CAZyme Information: MGYG000001400_03523

Basic Information

• Species: Erysipelatoclostridium ramosum
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium ramosum
• CAZyme ID: MGYG000001400_03523
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1746		197287.71	4.5429

Genome Property

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

• Gene Location: Start: 35891; End: 41131 Strand: -

Full Sequence      

MHRGKISKIFINQRKGRIMEKILRKGFISLLSLLMVFTTFNQLITNVAAEQEYENIALDK
VVVASSAIAGNEGSNAVDGKIDTKWEVGNISTNPSIIVDLGKEESFEKITLKWASNFAFR
YKLYVAKADQKYGQVLFHEEGTGGDEEWEMEENTIARYVKIELIEAKSGESTIGLKELEV
LRVKKDTSNDPVNIALNKPAYASGNEANLDRLGPGGAFDGKYSNDYNERWSSGNITKSPQ
WIYVDLEAEMTFSSIHIFWENAFATKYVLQYSNDVGTDKNWITFVNVDDGKGSWEKFDFD
PITARFVRLYATASNGVGSAKSISIWEMEIYEEVNNSLTVDDIAKDFTIGTITSNMDKMP
VYHYDNDNIVAEIFCSDTDFVVEDNGMIHKPLVDKEVLVTYIIKDKRTNATKEMKNIPVI
IPGQNSVALDSNPVPTTVPTIQEWNGATGTYQLTNNSRIIVQDESLYKAAQITKDDIKDL
FGLELEISNTTVKKGDILLTKENADTTIGDQGYTLEIGDSITIKSTTYQGIFFGTRSVLQ
ALVASGDALTINKGEARDYAKYEYRKFMLDVARKYMPMWYLKDFVKYASWYKFTDIQVHL
NDTSYNGHSRFRLESDIPGLTATDGYYTKGEYRDFQYYAEDYGIRIVSEFDTPAHSAVFI
DNNSELGFDGTHLDIRLNSDKKETVYKFIADLYEEYMGGDNPVFVTDAFNVGLDEYNSAY
KEDMTQYTQYVMDLVYNKYGKTPMAWASMGCVDSDKTKIPDYPIMDAWANYAISLKSLFN
QDYKLINATNKYGYIVPGGNNGYPDFAKEEEMYNNLSAGKFRDKMGAGVDVAEGHPKIVG
GSISLWNDRGIFNGISVYDVFARIQSILPIYAQTFWYGKDNDKSYDQFKAEVNTLGTGPN
VEMDKEISSKTEKVYDFDMENTSKQGDNLVIKDNSGNGYDATAIKATVETTDEGRALKLN
GDGYLQMQHSALKWPYTLAFDLKIDESQTGDIVLFEETMPIEECNQWIDTKYQTRKIYLK
EIDGKYKLMYDRDSYHYEHNIELEKGKLYQLAFTSDKKYTNAYLDGVVKSTINGPILTNS
GNKWYDSASINLPLQKIGQNLVGTLDNIKVYNRLLNNEEIKNLYDTGIDVIHENVALNKK
ATASSSYTDYQTPNKAFDGIINQSASGPEQSRWASARTHDQWIQVDLNKVYKVDQIKITW
EDAYGVDYELKGSVNGKDWFTIKNVTGNVAKENNHTGLGDIEARYIKLIGTKAANNAKYG
YSIYEIEVYENPKNDLLRTISQVKDKLSEMNVGNFHGQIKEEAYQTFTAYLTNLENEVVG
KESISEEEMLKFKEELSKKYTNLKKQVVRVDKSALETVLEVAESKLAEGYSEANSTVSSW
QSFIQNKEAAEAMADRMDITQSDVDKMVSELQTALDNLTFRALESSFNELVALIDEVAKM
ETDYSAEMFKVMKGYLDQANALVALGAGEVVEKDVQANLTNLANEKAILISYRELKVSVE
VAKEILDKEAVNLRPATLKVLQDAYEAGRKLIDDNSKELIVLQNAKQEINEAIEGLLEIV
ERKDLDKLIEQVKDLKEEDYTEESWKTFKNGYERAVIVNQDLDANEGAIQNAYDELLRAF
NELKQVVNKDNLLLQIELAKQVLANKDKYDIELVKELEELLSQAVALIANDVSSEDVNKM
SDALLTKIEAVKASQKEEPKVEEQPGTEVSDKTKKNAKTGDETMLFEFAMISLVALLAVV
RLRKKS

Enzyme Prediction     

No EC number prediction in MGYG000001400_03523.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	557	877	1.7e-46	0.9703264094955489
CBM32	1140	1267	2.6e-24	0.9435483870967742
CBM32	212	329	7.6e-20	0.8548387096774194

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	2.99e-99	563	878	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	1.91e-30	564	867	1	297	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	3.26e-25	562	846	1	317	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
pfam00754	F5_F8_type_C	2.47e-20	1140	1266	1	127	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
cd06568	GH20_SpHex_like	3.66e-20	562	762	1	210	A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. 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. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQY27138.1	0.0	1	1746	1	1746
QMW75623.1	0.0	1	1746	1	1746
QPS14043.1	0.0	1	1746	1	1746
QQV05909.1	0.0	53	1746	333	2020
QQY27139.1	1.01e-184	53	1648	333	1915

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	3.79e-50	343	899	3	569	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	2.81e-21	435	896	34	494	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	1.10e-19	431	746	35	375	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	5.28e-19	193	331	7	135	Solutionstructure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis]
4ZXE_A	5.44e-19	193	331	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	2.44e-53	343	899	25	591	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	2.38e-11	362	715	89	435	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
P29416	1.39e-10	511	768	114	391	Beta-hexosaminidase subunit alpha OS=Mus musculus OX=10090 GN=Hexa PE=1 SV=2
Q54SC9	5.68e-10	510	849	108	454	Beta-hexosaminidase subunit A2 OS=Dictyostelium discoideum OX=44689 GN=hexa2 PE=3 SV=1
Q0V8R6	9.62e-10	511	768	114	392	Beta-hexosaminidase subunit alpha OS=Bos taurus OX=9913 GN=HEXA PE=2 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
0.201261	0.780775	0.014007	0.001335	0.000882	0.001725

TMHMM  Annotations     

start	end
27	49
1723	1740