CAZyme Information: MGYG000002452_02369

Basic Information

• Species: Akkermansia muciniphila_C
• Lineage: Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales; Akkermansiaceae; Akkermansia; Akkermansia muciniphila_C
• CAZyme ID: MGYG000002452_02369
• CAZy Family: GH33
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1045	MGYG000002452_3|CGC7	110448.09	4.9751

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002452	2902150	Isolate	China	Asia

• Gene Location: Start: 472813; End: 475950 Strand: -

Full Sequence      

MSTFHPLRRTFASAAALLLLYLGAGMALRASEPVSENFDSFQTGGFTSLSTALGTMTAES
GHAAIANNRWSSQPNCLRLTGRGAGMTSTATLTLPAPLAVKKILSLRGERWTASNPFSFT
IHAVDREGNETLVADGSSLKTGGSPMTQQVEGMIPSGTAGLIFRCEAPANTGVLLDDLAF
SEFKPFSSAAEAWPAMIRMEANGILRFSLTQTPATYAGMAVTVDMSPSDDLGDIESVSLY
TGDASNIYSAPAYGSSGHGAMSSPGILASPAQPPAPVMTFPVTSGALTDGQQYYFWVSVK
LKDSASMDHKVGARIASVTVNGETTDFTDGVTARQRIGYAIAKGNDPVYGGPTEGKTSRK
FRIPGIVRAGNGDLVSVFDIRYDGRNDMQANIDMGCSRSMDNGRTWTPVNVAVNFNPTSN
SANDYNSGYGVSDPCILLDEVNGTLWVAGIARHGLASSKANVDVESLETAQYVVAYSTDN
GQTWGSVDPDTGEFVKMKPRSINKDIKNRAWKSFFQGPGHGITMKKTVNGVRPIVFPSQI
WTGTSGAGTPQSCIIYSLDRGQTWISADTGKSGTLGIGASSSECVVTELSDGRLMLNARN
ENKSGYRKVFTTDDMGETWTAHATSLKALPEPAACQASQLAVENSGNISRAILFSNPDKT
SAPRALMTLKASFDEGATWPANRQVLYDSRPSCGYSDICETGDGHIGVLYEGLAGDENIF
FLRIPYHEFLPTLDVPAAAQTIRVEAEGITASTFTVSSDGSWTASSSADWITVSPASGSG
NGTVTYSVNRWEGAGERTGAITVTVPGVQPAVVTVIQSGRAPALTVSPGAHVLPKNGGTA
IFSVTCDAAWAVSKTADWLNITGTQGAETGNGTVSIAAAANPGESSRTAGLSFSSFGTVR
SATVVQRGQKRTWNEWKEDEITSRDPAADQTGPNDSPAGDGIPNLLKYATGLDPLKPSGS
VVQVSTEEAGGDTFLVLDWPVNPEATGIRHLVEASEDLRTWEEITEVETEGKSSASFRDT
VPMKAEAPRRRFLHLKISREGENTP

Enzyme Prediction     

No EC number prediction in MGYG000002452_02369.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH33	354	725	1.3e-77	0.9590643274853801

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd15482	Sialidase_non-viral	7.62e-79	361	725	14	339	Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
cd14948	BACON	5.27e-18	740	818	7	83	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
pfam14873	BNR_assoc_N	2.60e-16	190	324	8	149	N-terminal domain of BNR-repeat neuraminidase. This domain is usually found at the N-terminus of the BNR-repeat neuraminidase protein family.
pfam13859	BNR_3	1.99e-15	363	620	1	212	BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
cd14948	BACON	8.01e-15	823	906	1	82	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWP54611.1	0.0	1	1043	1	1043
QWP27708.1	0.0	1	1043	1	1043
QWP61791.1	0.0	1	1043	1	1043
QWP69127.1	0.0	1	1043	1	1043
QWP03917.1	0.0	1	1043	1	1043

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MYV_A	2.68e-67	294	711	121	504	Sialidase26co-crystallized with DANA-Gc [bacterium],6MYV_B Sialidase26 co-crystallized with DANA-Gc [bacterium],6MYV_C Sialidase26 co-crystallized with DANA-Gc [bacterium],6MYV_D Sialidase26 co-crystallized with DANA-Gc [bacterium]
6MNJ_A	4.59e-67	294	711	141	521	Hadzamicrobial sialidase Hz136 [Alistipes],6MNJ_B Hadza microbial sialidase Hz136 [Alistipes]
6MRV_A	5.03e-67	294	711	142	525	Sialidase26co-crystallized with DANA [bacterium],6MRV_B Sialidase26 co-crystallized with DANA [bacterium],6MRX_A Sialidase26 apo [bacterium],6MRX_B Sialidase26 apo [bacterium],6MRX_C Sialidase26 apo [bacterium],6MRX_D Sialidase26 apo [bacterium]
4FJ6_A	3.79e-65	294	711	122	504	Crystalstructure of a glycoside hydrolase family 33, candidate sialidase (BDI_2946) from Parabacteroides distasonis ATCC 8503 at 1.90 A resolution [Parabacteroides distasonis ATCC 8503],4FJ6_B Crystal structure of a glycoside hydrolase family 33, candidate sialidase (BDI_2946) from Parabacteroides distasonis ATCC 8503 at 1.90 A resolution [Parabacteroides distasonis ATCC 8503],4FJ6_C Crystal structure of a glycoside hydrolase family 33, candidate sialidase (BDI_2946) from Parabacteroides distasonis ATCC 8503 at 1.90 A resolution [Parabacteroides distasonis ATCC 8503],4FJ6_D Crystal structure of a glycoside hydrolase family 33, candidate sialidase (BDI_2946) from Parabacteroides distasonis ATCC 8503 at 1.90 A resolution [Parabacteroides distasonis ATCC 8503]
4Q6K_A	3.34e-61	294	724	124	520	Crystalstructure of a putative neuraminidase (BACCAC_01090) from Bacteroides caccae ATCC 43185 at 1.90 A resolution (PSI Community Target) [Bacteroides caccae ATCC 43185],4Q6K_B Crystal structure of a putative neuraminidase (BACCAC_01090) from Bacteroides caccae ATCC 43185 at 1.90 A resolution (PSI Community Target) [Bacteroides caccae ATCC 43185],4Q6K_C Crystal structure of a putative neuraminidase (BACCAC_01090) from Bacteroides caccae ATCC 43185 at 1.90 A resolution (PSI Community Target) [Bacteroides caccae ATCC 43185],4Q6K_D Crystal structure of a putative neuraminidase (BACCAC_01090) from Bacteroides caccae ATCC 43185 at 1.90 A resolution (PSI Community Target) [Bacteroides caccae ATCC 43185]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P31206	2.19e-63	294	711	143	526	Sialidase OS=Bacteroides fragilis (strain YCH46) OX=295405 GN=nanH PE=3 SV=2
Q02834	2.12e-29	315	715	24	390	Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1
P15698	8.14e-21	361	622	54	285	Sialidase OS=Paeniclostridium sordellii OX=1505 PE=1 SV=1
P10481	1.27e-17	358	730	33	379	Sialidase OS=Clostridium perfringens OX=1502 GN=nanH PE=1 SV=1
A5PF10	6.70e-11	361	707	78	382	Sialidase-1 OS=Sus scrofa OX=9823 GN=NEU1 PE=3 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
0.288538	0.678029	0.031598	0.001030	0.000369	0.000418

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002452_02369.