CAZyme Information: MGYG000000140_01197

Basic Information

• Species: UMGS1375 sp900066615
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UMGS1375; UMGS1375 sp900066615
• CAZyme ID: MGYG000000140_01197
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1540		171177.56	5.4766

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000140	3539979	Isolate	United Kingdom	Europe

• Gene Location: Start: 252686; End: 257308 Strand: +

Full Sequence      

MKKKKCIAAGALAAFLLCESLFTPNLAGMGAGLLKVQAAAANVALNKEVTSSANESATWS
ADKAVDGDKTSDSGRWSSGDMGTNRDNPQWLVIDLSAATTNVESINIYFNLKAWSTEYQI
QTSDSNGADANWETVYELSRDSANVQRNDPDVINASDLSKAELKRYVRFYFKKGNINGWK
CISVREIEIMGTQSGMIETAASVLKNLSSLTVEANEEELVIPNTSEQYDISIYGSELDQL
LTEDGKASAMRIGDRSFNVILKATNKNDPQDTAKKNVTVTVKGNTDKYPELFKKVSNPNP
MPKVLPTIQEWYGYEGNFKLTEQSRIVVNDAAGVDAEEAAKEMQSDIHDICGLDLEIVKG
TSAGTNDIYLESQTEDVYDVGKEGYLMVNGDAGLKIYSSTKTGLLYGTVTVEQILYQDSE
HANVPKGVIRDYPAYEMRGVMFDIARIPTRISFLNDYTKIMKWYKLNEMQLHINDNQWSD
PAYSAKYEDWADTEASHRLESELFPSLATQKSKFVKTGDSEDRYDYYYNVHTGKSGELYY
TKEEFRKMNEEAKACGIQVVAELDTPGHSAAYTKYVHDHQEEVIKSLVKYGYLKAADYLN
ADGNVKQGASFYIHNPGNWELLALDDQSSNAQIRQNAINARIFMKALFDEYLGGIDGIDA
VFDAKNVNAGVDEYWDRTDANKEAFRRYMNEMYSYLHDKYDVEVEMWGAMEVLKGNTKVN
NNIILNMWSATEDSPSARLAEGFRLINVPQTYLYNTPGRYHKDMIQENNLFYNWDPSVFS
GGVKTDKGDPQVLGAKTALWGDENREGITEADLNERYLRAAAMVSQKTWGSNKETSFVNY
EQTFDALREGPGTAISYDVESVSDVVLDYDFANLSADGEIIYDTSGNAYNGQVSGGEKAE
KDGETYLKFDGNTVIRTPLTTLGYPYTMSFDVYLDGTEKNTKESSLFSGYDGRLQLAGIN
GSLSLNRDYFNQSFEYQVEKNKKHRITVVGTYQTTKLYVDGVFKKILYAAASDPENNGAL
GASTWTDADNNYRSTFVFPLNEIGKNFSGYLGNIKAYNKALSTEELAVENVGATLVDVAR
NRGAYADLGNKGYKGDEMRLYPAWKATDGDGHVTGTRGVSTSYESRWCSSDRNDDFLMID
LGRERKVSKVVIDWVAGRYATAYDIQVSNDGADWSTVKSVSGNEKAWTEDSFTETSARYV
RMKGVQRKASEYAICEMKVYQSVDRSVLKNAYEEAKTILENTKADFAYASANTDELAELW
NASVRAKAVYGDVMAGQEELDAAKAELKSAQNAYLKKVTGCKETLTEEIKVSEKIDLSRY
TSESAAKYQEALKRAKEMLDRADAQPEELDAAKKELEEARKALTEKAEQQKPDPTPTPTP
NPNPAPDTVKTVPKKGTVFTDGKGISYKVTKSNAKKGTVAVTGTRKKGNKITIPATVTKD
GYTFKVTEIAAKAFQNNKKLTTLVLGANISKIGTKSFYKNSKLKSITFKNKNAVKIGSQA
FKGIKATAKVTVPKKMTAKNFGKLKKAMKSAGKKVKYKKK

Enzyme Prediction     

No EC number prediction in MGYG000000140_01197.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	430	830	8.3e-44	0.9703264094955489
CBM32	1101	1217	1.6e-20	0.8467741935483871
CBM32	49	187	6.8e-17	0.9274193548387096

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	3.88e-67	436	830	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	6.63e-31	438	830	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	1.45e-21	302	431	2	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
pfam00728	Glyco_hydro_20	1.01e-20	435	823	1	338	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	2.87e-16	272	948	101	717	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AMN35076.1	4.66e-235	42	1220	191	1268
AXH51903.1	2.89e-232	42	1281	191	1320
ASY50997.1	4.32e-231	42	1281	191	1320
AWS25495.1	4.32e-231	42	1281	191	1320
QQA11576.1	6.06e-231	42	1281	191	1320

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	7.87e-47	203	1049	3	724	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	3.36e-26	302	833	34	478	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	1.85e-16	293	800	30	464	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]
6JE8_A	4.92e-13	375	571	29	196	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]
4C7D_A	1.25e-12	296	682	1	359	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	6.77e-51	187	1049	9	746	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
B2UP57	2.95e-12	375	571	50	217	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
P49008	1.43e-11	304	571	37	274	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P96155	2.69e-11	267	574	104	376	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
P29416	6.89e-11	383	836	114	491	Beta-hexosaminidase subunit alpha OS=Mus musculus OX=10090 GN=Hexa 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
0.001181	0.952569	0.045577	0.000243	0.000213	0.000206

TMHMM  Annotations     

start	end
7	29