CAZyme Information: MGYG000001018_01993

Basic Information

• Species: Mediterraneibacter sp900751785
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter sp900751785
• CAZyme ID: MGYG000001018_01993
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1703		187522.18	3.9234

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001018	2841260	MAG	Sweden	Europe

• Gene Location: Start: 15941; End: 21052 Strand: +

Full Sequence      

MKRRCIGFLAALMLTVTGFSVPAAAAGEADVFPAWNVASDRQVEVSSVEAALPGNVGGLV
VDGDNETRWSCDAMKTGTSEDQEQTPQWLVIDLEAPETDVDSITINFYKKVWGAQYKIQT
ASTNDEDTEWKDVKSIEHASGSLADDYVEEITDVGTLDRYVRFYFEKVNPQAAGTGVSIR
EIEIMGKQLVTGNISLDKSVEVSTVENAMPQNVGDNTVDGDSATRWSSEKMKENGITDDD
AQTAQWLVIDLGTDQSVVDDIKIDFYLKVWATKYRIETAASRDAESWTTVAEVDRTSSDG
ADDQTDTFSGNQLLTTDLQRYVRFYFEKINVNAGGTGVSVREITINGTQPYVSTPGESMT
AEEVMQGITEIPALTADSTKVELPDVPEGFEIAVIGSDKEQVISNDGVITDRNIGDREVT
ILVEVSSVTENDEEEADTARKNFTLTVPSKNAFYPEYFPAVDNPNSKPAVIPTLQEWYGY
EGNYTLSAESRIVINDAANVGLQAAAENMQGDLEEFAGVKPEIVSGTAADASSADIYIES
QTEDIYDTGDEGYFMTTDENGVRIYSSTYTGALYGTVTAEQILWQDDGNDNIPCGVIRDY
PDYEIRSVMFDVGRIPHRLQYLQDYTKILTWYKMNEFQLHLNDDFTYSPEGLPSGSEWNG
MHRLESDAFPSLTENQAYTGERFEYFNEVYGDPVYTKDDYRNLEDMANAGGIDLIPEIDT
PSHSNAYIRYAQENPDEIDWLGPIQSNNNAQMLALDINSSNANEAAKAQTARKFMEALYD
DYLGGDDPVFSGDTVNIGADEYWDKSNPEAYRQYVVFLDELMQKYGKTTRMWGALKLFPG
ETEISPDNIILDIWATYEDDPIARLEDGFRVVNFPQPYLYTTPGRDHKDMIVEEWLFKNW
DPTIFNGNIRAEAGEPLLLGAKASIWGDEFREGIVEADLHERALRSVAMVAEKTWGGSEK
TDDYIAYQETFDRLQEGPGAQIAMTIDSQTDVVADYDMSRTEETDGTITVKDSSGNGYDA
QVTNGKVVEVDGEMMIEFDGSTVMTTPLQTLAYPYTVSFDVKASEGNTEDSLLFSGYDGQ
LLAKGLDNDYISLNRSFYHQSFDYEIPEDESVTVTIVGTARNTKMYVDGQLVKMLYSSDS
GKSDEYFSTFVFPMEEIGENFHGYIGNIKAYNKALEPDMIRTDTADVTEVNVALNRNAYS
ERFGNQPDLNTGLLKYHPASKATDGDKADAEAEITSTDPNSYWISSNNNSDYLMVDLGEE
RQVSRVVLTWEGQYTAGGFDIQVSTDGSEWQTVKQVRGNTSSVTEVILDTPAAARYVKMQ
GVSRNANYYGVREMEVYEKVDRSGLSGLLAEVKQVIADKDLENSGDETAIALVEAVIPAE
NAMDNAAAAQKEIETAQAVLSEKYEAYKESAGEPEPPETLDTDLLEYTIGLASSADLTDV
VPAVVERFNAAFASAQEILEKAKAGDPSVTQEMIDESWRELISVMQYLSFRQGDKSDLEK
VVAMAEELDLDKYLDEGKDAFEAALANAQAVLADENAMQDSVDPAWRELLKAMSELRLKP
DKSALEELIAQAQGLNEADYEETSFRAMLSVLAEVQAVYDDSSAAQDEIDAAAEKLQAAL
DGLTAKADAPAGTDGSQNAGDAQDTAGGEKQTGADSGQADESGESKTAPGKAVKTGDTFT
YMLWAAAVLAAGAVILLEKKKQK

Enzyme Prediction     

No EC number prediction in MGYG000001018_01993.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	599	956	4.4e-50	0.9673590504451038
CBM32	1216	1334	4.9e-21	0.8548387096774194
CBM32	51	182	1e-15	0.8790322580645161

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.14e-78	604	957	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	4.50e-31	605	956	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.
pfam00728	Glyco_hydro_20	1.80e-30	603	955	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	1.70e-24	459	955	125	613	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam02838	Glyco_hydro_20b	1.89e-23	467	599	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
AXH51903.1	6.55e-274	36	1343	42	1274
ASY50997.1	9.21e-274	36	1343	42	1274
AWS25495.1	9.21e-274	36	1343	42	1274
QQA11576.1	2.56e-273	36	1343	42	1274
AMN35076.1	2.56e-273	36	1337	42	1268

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	5.49e-55	371	1165	9	726	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	5.40e-27	466	958	32	477	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]
7BWG_A	3.24e-18	551	963	87	484	AGlycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5],7BWG_B A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5]
3GH4_A	5.50e-18	449	964	23	501	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]
4C7D_A	6.17e-18	549	968	78	468	Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7D_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_A Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	7.90e-59	353	1165	14	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
P96155	7.03e-20	481	887	152	534	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
P43077	3.28e-16	525	964	86	514	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
B2UP57	1.31e-15	551	955	58	447	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
P20060	4.13e-13	536	968	110	506	Beta-hexosaminidase subunit beta OS=Mus musculus OX=10090 GN=Hexb PE=1 SV=2

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
0.000464	0.998555	0.000270	0.000304	0.000200	0.000174

TMHMM  Annotations     

start	end
5	27
1678	1697