CAZyme Information: MGYG000001304_00116

Basic Information

• Species: Erysipelatoclostridium spiroforme
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium spiroforme
• CAZyme ID: MGYG000001304_00116
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1582		174590.61	4.2871

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001304	2507485	Isolate	not provided	North America

• Gene Location: Start: 144210; End: 148958 Strand: -

Full Sequence      

MKDVKIKVANALLVGGMVLSTVSPQLLGVQARNDAAALLDTEPGTTDLVNLAKGKTATAS
EEESGTEFKATKAVDGIVNRDAENKADQSRWGTSQLNGTEEAWLKVDLGETKTFQSFVIA
WERQNITEYQIQTSNTGDGDWETVYTKDGNGEISDVVETIHLDEAVTAQYVRLLVTGYNG
KYVDGNPDADWKSVSVYEFQVYENDIPDDLLPDENYNREGKATASNSESGTSFTPDKAID
GNTKDKASRWATDTNSSNLARTLTIELPVSQRVRSFKIFWERANIEQYTISVSNDGTSYE
DVYTSSEAVSETEEVITLDKAVWAKYVKLNVTKYNGGNNNWPNVSLYEFEAYANVPKVES
PDIEPDDTAKEAAAKLKTAPTFNEDQTALVLPEVPEGFKVEFLADLEQIVAKDGKIYQPL
TDTAIKGIYKITKGEETAESTTELALTIPGIHETAGENTKPTVIPELAEWHGESGDFKVK
ASTRLVIDASAKDIATKAAQAFQADYKEASGKELEIVTDETAKPGDIFFTKDTTNNLGKE
GYIMDIDDIVTIKAEQSTGAYWSTRSMLQILKLEDDTMPKGLTRDYPKYSVRSFSLDVAR
KPVSMETLNSIAKEMAYYKMNDFQVHLNDNLIFYEDYGSVETAMEKAYTGFRLESDIKKG
QVIEGDSKGVANAADLTSTDLSYSKKEFREFILDSREMGVNIVPEFDAPGHSGAFMDVRP
DLHLKKTVEGNAARAGEQFDLSDEHYADSSNFVKKLWDEYLTEDMFDSSMVVHVGTDEYY
GDAEAFRKFSDDIIEHVQETNPTVRMWGSLSHKNGSTPVRSKNVQMNCWYNPYAQPKDMY
EQGYQLINTVDGDLYMVPAAGYYGDYLNTQRLFNNWQVNSIGGVEISAASEQMLGSTFAI
WNDSIDTRANGISEVDIYDRFIQAVPTLASKNWGDAKETTYAELTETVEQLGDAPGHNPY
HKASAKDGKYMEYKFEANDTKGDASENNRDLLTDVNAKFEKGALTLSGDESYVTTPIEKL
ATGNTLEFDITLNQEAKPGEILFEADAPGNERYVHDIRILDDGTLGYKRELYDFSFGYKL
PVGQKVHLAISTDGIRTYLFVNGEKYNAVGKYVDETGEVKQENIKPGLSLGNNNGGYGVG
TLLLPIQRIGSTSNAIDATIDNVVVSEGVQKDTTILDGKTFTVTTNNEQSDMGTEGPISY
AFDGNLSTIWHTSYSPYKNLPAEVIVDMNKTYDINKLTYIPRSSGTNGNITKYSLYYQVE
NSDEWVPIIEEGTWDGNGEEKIIKFDQVTARKLKFIALDGVTNNPGKPFAAAAEFYVHQV
VSDQPDVEADKELLSIAIAAAKEITQEHLDTVIPVVAKEFKEALANAEAVYADDKATQEE
VNNVFDRLANAMHMLDFIKGDKASLKTFIDKVSGLESSKYTEDTWTPFNDALTAATNVYN
DENAMQEEINTVYTELVKAFVNLRLIPNKDLLEDLINQANGLNVANYTKASFDGLTKALN
EAKAVFDDPNATQEQVNSAKDVLAKAMAGLQTVTTDNTVSTPVSNGDTTVSVKTGDDALV
GTLAGLALLSIAGAKVLRKKED

Enzyme Prediction     

No EC number prediction in MGYG000001304_00116.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	582	934	8.7e-57	0.9762611275964391
CBM32	222	350	2.8e-21	0.9435483870967742
CBM32	58	200	5.5e-21	0.9354838709677419
CBM32	1185	1316	6.5e-21	0.9435483870967742

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	6.70e-135	591	935	2	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.
pfam02838	Glyco_hydro_20b	8.66e-22	460	585	1	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
cd02742	GH20_hexosaminidase	5.02e-20	592	934	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.
pfam00728	Glyco_hydro_20	8.59e-20	589	910	1	326	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	2.15e-17	420	933	80	621	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPS14026.1	0.0	49	1571	43	1515
QQY27155.1	0.0	49	1571	43	1515
QMW75640.1	0.0	49	1571	43	1515
QQV05894.1	0.0	49	1571	43	1515
AYE35153.1	7.22e-282	222	1523	44	1462

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	1.39e-113	397	1104	26	679	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	4.18e-30	450	952	22	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]
4A41_A	5.09e-28	1184	1317	33	159	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]
2J7M_A	2.05e-17	1179	1318	9	148	Characterizationof a Family 32 CBM [Clostridium perfringens]
2J1A_A	2.11e-17	1179	1318	10	149	Structureof CBM32 from Clostridium perfringens beta-N- acetylhexosaminidase GH84C in complex with galactose [Clostridium perfringens ATCC 13124],2J1E_A High Resolution Crystal Structure of CBM32 from a N-acetyl-beta- hexosaminidase in complex with lacNAc [Clostridium perfringens ATCC 13124]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	3.95e-118	369	1104	22	701	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
Q0TR53	2.84e-17	1165	1386	613	822	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	6.42e-17	1165	1386	613	822	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
P26831	2.33e-14	1203	1565	1247	1599	Hyaluronoglucosaminidase OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagH PE=1 SV=2
P0DTR4	3.66e-14	1194	1318	526	644	A type blood N-acetyl-alpha-D-galactosamine deacetylase OS=Flavonifractor plautii OX=292800 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
0.092189	0.898940	0.007688	0.000546	0.000309	0.000302

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001304_00116.