CAZyme Information: MGYG000001027_00561

Basic Information

• Species: CAG-56 sp900752065
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-56; CAG-56 sp900752065
• CAZyme ID: MGYG000001027_00561
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1509		164926.02	4.641

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001027	2760146	MAG	Sweden	Europe

• Gene Location: Start: 81951; End: 86480 Strand: +

Full Sequence      

MFPKKMKKVGAMFLAACVMLGSVQLPPLQTKAAAANLALTAVATASNSEKDNGIARINDG
DMSTRWSHDESANSWAQLTWDTAQTMKSFRINWEVARTANYSLQISNDGATWQDIWTRNG
APGSTTDEITLDEPVTSKYLRLNMEGITDSVWQAVSVYELEVYATSLEDARSDVDKLVSG
ITAPQVAADGRSITMPEVPEGVSVRFCADYEQVIGEDGTIYPPYEDKVVKGFFEVTQGEE
KAKTSEFTVNVAGIYPQEAGANEKPSVIPELQEWHGGKGQFVPSASSKIVAAPELAKTAA
IFAADYEDITGNPIEVVEGNLLDAAAGDFCLTLDTDDQGLGKEGYLLRIGNVAVVEAAEA
TGAYWGTVSILQILKQTGGTIAKGIARDYPKYEVRGFSLDVGRKPFSMDTVKQFAKNMSW
YKLNSFQVHVSDDLIFMEDYYNDSEDKSKDAVLNLTKENAYSGFRLESSLVNEETGVSLT
SEDMYYTKDEFRSFIKDSRTIGVDIVPEIDMPAHALAITRVFPEYMSWDWISSTHRPIID
ELDLTNPESTELAKRIWNDYFEGDDPVFDEETTVHIGTDEFHGAAGQEGKEMFRKFSDDM
IRFVQGTGRKVRMWGSLSNKAGTTPVAVDGVQLNVWDKGYSVPKDMYDLGYDMINTLASA
GSGSLYVVPSGSGSKGGYADYLDTQHLYNNWTVNNFDGYEVMAGEDQMLGGVYAVWHDNI
DTRKNGISEYDSFDRFFDALPTVSAKLWGVPEKSWSEFTEIEEKTGTAPNTNMYYEVDSV
TSTVMNYTFDDTLTKDASANGYDATEQKNAEQVAVDGGKALKLAGGESYITTPVNKVGPN
NSLTVKVKMDEDAQGEQILCESWEEFGGFGTYAVKASQKETGKVGFSREGYDFSFDYTLP
KGQWVELTIKGYQNTAELYVNGELEDTLTQEPTVKNAGVKWVNTLVMPVGRIGSKTNSFK
GQIDYAVVGGAEWTASDDLGKIDQSEMTASACTQHSEGAASKAIDGDASTIWHTDWGSNP
KDLITDSHTHWFKLTLDTAKTINKLTYLPRITGTTGNITQYRIEVEKADGTVVTDAVSGT
WELDGTLKTVTFDPVEAKSITIHILDAGADSAGKHGSAAEFNLYQPVEVNADMLNAELDA
LKDLNAADYTAQSWKAFTDVIAKIEAIAGNSGSTDEEKLYAYGLAGKARDVLAEIPEAVT
VDTSALQAKITELENNMNSYTNESAAAFAEYLVNAKKLLVNPVTDTEVTMMLNTLENAED
ILVKKPTESAKLDGAVTDAEKLDLTGYTEDSVKIFKNALGEAKAVLADKNATQEQVDAVL
KKLNDAIAGLKKATASKPEPNPKPEPIPEPEPIPSLEPLPAVGKAVVLNGLQYTVTKSDA
KQGTVAVTKQINKTKKKVTIPATIEANGYTFKVTSISKNVFQKNKKLTTVVIGSNVTNIA
KKSFYKCSKLKNITFKGKKAPKIARQTFKGIQAKAKITVPKKMKQKQFNTLKKRMKSAGV
GSKATYKKK

Enzyme Prediction     

No EC number prediction in MGYG000001027_00561.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	386	748	1.3e-58	0.9703264094955489
CBM32	43	160	5.4e-20	0.9354838709677419
CBM32	990	1121	2.5e-16	0.9193548387096774

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	2.52e-111	393	749	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	1.30e-33	395	749	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	2.64e-27	264	388	1	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
pfam00728	Glyco_hydro_20	1.02e-24	392	725	1	326	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	1.29e-23	392	760	1	355	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
QQY27155.1	2.11e-280	36	1341	193	1483
QPS14026.1	8.24e-280	36	1341	193	1483
QQV05894.1	8.24e-280	36	1341	193	1483
QMW75640.1	8.24e-280	36	1341	193	1483
AYE35153.1	2.67e-273	4	1332	3	1330

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	6.75e-105	176	963	2	726	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	7.68e-36	264	766	33	494	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	9.14e-20	256	721	29	475	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]
2V72_A	1.90e-18	982	1125	11	143	Thestructure of the family 32 CBM from C. perfringens NanJ in complex with galactose [Clostridium perfringens]
2J7M_A	3.74e-15	986	1124	12	148	Characterizationof a Family 32 CBM [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	7.15e-109	173	963	21	748	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
Q0TR53	1.81e-14	976	1148	618	791	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
P0DTR4	1.99e-14	982	1138	509	665	A type blood N-acetyl-alpha-D-galactosamine deacetylase OS=Flavonifractor plautii OX=292800 PE=1 SV=1
Q8XL08	1.59e-13	976	1148	618	791	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
P96155	9.69e-13	224	538	92	394	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI 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
0.000338	0.998955	0.000192	0.000190	0.000153	0.000137

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001027_00561.