CAZyme Information: MGYG000000244_00401

Basic Information

• Species: Catenibacterium sp000437715
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Catenibacterium; Catenibacterium sp000437715
• CAZyme ID: MGYG000000244_00401
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1691		187558.26	5.1504

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000244	2463343	Isolate	China	Asia

• Gene Location: Start: 17787; End: 22862 Strand: +

Full Sequence      

MNKKQGVIGLVATVMIANAAFVDVRPVYAVENLNLAKGCTVNASSYEVISTSPDKAVDGD
IKTRWGTAQNKADNEWIEINLGGEKTVRQININFERTDDAQNILGYKVELEENGQYKEVY
RKTTKAKQNEIIQLDKDHQATKVKVTVLSADGGTINWKNVGINEIEVYSKIVEKADATPN
KNHMANATVTASSSEANTLSPDKVKDGSTEKANRWASDYETPTTNIWLNTKFAGLTLVKE
LKIHFFERDVAPMPSNVKSFDIKYKDKDGVEKLAKSFTNTKKGDGYNNEVVVKFNEPIEA
KELKLCNFVAEAASWNNVSIAEMEVYSNEQTAQKATLNSVVSSIESQSKTIEASVNTLDM
PAVPEGFTVRINGADLEQIIGADGKIVHPLVDKNVKVSYVVTETSTGKEKKTADVDYVVK
GMNEQVTGKNAKPTVIPEIQEWHSNSTEKISVNSLKTVTYTDDKLKAVVDEFVRDYKDFT
GINLTVKKGASQANAFNFELKAPDTLLGDEGYTMDIQKDRINVASVHTTGNMYGMQTILQ
MYKEDNEGYKIGKMRDYPRFKTRGFLFDVARKPVSLDMMKEVARTMRYYKMNDLQTHLSD
NYIFLEQYGKGDNENEAFKAYEAFRLESGLSNDKGETPTAKDYSISKKDFREFIQGERAL
GMKVVPEIDVPAHATSFTKVWPELMVQNKVSPLNRNRPLIDHLDVSKKETKDKIKEIFDD
YTKGANPVFDGETTVHIGADEFLSNYTAYRGFVNDLVPHLKETNTVRMWGGLTWIKDNPV
TQIKREAIDNVEMNLWSADWADGIEMYDMGYKLINTIDDFGYMVPNGNKGRANAYGDLLN
VNRIFNQFEANKVRVRGGAYKYVPAGDDQMLGAAFALWSDNIDKSASGLSESDLYWRFFD
ALPFYAEKTWAATGKEKGSADALAKVAQDKGTGPNTNPYYKENKKGENYESYDFNNGLKD
SSENKRDLKEGKNTEIKDNALVLKDGVSYVTSPIKELGNGNKLSFDIKLKKPAKPGDILF
ESDAAYGTHDIRIMEDGKLGFTRELYNYYFDYELPVGKSVNIEITTAQQKTSLYVNGEYV
CDAKGKFIHNDMVKKDNITHSTFALPLERIGSKTETVSAVIDNVVVSEKAPEVDLYNKTA
WTGRAESETPTSHGGNNEGIIGMAFDNKPSTIWHSDWSQATKDKVPTTSGAAGTGKGADG
SIWSEVKFDKAYEINQISFTPRQDSNSGQVTKASLYIQTEENGEWVEVAKDQTFDANKSE
KTFTFDKQNVYGFKFVASESNDGWVAISEFNIANKEVTNNTYTVYVEAEKGGKVSGGQEV
KAGQSATITATPNRGYVFKGWYRPNGEKVSDKAEYAFNVKCNTALIAKFEKSSEADVKIT
DIQKLDDLTVVKGTSFDSLNLPNKVSITLENNETEEVDVTWNKASYKANECGTYVLEGTL
TLPEGVVNPDGLKVVVKVTVENKKYTVVVDSDQNMGTVSMDKEDGIYEEGSNVTVTAKAN
KGYEFVSWTDENGREVSTSNPYTFEATTNTTLKANFKKVKVTPAKPSSQDILDDLLAGNK
VQSVVAKGQTQFVLPEVPEGYSITITKVSPEGIISLDGKVTTPKKDADVIVTITVTDAEG
KTASHDFTVKVIGLNEVDKETPKDPETGKDTPKDPTQDKKPAKTGDATSIASWISMMTVA
GAMLLKRKKRS

Enzyme Prediction     

EC	3.2.1.52

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	556	912	1.9e-52	0.9703264094955489
CBM32	45	165	8.1e-19	0.9032258064516129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	7.93e-109	561	911	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	2.22e-29	563	910	2	302	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	3.57e-27	432	556	1	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
COG3525	Chb	1.85e-21	506	960	202	666	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam00728	Glyco_hydro_20	1.61e-20	560	912	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBA55782.1	0.0	34	1376	15	1357
BAI94822.1	0.0	4	1439	7	1433
ADO53681.1	0.0	4	1376	7	1378
QRI58902.1	0.0	34	1439	15	1412
BBA57859.1	0.0	4	1376	7	1378

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	1.33e-91	351	1112	12	720	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
7DUP_A	1.86e-14	456	741	29	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]
7DVB_A	5.64e-14	456	723	29	303	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_C Chain C, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_D Chain D, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
6YHH_A	5.72e-14	462	741	38	317	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
7CBN_A	9.93e-14	504	684	72	252	Crystalstructure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835],7CBO_A Crystal structure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila in complex with GlcNAc [Akkermansia muciniphila ATCC BAA-835]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	9.56e-97	351	1112	34	742	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
Q9HGI3	1.12e-15	418	919	9	554	Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA PE=1 SV=1
P43077	2.09e-14	504	918	105	513	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
B2UQG6	5.60e-13	504	684	91	271	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
P13723	1.62e-12	509	814	100	392	Beta-hexosaminidase subunit A1 OS=Dictyostelium discoideum OX=44689 GN=hexa1 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
0.000248	0.999150	0.000142	0.000171	0.000147	0.000135

TMHMM  Annotations     

start	end
7	29