CAZyme Information: MGYG000002014_00477

Basic Information

• Species: Merdibacter sp900754715
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Merdibacter; Merdibacter sp900754715
• CAZyme ID: MGYG000002014_00477
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1952	MGYG000002014_13|CGC1	217378.83	4.0672

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002014	2253473	MAG	Spain	Europe

• Gene Location: Start: 1029; End: 6887 Strand: +

Full Sequence      

MNGKKMMKAALAVGLSVTSVLSSVSIQTLANTQTVSETNSEKENIALNKPVTSTQIEHSS
YASYAVDGNENTYWASVNPAELEIDLQGYYKIDEMNLMAYFDPSTGAVDRYYEYEIYASM
DQEEYTKVAEKKDTAFETPQGDTYTFEETFTARYIKIKFLSTHAQGQPQNNTAHIKEFRV
FGELDPDVEQPQEKQNVALGKMAYAPSNEGSNDASKAVDGNKGTYWAGPNPTYIEVDLER
YYDIDEITVIPYYGDGRCYHYEVYTSVDGYEYEKVGEKTSDEAQTADGETYAIEGKTARY
VKIEMLSNSANPAVHVNEIEVYGTENSEYEPPEEDNEGNIAMSKPTRSYSDNTAHPASAV
NDGQRSTSWTGLYYPAYVDIDLEQNYNLNKIVVMPSYSNMNAYYQYSVYTSMDGVNFDLL
VEKDDKEKVKKEGDTYVIDGKEARIVRLYLQYASSGNTGSFQEIKVYGEASGTPLQERAP
ISVSDFEDTTYAQPVTEEETISEVRGVLGRVIGDRYQDWFEFALAENSESDNDYYEIRNH
EGKILITGNKGLSLTTGLNHYLKYYCNVSVSQQTRNVEMPAEIVPVEEPIRKETPYQIRY
AYNYCTHSYTMAFWGETQWQNELDWLALNGFNAILDITGQEEVWRRFMGELGYTTDEIKD
WLVGPGYFGWQYMANMENVNGPIPDNWFAQRTELARKNQRKMRALGMTPILQGYSGMVPN
SIQDKDPSAQIIAQGQWNGMQRPAMLKTNTATYQKYAQMFYQAQKEVYGDVSHFYATDPF
HEGGNTGGIGRDIVGRAVLDEMKAYDSDAIWVIQSWSFQPELLQNITAEEKQNNILLLDL
NATKGARYSSTDEFAGSNWVYCMLENYGGRSGINGNLQKYTTIPSQIKDTTEHMVGMGIS
PEGTNNNPVKYDLFLEMMWEEEDIDLNEWLTHYIERRYGELSEGAQKAWEVLLETAYQNS
SNYADPPESIINARPAFDITKAAPNGNTGRSYNTKRFEKAVEYLMEDYELLKDNEGYLYD
LTDLLRQAIANSAAQYYQDFTAAFEAGNKEVFDQKAQAFRDLIDLQDRVLNTNENFMVGK
WLNASTEAAEGQDEFTQMIFQLNGKAIISTWAPYYCWGVYDYANREYGGLTRDYYLQRWQ
LWIERLNDKLNGEDVSNYQEISTAESHAIAWEWARSDKVYSDEPTGDIQALYEEFKANYS
LNDQEEDELKVDQLDIRISTDLPGYNGHPLSNAIDGNSATFWSSAYGDLEPYEVFFEFDQ
PETISTFSILPRDYDNRRTGNGDILGIELWVSDDGESYRKIAEGQYPEDGEERRCTFEPV
TTKYVKLVITDFLIWNNNHAIKSVTAGEFNFYRPYAMLESDVYSFEDGEIKNVAEGTSVA
QLRNQIEVSQRGSLQVMRGEEELDDDAVLQLGDVIAYYYDDALAQSYEIKAFSEPSDFSA
LNALIAECEKLNENDYTSESWKAFSEVLTVAIGVQVNPEATQEEIDEATADLKAAMADLV
PNVDLSGLRAAILEAEALTEADYTKTSWNALAEALAAARTIAEDQHVTQAAADQAASALR
TAMAALQIKASDAAMAALQNIVDSAQALQNEALSEAIAAAQGLLADPDNSSTTAVVTALL
NLSEAIQAVNTGESTDALRADVQATIDFINENILTNVDNVRPGKVDALEAAVEAAQTLVD
DPDASADALKAANKAMTKAAQELWQIVSKAELEALIEAANGYTDGSYTAESIAVLQDAIT
NAQATANNDDATTAEVTDAIMNLANAIAGLEQIMLDTSALAHEIDLVTEMVANIDDYVPS
TVEGLADKLADAQAAMNATTQEEIDAATATLREARLNARTKADISALAEIIAYANSLNLT
GYTAESRNMLDRTIFEVKKVLADPEATQEKVDEAVTTMQDAIASLVPVQESTDSVSAGSA
NTAAALQTGLFAGMMAAAAAAALHLHRKKQAK

