CAZyme Information: MGYG000003396_03135

Basic Information

• Species: Clostridium sp900766315
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900766315
• CAZyme ID: MGYG000003396_03135
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1607		179764.44	4.2739

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003396	3926186	MAG	United States	North America

• Gene Location: Start: 74917; End: 79740 Strand: +

Full Sequence      

MRGLKKKKIINLSLATMLTFTMLISNVSAYVNTNDEKASEKVNLALNKAAFASSEETNTF
TAKKVTDGIVDREGSKSSRWACERYENGPWVAIDLGQKQSFDEVNITWERRNVNSYKIEI
SDDSENWTSIYVGGGATDFVEAVNVGNQEARYIRVVIDDYSATAENVTWETVSIYEIEVY
GEGTIVDQDPEPGVNIALNKTASASSIETNDFTGNKAFDGVVDRTTTKKSRWASAVSSDP
QWLKVDLGKATKFDSFVIEWERRNSNNYRIQVSDDDSTWTDVYAANKYPANFRENIELSE
AVKARYIRLYIDEHIANSEGVNWNTVSVYELEVYNGGIPEAPKTVSEVANNLVVQELTSE
DTVLTMPSVPEGFEISFVGADYEEVIDYEMNIHKPLVDTNVEVNFEVRKGKEKATSPVIE
ITVPGAHNVEGNKKPTVIPELREWAGKSGNFTISNTSRIVINEESEAKLRETAEVFAKDY
EDITGKEIEVVVSNSPKSGDFYIALNSNYPELREEGYYMNVDDFVSIEANTEQAIFLASR
TILQILKQNEDFIPKGLVRDYPQYDIRGFMLDVGRKPISLDYLYEVVKTMSWYKMNDFQV
HLNDNYIWLERDYSNIGEDAMNAYAAFRLESNDVGENGVSLTAQDLYYTKAEFGEFIDNS
KVYGVNIVPEFDTPGHALAFVKAHPEYAYRDGQGENAAMLDVTNPEVIDYIKGIYDEYLD
GGDDSVFRNATFHIGSDEFYGDSEEYRAYLDEMLKYVRDEKGRTTRVWGSLTHKSGSTPV
TSENIEMNIWNCGWANPQAMYNQGYDLINTDDAYLYIVPGANYYMNYLNSQWLYNNWEVN
KFSNGVVIPQGAKQMRGGMFALWNDMIDKSANGIVEYDLFDRTLPAIQVLAEKMWGEADD
KTYNEFKEVVNEVSLAPNTNPKYEVESKTEKVIEYDFNNVNGNLVEDKSGNEYDSVGLNN
SSIEEGTLNLNGENSYLKTPVKNIGPNYSISFSVNRSTDSDESEQILFESPQGSFKAVQS
ETGKVGFSREGYNYSFNYTLPKGEWVDITIIGKINKTELYVNGEYVDEISKSGSEGKFGT
FVFPLETVGSETNAFKGQVDNLIIANVATIYDETLIPQSQMTITATSEHPNVGTEGLASF
ALDGDEGTIWHTKYSPKDELPQSVTINLGNTYKVDRFTYLPRQAGGTNGIITKYAIYTSI
DGEEFTKVSEGNFENNIKLKTIKFDTPIEANYIKFEALQGVGGFAAAAEFNVYKEKENNE
EKPEVNKTALKFAIDYALEIIENGDLEDVVPAVVREFNEALNEAKKVYENNEATAVEVDA
TFKRLTNAIHMLEFKQGNKEALKNLIDSAEALDEKVYTNESWIKLVEELEKAKSVYNDEN
AMQDEVDKAAESLKAAIDNLVINNVNKEELQSLVDKISSLNKDEYIESTWNALESKVNIA
VGILNNSDATQAEVDKAYNDLLVSYLGLRLKPDKSKLEDLVNKVKEIDLSKYTKESVNNL
NLALATASETLANDEATQKDIDKAISELEIAKANLVANSNESNNSNGSNNSNDNTNKPNS
NGDKGNSNLTNSLPKTGAVVSSAIIIILAVVVVGVGVVMMKKKKTDK

Enzyme Prediction     

No EC number prediction in MGYG000003396_03135.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	558	896	1.5e-63	0.973293768545994
CBM32	200	331	1.9e-24	0.9435483870967742
CBM32	1127	1250	3.6e-22	0.9193548387096774
CBM32	49	177	6.6e-21	0.9354838709677419

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	8.35e-128	567	896	3	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.
pfam00728	Glyco_hydro_20	1.32e-42	567	895	4	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	8.35e-41	566	896	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.
cd06563	GH20_chitobiase-like	4.28e-37	567	908	4	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.
COG3525	Chb	8.32e-31	495	899	187	617	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYE33718.1	0.0	1	1542	1	1677
QAS61873.1	0.0	1	1542	1	1677
ATD55826.1	0.0	1	1540	1	1674
SLK21750.1	0.0	1	1540	1	1674
QBJ76126.1	0.0	1	1540	1	1674

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	6.30e-140	347	1099	2	726	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4A41_A	9.99e-49	1116	1253	25	160	CpGH89CBM32-5,from Clostridium perfringens, in complex with galactose [Clostridium perfringens],4A44_A CpGH89CBM32-5, from Clostridium perfringens, in complex with the Tn Antigen [Clostridium perfringens],4A45_A CpGH89CBM32-5, from Clostridium perfringens, in complex with GalNAc- beta-1,3-galactose [Clostridium perfringens],4AAX_A CpGH89CBM32-5, from Clostridium perfringens, in complex with N- acetylgalactosamine [Clostridium perfringens]
4H04_A	1.09e-39	434	913	33	493	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]
2V72_A	3.03e-35	1107	1254	2	143	Thestructure of the family 32 CBM from C. perfringens NanJ in complex with galactose [Clostridium perfringens]
7DUP_A	2.21e-27	439	908	8	504	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	5.08e-145	339	1099	16	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
P0DTR4	3.66e-30	1096	1253	491	644	A type blood N-acetyl-alpha-D-galactosamine deacetylase OS=Flavonifractor plautii OX=292800 PE=1 SV=1
Q0TR53	2.37e-24	1039	1313	560	826	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	1.21e-23	1039	1313	560	826	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
P49008	8.82e-19	430	738	30	335	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 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
0.000695	0.998498	0.000237	0.000194	0.000173	0.000165

TMHMM  Annotations     

start	end
9	31
1576	1598