CAZyme Information: MGYG000001850_00478

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; QALW01; UMGS1322
• CAZyme ID: MGYG000001850_00478
• CAZy Family: GH33
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
362		40716.92	5.6308

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001850	2350438	MAG	Denmark	Europe

• Gene Location: Start: 10248; End: 11336 Strand: +

Full Sequence      

MFITDRHALSAYQKEHRLWQGIPGIEKTKGGRLFITFYSGGETEAPGNYVVLKKSDDDGV
TWSDILAVNAPQFPARAFDPCLWIDPMGRLWWFWSQQETGQFDGVGGVWYVRCDRPEEET
LAFTEPFRFANGVMMNKPTVLKNGTWLFPCAIWTDACYSGMPVVEGIKAERFSNVYASTD
HGQTITLLGSADIPNRCFDEHMTVELSDGRLLMLVRTHYGIGRSFSYDGGKTWTPGEDSG
ISGPNSRFFIRKLASGRILLVNHYHFQGRNNLTAMLSEDDCVSWKGFLLLDERGAVSYPD
GTEDTQGNLYIVYDRERGGSHEYKNHSDAAREILFAKITEEDILAGRLVSAGSRLKCIAD
KL

Enzyme Prediction     

No EC number prediction in MGYG000001850_00478.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH33	22	325	2.3e-31	0.9122807017543859

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd15482	Sialidase_non-viral	9.90e-49	22	339	16	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.
pfam13088	BNR_2	1.23e-26	31	311	1	280	BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
pfam04616	Glyco_hydro_43	7.39e-04	30	162	76	199	Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyze the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd18617	GH43_XynB-like	0.008	43	109	89	148	Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain 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
AEN08048.1	1.69e-119	3	361	12	375
AWL41261.1	5.32e-118	12	361	21	374
AHF93797.1	2.16e-117	10	362	23	372
QOV18850.1	1.23e-114	12	361	22	379
QDT85478.1	3.43e-109	12	361	49	389

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LBU_A	6.11e-08	22	316	96	415	ChainA, Exo-alpha-sialidase [Cutibacterium acnes],7LBV_A Chain A, Exo-alpha-sialidase [Cutibacterium acnes]
1EUT_A	2.83e-06	22	343	27	371	Sialidase,Large 68kd Form, Complexed With Galactose [Micromonospora viridifaciens],1EUU_A Sialidase Or Neuraminidase, Large 68kd Form [Micromonospora viridifaciens]
1EUR_A	3.68e-06	22	318	27	348	Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens]
1W8N_A	8.70e-06	22	343	23	367	Contributionof the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens. [Micromonospora viridifaciens],1W8O_A Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens [Micromonospora viridifaciens]
1WCQ_A	8.70e-06	22	343	23	367	Mutagenesisof the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens],1WCQ_B Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens],1WCQ_C Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens]

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
1.000008	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001850_00478.