CAZyme Information: MGYG000001918_01343

Basic Information

• Species: Prevotellamassilia sp900541575
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotellamassilia; Prevotellamassilia sp900541575
• CAZyme ID: MGYG000001918_01343
• CAZy Family: GH89
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1746		191692.17	4.838

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001918	2523391	MAG	Denmark	Europe

• Gene Location: Start: 193; End: 5433 Strand: +

Full Sequence      

MKHNLLCLRTFCIIAALVCLSTIHTWAASEKNPEAVTAMLNRIGGEGAASRFETVLDASL
TSNGKDAFTITSQSGKPCIKGSSVLAITTGINWYLNHYAHINLAWNNLTTDLSQASLPTP
TTEEKRTCSADYRYYLNYCTFSYSMATWTWERWQQEIDWMALHGINMPLQIIGVDVVWKK
LLTQDLGYSSADANKFIAGPCFQGWFGMNNLEGWGGPNPDWWYTRQEQLAKKILAREREL
GMQPVLPGYSGMVPSDIESKKGYKAYAQGGWNYFTRPYILDPNSQTFTEVAEKYYQRLKE
VMGESEYYSMDPFHEGAQTGDIDVASAYAKIAQAMTKANSTGKWVIQYWQWSYDQNKVLS
NVDKGKLIVLDLYSDAHSHFGEYQGHDAVYCALPNFGARTGFFGRLTKVMTDYFTQKANH
SNMKGVGATPEGIEQVPVLYDALYELPWYASAPDAKAWLANYTIARYGATNTEAQEAWEK
ARNSALNCPSSLQGPQEAVLCARPSLTVDRVSSWGGTDIFYNAQDMVDAAYKLLQAKATI
SGENFSYDLTDFSRQALTDYANFLLKSINDAATRGDQTAYATRRDAFLQLLLDMDQLLNT
NKNFMLGRWTTMARAIADETTGTTESDKQWLELNNARTLITTWGDYNASELGGLRDYSYR
EWGGMLKDFYYNRWKAFFDNRDKGTALPNWYEHDWNWAHNAKLSYSNQPVGSTAEVATTL
FDKYFAILTQADGTPYYLYRYMNTDLTSTFAQKALRGETYTFPLQNVPNGTTASLGIDLN
NDGTISANETFSTLSVAIPANAAIGKVAAKFTLNDGTSLDFKVTLKDDIQADRTISVSSA
DDQQGSVSIEGSNSLSVTGKDEVTMKATPKGGYDFLNWTDAHGNVVSTDNPYTYYGAAGA
TFRANFIVNKWGSPEEDRSEIGVVSDYGQYIKQLDMSQNGSSEQTIYSTDVCPQSLCQTS
QVIKAAKGSQITLHWTSAGGLNYCNLSAYADWNCDGDFDDANELVATAGKKETNDNPELN
DYTLKVLLPYDVPEGITHIRLRLDGAWAKGYDSNGAMPAKAQAMRMVYDVPVKVTSQAST
PCTITVKSADLSKGTVDANGQPETFTYDTGNEIVLRSYPIAGYSVKWTDQYGRAVPKSWI
DGNFLRFHAPESGTYTANFQKELPGELTIGNWTFLYTTNDNDELTLTRATSGSGALDIPA
SYESHPIVGITPEALQGNTKITSISLPSTIKQFAASGAIYAGSYTGKGTENDAIKLSTSL
AANKAWSVSFNVENGGQTFNQWGSSLLATGTEALASIYDKGFQLYLAASGNIVLKLGSEE
KKVFTLTQGKTSFSVNVVHNASGDLSVSINNGSETDSYTEKSYELNDVEQFCTALPKGVN
LNNLVASFTGVSVNPLKGCTNLRTISVSKENPYFSATDDVLYDAQGTTLLACPAGRLSSF
LNLPSKVKAISNEAFSQCRNLRYISCTNATPAVAMAKAFDGCKLYAQVGESNIEAYRKAW
GLPILALVSGSDDLADATALKLASEDAVYLKSAGEEVPTASTLSQDIPVWLSIEMPANVY
GSFYFPTVPTGIFVEGIDADEVSESKLNLLRYENGTFTNASEIQNGIYLMSIPEEWSGKS
LTLQFPHSEAEWKQLNGAVVNGSTKGANFTARIYVFNEDYTLLKLLDKESTISISPFTAM
LTGDDSSAPTINIAALTGIHASNTSTSIQPVSIYDLNGRQISNSKLKSLKSLQRGVYIIN
GKKVVK

Enzyme Prediction     

No EC number prediction in MGYG000001918_01343.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH89	75	722	8.5e-195	0.9939668174962293

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam05089	NAGLU	9.87e-149	133	448	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	4.80e-67	458	717	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	2.75e-18	34	120	1	79	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.
TIGR04183	Por_Secre_tail	0.002	1702	1746	14	68	Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.
pfam18998	Flg_new_2	0.008	856	906	12	70	Divergent InlB B-repeat domain. This family of domains are found in bacterial cell surface proteins. They are often found in tandem array. This domain is closely related to pfam09479.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFQ12583.1	9.95e-226	6	725	4	718
QRQ55998.1	2.52e-181	25	702	14	705
ALJ49197.1	2.52e-181	25	702	14	705
SCV08615.1	3.02e-181	65	702	40	690
QDM11879.1	4.75e-181	65	702	54	704

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VC9_A	9.72e-116	28	717	166	873	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	1.17e-115	28	717	174	881	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	1.07e-114	28	717	189	896	CpGH89(E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactose [Clostridium perfringens]
4XWH_A	1.02e-89	35	725	8	712	Crystalstructure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P54802	6.97e-89	27	725	21	735	Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2
Q9FNA3	2.75e-88	79	725	97	805	Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU 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
0.000271	0.998925	0.000303	0.000170	0.000159	0.000144

TMHMM  Annotations     

start	end
5	27