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CAZyme Information: SHO78134.1

You are here: Home > Sequence: SHO78134.1

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 Malassezia sympodialis
Lineage Basidiomycota; Malasseziomycetes; ; Malasseziaceae; Malassezia; Malassezia sympodialis
CAZyme ID SHO78134.1
CAZy Family GT69
CAZyme Description UDP-N-acetylglucosamine transferase subunit ALG13 [Source:UniProtKB/TrEMBL;Acc:A0A1M8A7D6]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
187 LT671824|CGC5 19415.26 8.1625
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_MsympodialisATCC42132 4618 1230383 143 4475
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in SHO78134.1.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
227350 COG5017 1.54e-13 6 149 2 123
UDP-N-acetylglucosamine transferase subunit ALG13 [Carbohydrate transport and metabolism].
397977 Glyco_tran_28_C 1.35e-08 5 160 1 141
Glycosyltransferase family 28 C-terminal domain. The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.
340818 GT28_MurG 2.20e-05 72 161 231 319
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase. MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
223779 MurG 1.78e-04 71 164 232 326
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
227017 COG4671 0.002 68 156 271 359
Predicted glycosyl transferase [General function prediction only].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.19e-127 1 187 1 187
1.07e-40 5 183 6 183
4.27e-40 5 183 6 183
3.94e-17 7 164 244 408
3.94e-17 7 164 244 408

PDB Hits      help

SHO78134.1 has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.19e-12 8 182 5 160
UDP-N-acetylglucosamine transferase subunit alg13 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg13 PE=3 SV=1
2.28e-10 3 179 4 192
UDP-N-acetylglucosamine transferase subunit ALG13 OS=Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) OX=214684 GN=ALG13 PE=3 SV=1
2.28e-10 3 179 4 192
UDP-N-acetylglucosamine transferase subunit ALG13 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=ALG13 PE=3 SV=1
3.84e-08 8 144 9 146
UDP-N-acetylglucosamine transferase subunit alg13 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=alg13 PE=3 SV=2
5.36e-07 6 142 4 120
Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 OS=Homo sapiens OX=9606 GN=ALG13 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000084 0.000002

TMHMM  Annotations      help

There is no transmembrane helices in SHO78134.1.