CAZyme Information: MGYG000003087_00360

Basic Information

• Species: Merdibacter sp900543035
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Merdibacter; Merdibacter sp900543035
• CAZyme ID: MGYG000003087_00360
• CAZy Family: GH89
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2145	MGYG000003087_5|CGC1	235877.09	3.8387

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003087	2304658	MAG	Spain	Europe

• Gene Location: Start: 44525; End: 50962 Strand: -

Full Sequence      

MHYLRKGCMLILAGIMAVSGAFGTMGGMQVKAAEDPQIDGIEASGKSTAGHEAALAIDGA
VDTYYLTPSSSSMEDYYRYIDLKLDGLYHITKIEIFNQTNNTYNHHEIYASQTGAEFNKI
AYKADDDLADAEGDVYTVDVDASQLRINLSYNSAQMEGNLAEVKVYGTRIGDAQTYETNI
ETTDFSETQWAEEYERFENDEEYANQKTINEMSELVGRVIGDEWKDDFVFALREDNSDGK
DIFEVSDGEDGKILIRGNNGVAMASGFNYYLRYYCKVDYNPLFASQLDMPDTLPAVGESI
VKETDYDVRYALNFCTYSYTMAFWDWDEYEAFLDWAAMSGINLMLDIVGQEEVIRRTLQD
YGYTDAEIKEYLCGPAYFAWYYMQNMTGYGGELPDSWFENRVELARKMHDRMQTYGITPV
LSGFSGMVPTNFDEKYTDATVIEQGTWCGYTRPDMLRTYVDDGQKDYFSEMADYFYQNQR
DIFGDVTNYYAVDPFHEGGRTGDMDVSLVYETVQQKMIENDEDAIWLIQQWSGSMTDAKL
SGLKVKDQALVLDLFSEINPSYSVMERNDIPWVWCMLHNFGGRMGIDGNPDDVSQNIPDD
HQSTEYMQGIGMTPEAIENSPMMYELLWDMTWTKDPIDYREWVQDYAERIYGGTNEDIQR
VWEIMLETGYNSKDTYYQGAAESVINSRPTTNFTSASSWGHSDINYDKELLEEAAALMAK
NYDTFKDSPAFVYDFVDILRQVVANSAQEYHTEMVSAYQNGDLELFDAISSDFLEMILLQ
DEILSCSSDFLVGTWIEDARSMVADSDDWTKDLFEFNARSLITTWGGYKNANGGGLRDYS
NRQWAGLTKDYYYPRWEKWVNDAKAALTDGTAMPSTNWFLMEFEWANEKSDQGTAYATEA
SGRDLKALSQQVLDNYTIADLEELVETPSTQSENLALGKSVNASIATAEGSSTDLLTDGG
KETLWQAAEHADSFTLSINLEEEAQISGMEIDMQQIAGGFPYSYVVEAYSDGAWQIVAED
DSGEITSQTLIDWQGIASAVRFTFTSDDASIVPAVAELIVYGVQQEQKNYENVALGASVT
TPTGETSLITDGDTGSLWVSNGDYYPAQIVLELDEEQYVDIMELYFEKPGLRYQYDVIIE
DAQGSQTTVQDMSDNTQDLAGMYTIEIGANVKKVYVNLKARAEGGEFYLAWPALAEIELL
QEQAVRFMGADVASGKTSQVINANGTVDTDILTNGSTSDLYNVGSDVFPTTFQTDFGREE
SIEQVVVHFEKAGLRFQYRVILEAEDGTQTVIQDMSENTADMVQSYTITLDEAVKARKVL
VEISGRAAGGEFYLASPALSEIEAFATAENVAADAQITTDPQLSDEDLQKLLDQDSATSI
TLAEDGTQVFEFQLPQEIDLYAYEIIKKSDAPLRFQIETKLGDGEWQMFVDRSANTSDAD
RYVETLDAVLCDSIRLTVNAAGDELQDIAFYSSNQSAELLSYISDLRSKVNGTTVGEYAG
NYGQAQYDALQAAITAAEELAAGEMTSMAVSAQKEVLSEAYRNYLLSYVSIDRGALLREL
NEAEILMSHADLADNEALNAAYDSARTVYETYKVTQAQLDDAQQALAAANDTALALLEGK
EALQAQIELAQQLLDSCAVGSDTGNVSQEAHDALAAAIAKAQDALDSTDASVLSQAAEEL
KQAAETFTDQIITTDKSELNEWIAKAHALQGSAYTTDSWAALETALAQAETILAQSDSQE
EVDQAAADLQNAMNALQAKASASALNALQDMVGKAEALGSDDDALNAAITAAKALLADPD
NASVTAVVSALLDLSEALQDLNGSSDVEALRADVQATIDFINEHILSNVEGLRPAKVQAL
KDAVAAAEELLASEDATADALKAANKAMTKAAQELWEIVSKTELNALIEAANGYLDGSYT
TESLEALQAAIDAAQAVAINDDATTAEVTDAITNLSSAIAGLESITLDTSALEHEIELVS
EMIANIDNYVPSSVEGLQDKLDAAQNALNTAASQAEIDEAVKTLREARLNARTKADTSAL
EEIIAYANSLDLAGYTVESRNMLDRTIVAVKRVLADPEATQEEVDQAVQTMQIAIDGLQL
VENSTGSTNADTTNTAAAAQTAAFAGMLAVSAAGIFLFRRKRQVK

Enzyme Prediction     

EC	3.2.1.50

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH89	250	910	1.3e-227	0.9909502262443439

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam05089	NAGLU	2.21e-138	309	634	1	333	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	4.87e-87	642	910	1	258	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	7.55e-25	210	294	1	81	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.
pfam07554	FIVAR	1.86e-05	1696	1756	4	68	FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
pfam00754	F5_F8_type_C	0.001	940	1046	1	114	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
AYE33274.1	0.0	56	1962	60	2131
QAS61445.1	0.0	56	1962	60	2131
ABG84150.1	0.0	12	1752	1	1920
AMN32327.1	0.0	12	1752	10	1929
AQW23250.1	0.0	12	1752	10	1929

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VC9_A	0.0	39	925	6	886	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]
4A4A_A	0.0	39	925	29	909	CpGH89(E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactose [Clostridium perfringens]
7MFK_A	0.0	39	925	14	894	ChainA, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124],7MFL_A Chain A, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124]
4XWH_A	5.59e-93	215	872	12	664	Crystalstructure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens]
4A6O_A	6.13e-27	1058	1200	14	160	CpGH89CBM32-4,produced by Clostridium perfringens, in complex with glcNAc-alpha-1,4-galactose [Clostridium perfringens],4A6O_B CpGH89CBM32-4, produced by Clostridium perfringens, in complex with glcNAc-alpha-1,4-galactose [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9FNA3	4.39e-93	252	916	94	804	Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1
P54802	2.89e-92	215	872	35	687	Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2
E8MGH9	1.32e-11	1899	2142	1666	1932	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
0.000557	0.998423	0.000368	0.000251	0.000196	0.000166

TMHMM  Annotations     

start	end
7	29
2116	2138