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CAZyme Information: MGYG000000922_02074

You are here: Home > Sequence: MGYG000000922_02074

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species UMGS416 sp900542005
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; UMGS416; UMGS416; UMGS416 sp900542005
CAZyme ID MGYG000000922_02074
CAZy Family GH33
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
584 65769.67 5.6046
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000922 2901170 MAG China Asia
Gene Location Start: 25179;  End: 26933  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000922_02074.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 59 325 3.4e-20 0.5350877192982456

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd15482 Sialidase_non-viral 9.08e-21 154 322 157 293
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 5.14e-11 174 322 142 251
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
cd08978 GH_F 0.008 149 277 6 134
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 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. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 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.
pfam13859 BNR_3 0.009 172 244 154 211
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AIF26887.1 4.26e-194 6 579 5 577
QNN21869.1 2.29e-182 11 582 20 608
AHF90365.1 1.09e-161 21 584 13 600
QRX64725.1 8.35e-124 7 584 22 559
AKA52559.1 1.06e-123 20 561 27 542

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000040 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000922_02074.