Enzyme Prediction     

EC	3.2.1.50

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH89	541	1192	8.5e-209	0.9879336349924586
CBM32	58	178	1e-20	0.8709677419354839
CBM32	207	319	1.3e-20	0.8870967741935484
CBM32	1226	1335	4.5e-17	0.7661290322580645

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam05089	NAGLU	2.58e-132	599	919	1	331	Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This central domain has a tim barrel fold.
pfam12972	NAGLU_C	1.50e-70	929	1187	1	252	Alpha-N-acetylglucosaminidase (NAGLU) C-terminal domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This C-terminal domain has an all alpha helical fold.
pfam12971	NAGLU_N	1.17e-22	502	581	1	78	Alpha-N-acetylglucosaminidase (NAGLU) N-terminal domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This N-terminal domain has an alpha-beta fold.
pfam00754	F5_F8_type_C	2.26e-13	50	163	1	116	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam00754	F5_F8_type_C	1.26e-11	207	319	7	127	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNM12248.1	6.62e-209	557	1563	2	1027
AYE33274.1	1.33e-199	335	1244	33	964
QAS61445.1	3.44e-199	335	1244	33	964
AMN35090.1	2.56e-192	357	1242	55	962
AMN32327.1	2.51e-191	362	1242	60	962

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VC9_A	1.44e-199	362	1152	26	830	Family89 Glycoside Hydrolase from Clostridium perfringens in complex with 2-acetamido-1,2-dideoxynojirmycin [Clostridium perfringens],2VCA_A Family 89 glycoside hydrolase from Clostridium perfringens in complex with beta-N-acetyl-D-glucosamine [Clostridium perfringens],2VCB_A Family 89 Glycoside Hydrolase from Clostridium perfringens in complex with PUGNAc [Clostridium perfringens],2VCC_A Family 89 Glycoside Hydrolase from Clostridium perfringens [Clostridium perfringens]
7MFK_A	1.84e-199	362	1152	34	838	ChainA, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124],7MFL_A Chain A, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124]
4A4A_A	2.14e-198	362	1152	49	853	CpGH89(E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactose [Clostridium perfringens]
4XWH_A	1.31e-86	497	1199	2	711	Crystalstructure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens]
4A41_A	6.82e-09	1233	1328	50	143	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P54802	8.01e-87	497	1199	25	734	Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2
Q9FNA3	4.20e-86	502	1199	47	804	Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1
Q8XL08	4.89e-07	1219	1403	635	802	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
Q0TR53	6.41e-07	1219	1403	635	802	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
E8MGH9	1.65e-06	1435	1663	1665	1882	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

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
0.000300	0.998920	0.000243	0.000184	0.000163	0.000142

TMHMM  Annotations     

start	end
1923	1945