CAZyme Information: MGYG000001027_00048

Basic Information

• Species: CAG-56 sp900752065
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-56; CAG-56 sp900752065
• CAZyme ID: MGYG000001027_00048
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1574	MGYG000001027_2|CGC1	175772.4	4.9253

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001027	2760146	MAG	Sweden	Europe

• Gene Location: Start: 13546; End: 18270 Strand: -

Full Sequence      

MKKKAAKCFVPVLALSLLCQNLGTGLPVKAADTGDSKITIAAENISAKNASGHEAAKAVD
GDSSTYWQSIPSNGEGDDYKRMYDHNRYIDITLDGTYSLSQIKIFNKVDNSFNNYYVYAS
ADGVNYEKIISKTSNTAADAAGDSFSVATEASYLRLNMAYNSNSFATNLAEIEVYGTKIS
DTVVQPPEIQVEDWEGSSWQKEWDRFETDEAYAKEKTLKEMSNLVGRVVGEKWKESFRFE
MRDTLKDGSDVFELKDGGDGVIVIRGNNGLAMASGFNYYLKNYVNVDYNPLYESNVDLKE
LKPVGKRVVKEAQFDIRYALNFCTYSYTMSFWNWDEYEEFLDWCAMNGINLVLDIVGQEE
VLRQTLREYHYSDEEIKDYISGPAYFAWFYMQNLYSIGGPLPDAWFAQRVELGRQMHDRM
QTYGISPVIQAFAGQVPETFAQKNEGAVLTPKDGWSGFTRPSIIKTYLTEAEAAEGKVNY
FADVANTFYEKQKNVFGDVSDYYAADPFHEGGATGGLDIANIFKTVQDEMLKSNPNAIWV
IQHWQDNQKGTKMSKMDKSKTLSLDLQTDMNPQYGVFENQGSDWIYCMLHNFGGRMGLDG
EVPVIAANPVETYNNTSHMKGIGMTMEAMENSPVVYELLFDTNWSKDPIDYEAWIEKYRQ
RRAGGDSESLEKAWDILLETAYADKGIYYQGAAETVINCRPGDSFNSASTWGHSNIRYDK
AQLDKALLLLADNYEKFAASPAYKYDLADVAEQVLCNAAVEYHRLMVSAKNSKDTEKFKN
LSTQFLNLIDLSDKILSVTDEFMLGTWIEAARKMIPGADDWTKDLMEFNARSLVTTWGGE
RVGSLKDYSNRKWAGLTSSFYKERWSIWVRNRIAELENKTKDAADAKAESNWFLWEYQWV
NRKSDDENGKYSFSTTPSNADLYSLVMKAYTDFSYTKLEENTGSTTVERVNAAQGKKVTS
SSATQSGTLSNITDGDTATEWVAVGEGPHTLEIDLEESCEIESVTISIPQLAKLFPYTWK
LEYYDPAAGNWTDWKEYTGREMESNVNVVAASSIQASKLRLTMTTSDTANSPVTITEVAV
YSKGSSEEIQYTNLAKGILPTTNKGNTASGYPLSNITNENTGDLWKTDDWGSSAYPAWVE
VDLGSARDVKYAEVWFESAGRPFQFYVAAVGEDGTETTIFDEYKDHTGVLNQASYRIDIP
ESLGRVQKVKVYLNGITGQGQYGQSGPALSELKIMGVGEEGEEPVPEKNTFDRSDLLAKI
VDAQELMAKMEKFGKTEGKEELQRLCVEVRSVYDTYTSTVEAQKEVLASLGGKMDEISPK
VEEAALVVVKEELQDALTETSGQVTGTKGDYTVESWAQYQAALEKVTKLLANPTTSEELE
SARLELLEAAGALKKANKPQQPIDTPVKTEPEKPQPDKPETPKPQPSLPKNGEKYTVGKF
VYKVTASSEAKKTVTLVKPVKKNNKKITVPSTVKIGDYSYQVTAVSAKAFRKNAKLTQVT
IGKNVTQIGKQAFESCKKLKKVTIQSKVLKSVGKKAFAGMKAGGKIYVPKAKYKAYTKLL
KKAKTAKSIVIKKK

Enzyme Prediction     

EC	3.2.1.50

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH89	259	905	8.3e-209	0.9683257918552036
CBM32	46	172	1.9e-16	0.9032258064516129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam05089	NAGLU	1.20e-134	317	646	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	8.65e-69	654	926	1	257	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	1.27e-16	219	288	1	67	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.
sd00036	LRR_3	2.22e-11	1467	1539	19	81	leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.
sd00036	LRR_3	7.36e-11	1467	1539	65	127	leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCT45696.1	0.0	19	1240	12	1232
ADP36534.1	0.0	16	1235	3	1184
BBA55754.1	0.0	18	1235	1	1180
AFL05078.1	0.0	12	1235	33	1218
QRI58438.1	0.0	16	1235	3	1184

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VC9_A	1.67e-305	49	943	15	887	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	2.20e-305	49	943	23	895	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	2.93e-304	49	943	38	910	CpGH89(E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactose [Clostridium perfringens]
4XWH_A	1.88e-79	224	869	12	656	Crystalstructure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens]
4A3Z_A	1.85e-08	1091	1206	26	134	CpGH89CBM32-4(seleno-methionine labeled) produced by Clostridium perfringens [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9FNA3	1.09e-85	239	905	64	783	Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1
P54802	1.66e-78	224	869	35	679	Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2

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
0.000403	0.998699	0.000310	0.000209	0.000182	0.000167

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001027_00048.