CAZyme Information: MGYG000001400_03524

Basic Information

• Species: Erysipelatoclostridium ramosum
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium ramosum
• CAZyme ID: MGYG000001400_03524
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1946		216711.87	4.3893

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001400	3785853	Isolate	not provided	not provided

• Gene Location: Start: 41421; End: 47261 Strand: -

Full Sequence      

MRRTKRIIASLVAAVTVISQVMPMMKVTAATDNVRLATFNIAANKKPDITKLNELLKTNN
VDIVGLQEVDINTSRNPYNMLEKFVEQGDYAYSSFQKAIETGGGDYGVALLSNLELINTN
GGALNSEGIKEARAWQKGEIEINGKVIAVYNTHLTYESVEARAKQLLELKATMDQDPAEY
KVAFGDFNVDQNHNEIYPFLEDYNIANGKGGKWYDTFNGTDASMKTSAVDNIITSRNLEI
SNITMVETDLSDHNLFYADAKLLDQPVASRDYLDLVISDANALDEGKYSNASYNTLDEKL
VAGELLDQNATQEQINKAVKDIQTAQDNLKTRYPNLALNKDVSVSGLEVNDGRWTAPMAV
DGIVSSDSRVSLAKDKDEQWLEVDLGKTETISNFVINYESQVPAFKIQVAGEDKVYRDIY
EVSNLEGQISNIQKISIDPTEARYVKYVQLKRWTHSGNGKQYSGSIYEFEVYEQDPDAKD
YSNIALNRPVSASSLEVGDGRFTAPMAVDGVVSKDSRVSFGKTADNQWLLVDLGSRKTVS
EFVINYESCPPAFKIQVSTDGVNYQDVYEAADLPDGGPSEIKEIQIEATKARYVKYVQLK
RWTHTNKNKYSGSIYEFEIYKERDHTVTTADEVLKSLNKEAPQINGNKIVLPAVPDGFEI
SLYGCDNKQVVAMDGTITRPLEDMDINVLYQVKNLNDETDIAYSEADINFIVPGAYNKEE
SINAKPNVMPGLREWKGNEGEFTLSKNSKIVVKDASLEATAKQIQFYLKEMIKHELEIVT
SGEKSGDIVLVKDGSVDNLGKEGYTLAIDDMIEIKSNYETGILYGGISITQMFSQNDGMN
NVAKGLARDYPKYEVRAGMLDVARTYIPMEYLQEMTIYMAYYKLNEVQVHVNDYWGATGY
SAFRLECDTYPMITATDGSYTKEEYRQYQIDMKNYGINVITEIDTPYHAECFRNVPGVKM
LKAGALDIREQSSYDVIEAVLDEYLDGPNPVIQSDKFHIGTDEYDKSYSEQMRKWTDHFI
NYVNDKGYDTRLWGSLGSRGFNGTTPVSNDATVNLWAPYWADVKETYNAGYDIINTCGGW
LYIVPGANAGYPDRLDIASLYDKFDVNNFSPSRNAGQGTAIMPIAHPQTKGGQFCVWNDM
TSYGGGFTWFDIYDRFIDAVMVTSEKTWYGEKTDGQTADEFVERANKLNSVVPGANPGRV
VESKGENITAIDFETIKNGKAVDTSGNNYNATLNNAIIEKANGNNIATVNGDGYVALPYK
SIGYPYTVMMDIKLDSNTSENTEIFSGDDGVMYANIDGTGKIGYSRSGYNFTFDYELPKD
TWVNLALTCDQKNTTLYINGKVITTGINMGTAINNRKDSSTFVLPVEKNLNNAKGSVDNI
KIYNKTFSATEISDELGYIQLENLALNKNATASSVNPLTPNLTPNLAVDGDNTKVTTNRW
SSKRATGAGTNEGDTEYGTVEQDLTVDLGANYKVDKVFISWEGAYATKYTIQGSLDGVNF
FDIKDITNGTGGEITHKDLGDVETRYVRIACHDAKNRNWGYSIYELEVYQSTNEGLRALV
KEGQAELAKFDAGNKNGNIAKDDYKVFEQKFEDYLALADGTEISTEEIGKLLKEVTAIIN
SIEDSVIYSKNELNELYQKVSLYQEKDFTKDSFVDFNTKLTAIKGLIDNADDYIKVNEAM
GQLQTLDSSLVKLDRSKLKTAIESYDNFQETDYTTSSWQTMKTIVDAAKLVHENVSLNQV
DVDNAIAALNEINLEKRGNTKELAKLLKEYDEADYTISTWAEFAGVYQAANAMVVDNSDV
NQEQVDAMVALVREAAMKLLELGNSKDLEKVINKITEAIKDLDQANYDQDSWNKLQTMIK
AAKELLDSKDVSQAELDAMLDSLNQVYDALKPIEVKPGEETETPTNKPVTDTSDKSVKTG
DDVNLFGYAGLLGIALMGLICRKKFD

Enzyme Prediction     

No EC number prediction in MGYG000001400_03524.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	846	1169	4e-47	0.9762611275964391
CBM32	1412	1547	1.7e-22	0.9596774193548387
CBM32	492	618	5.9e-19	0.9354838709677419

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	6.30e-105	854	1170	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	1.72e-27	856	1139	2	278	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	2.25e-24	853	1137	1	317	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	6.11e-22	853	1137	1	316	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	1.18e-18	695	1139	102	589	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW75624.1	0.0	1	1946	1	1946
QPS14042.1	0.0	1	1946	1	1946
QQY27139.1	0.0	1	1946	1	1946
QQV05909.1	0.0	1	1944	1	2018
QTY17007.1	2.90e-270	608	1891	19	1462

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	1.50e-61	632	1197	2	573	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	9.80e-21	716	1168	23	474	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	1.37e-12	724	1003	37	345	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]
2RV9_A	3.76e-11	1403	1549	7	135	Solutionstructure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis]
4ZXE_A	3.85e-11	1403	1549	8	136	X-raycrystal structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5. [Paenibacillus fukuinensis],4ZXE_B X-ray crystal structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5. [Paenibacillus fukuinensis],4ZXE_C X-ray crystal structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5. [Paenibacillus fukuinensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	6.82e-65	630	1382	22	753	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
E8MGH9	1.05e-12	1693	1944	1666	1931	Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 PE=1 SV=1
E9DFH0	3.85e-12	802	1116	122	475	Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 SV=1
A7WM73	7.11e-11	776	1031	95	356	Beta-hexosaminidase 1 OS=Arabidopsis thaliana OX=3702 GN=HEXO1 PE=1 SV=1
B2UP57	3.31e-10	783	948	39	214	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

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
0.000287	0.999002	0.000185	0.000178	0.000175	0.000154

TMHMM  Annotations     

start	end
7	24