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CAZyme Information: MGYG000001691_02496

You are here: Home > Sequence: MGYG000001691_02496

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 Aeromonas veronii_A
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Aeromonadaceae; Aeromonas; Aeromonas veronii_A
CAZyme ID MGYG000001691_02496
CAZy Family GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
239 MGYG000001691_20|CGC1 28339.31 7.8103
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001691 4542842 Isolate not provided not provided
Gene Location Start: 32007;  End: 32726  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001691_02496.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 2 152 1.2e-22 0.5652173913043478

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4092 COG4092 1.42e-19 1 154 128 290
Predicted glycosyltransferase involved in capsule biosynthesis [Cell wall/membrane/envelope biogenesis].
pfam10111 Glyco_tranf_2_2 1.66e-19 2 149 116 269
Glycosyltransferase like family 2. Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.
cd06420 GT2_Chondriotin_Pol_N 3.18e-05 53 82 135 164
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase. Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.
pfam02709 Glyco_transf_7C 3.64e-05 49 83 24 58
N-terminal domain of galactosyltransferase. This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.
cd02510 pp-GalNAc-T 5.43e-05 43 76 170 203
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans. UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QSR45780.1 1.41e-175 3 239 46 282
AHV35627.1 2.01e-175 6 239 1 234
AXV34919.1 5.76e-175 6 239 1 234
AAM22575.1 1.93e-173 4 239 125 360
QSR70786.1 1.43e-172 3 239 53 289

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
1.000048 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001691_02496.