDKCASNQHWINFEMKEPTAVSGLTYTPRANGGNGNL
TSYEIKASDDGKNYTTVKTGTLADDAKEKVIDFGKTVTTKHIRVIYKASHGGFGSAAEFL
IHRAGVKADVEGLNALINEAKAMKNEGYTEDSWKALQDKIADAEELAKAENPDANDVEVM
KKQLRKAMMSVVLEEKGDEPTDDEKAALRDAVKKYSKYDEKDYTAESWKAFAKALADAKK
VLDNKNATKEQIDNALNTLEEAADALVPADNGNGNDNGNNNGNGNNNGNGNNNGNGNNNG
NGNNNGNGNNNGNGNNSGNGNNNGNSNNKPTGTKPPKTADATPIGLWLALLVVAGGSIFF
SKKRKHS

Enzyme Prediction     

No EC number prediction in MGYG000001373_01858.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	552	887	1.3e-58	0.9673590504451038
CBM32	1254	1379	3.2e-24	0.9274193548387096
CBM32	43	151	1.5e-20	0.8467741935483871
CBM32	193	326	7.8e-19	0.9354838709677419

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.07e-118	558	888	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	3.04e-29	560	874	2	293	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	1.23e-27	557	875	1	335	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
pfam02838	Glyco_hydro_20b	1.97e-27	431	553	1	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
cd06563	GH20_chitobiase-like	1.70e-26	557	875	1	334	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	1534	1	1494
QWT17580.1	0.0	37	1427	40	1452
QPS14026.1	9.13e-282	1	1526	1	1401
QQV05894.1	9.13e-282	1	1526	1	1401
QQY27155.1	9.13e-282	1	1526	1	1401

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	4.68e-112	357	1040	18	665	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	9.36e-28	432	876	34	467	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	8.38e-23	432	770	39	383	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]
7DUP_A	1.11e-20	459	733	34	316	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
6YXZ_JJJ	1.80e-20	191	685	39	454	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	2.93e-117	328	1040	11	687	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
P49008	3.68e-16	429	737	32	339	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q0TR53	5.85e-16	1140	1382	532	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
Q8XL08	5.85e-16	1140	1382	532	766	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
B2UQG6	3.63e-15	430	733	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
0.000288	0.999032	0.000214	0.000171	0.000161	0.000140

TMHMM  Annotations     

start	end
1604	1621