CAZyme Information: MGYG000003355_04003

Basic Information

• Species: Lachnoclostridium phytofermentans_A
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnoclostridium; Lachnoclostridium phytofermentans_A
• CAZyme ID: MGYG000003355_04003
• CAZy Family: GH33
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
337	MGYG000003355_177|CGC1	38341.31	8.6841

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003355	5194070	MAG	China	Asia

• Gene Location: Start: 1559; End: 2572 Strand: -

Full Sequence      

MKTIAHELIIPKDLINRNCHASHCLPLSDGSVFAVWFEGTKEGNDDVCIWGAKRSVDGTW
SQKKQLTEDNHLPHWNPVLLQSTKDTITLYYKQGKPISNWYTMYMTSIDNGNSWSKPKEL
VPGDIGGRGPVRNKAIVLSNGWILAPSSSESSIWSMFSDLSKDNGITWTTSNKVNIFHDS
EVPLTWYDKLLDNSLIRKKRGVIQPTFWESTPGHVHALLRSSEGKIYYAESLNYGQSWNR
PQKTILPNNNSGIDAVKTPNGHLYLIYNPVDKNWGKRYPISLAISKDNGSTWNKIMDLES
GSGKDELSYPCIQFQDNRLYITYTHNRTNISFWILTI

Enzyme Prediction     

No EC number prediction in MGYG000003355_04003.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH33	27	332	1e-29	0.9035087719298246

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam13088	BNR_2	5.35e-74	30	321	1	280	BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
COG4692	COG4692	3.16e-44	19	332	33	368	Predicted neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
cd15482	Sialidase_non-viral	2.48e-42	7	336	1	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.
cd18621	GH32_XdINV-like	0.008	244	295	72	125	glycoside hydrolase family 32 protein such as Xanthophyllomyces dendrorhous beta-fructofuranosidase (Inv;Xd-INV;XdINV). This subfamily of glycosyl hydrolase family GH32 includes fructan:fructan 1-fructosyltransferase (FT, EC 2.4.1.100) and beta-fructofuranosidase (invertase or Inv, EC 3.2.1.26), among others. These enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Xanthophyllomyces dendrorhous beta-fructofuranosidase (XdINV) also catalyzes the synthesis of fructooligosaccharides (FOS, a beneficial prebiotic), producing neo-FOS, making it an interesting biotechnology target. Structural studies show plasticity of its active site, having a flexible loop that is essential in binding sucrose and beta(2-1)-linked oligosaccharide, making it a valuable biocatalyst to produce novel bioconjugates. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUS95056.1	5.80e-104	2	333	3	329
ALS21221.1	2.97e-97	3	332	4	332
AEL25808.1	6.02e-96	1	333	45	361
AKP51429.1	8.00e-96	1	333	43	359
AZS14954.1	2.20e-94	4	332	5	331

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4YW1_A	1.47e-07	83	242	400	540	ChainA, Neuraminidase C [Streptococcus pneumoniae TIGR4],4YW1_B Chain B, Neuraminidase C [Streptococcus pneumoniae TIGR4],4YW2_A Chain A, Neuraminidase C [Streptococcus pneumoniae TIGR4],4YW2_B Chain B, Neuraminidase C [Streptococcus pneumoniae TIGR4],4YW3_A Chain A, Neuraminidase C [Streptococcus pneumoniae TIGR4],4YW3_B Chain B, Neuraminidase C [Streptococcus pneumoniae TIGR4],4YW4_A Streptococcus pneumoniae sialidase NanC [Streptococcus pneumoniae],4YW4_B Streptococcus pneumoniae sialidase NanC [Streptococcus pneumoniae],4YW5_A Chain A, Neuraminidase C [Streptococcus pneumoniae TIGR4],4YW5_B Chain B, Neuraminidase C [Streptococcus pneumoniae TIGR4],5F9T_A Chain A, Neuraminidase C [Streptococcus pneumoniae TIGR4],5F9T_B Chain B, Neuraminidase C [Streptococcus pneumoniae TIGR4]
4YZ1_A	1.48e-07	83	242	419	559	CrystalStructure of Streptococcus pneumoniae NanC, apo structure. [Streptococcus pneumoniae TIGR4],4YZ1_B Crystal Structure of Streptococcus pneumoniae NanC, apo structure. [Streptococcus pneumoniae TIGR4],4YZ2_A Crystal Structure of Streptococcus pneumoniae NanC, in complex with 2-deoxy-2,3-didehydro-N-acetylneuraminic acid. [Streptococcus pneumoniae],4YZ2_B Crystal Structure of Streptococcus pneumoniae NanC, in complex with 2-deoxy-2,3-didehydro-N-acetylneuraminic acid. [Streptococcus pneumoniae],4YZ3_A Crystal Structure of Streptococcus pneumoniae NanC, in complex with Oseltamivir. [Streptococcus pneumoniae TIGR4],4YZ3_B Crystal Structure of Streptococcus pneumoniae NanC, in complex with Oseltamivir. [Streptococcus pneumoniae TIGR4],4YZ4_A Crystal Structure of Streptococcus pneumoniae NanC, in complex with N-Acetylneuraminic acid. [Streptococcus pneumoniae],4YZ4_B Crystal Structure of Streptococcus pneumoniae NanC, in complex with N-Acetylneuraminic acid. [Streptococcus pneumoniae],4YZ5_A Crystal Structure of Streptococcus pneumoniae NanC, in complex with 3-Sialyllactose [Streptococcus pneumoniae],4YZ5_B Crystal Structure of Streptococcus pneumoniae NanC, in complex with 3-Sialyllactose [Streptococcus pneumoniae]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000043	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003355_04003.