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CAZyme Information: MGYG000001490_01252

You are here: Home > Sequence: MGYG000001490_01252

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 Bifidobacterium catenulatum
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium catenulatum
CAZyme ID MGYG000001490_01252
CAZy Family GT28
CAZyme Description UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
406 MGYG000001490_1|CGC13 43161.29 6.5675
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001490 2079525 Isolate not provided not provided
Gene Location Start: 1423088;  End: 1424308  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001490_01252.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT28 219 391 1.5e-46 0.9872611464968153

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK00726 murG 1.68e-131 20 403 2 355
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785 GT28_MurG 6.44e-112 21 396 1 348
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.
COG0707 MurG 1.64e-91 22 401 3 353
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
TIGR01133 murG 7.83e-88 20 396 1 345
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase. RM 8449890 RT The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. RA Bupp K, van Heijenoort J. RL J Bacteriol 1993 Mar;175(6):1841-3 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
pfam04101 Glyco_tran_28_C 3.77e-35 218 395 1 166
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAR02175.1 1.94e-292 1 406 9 414
QGM63077.1 4.21e-285 1 406 1 406
BAQ29543.1 4.21e-285 1 406 1 406
AIZ14901.1 1.36e-275 16 406 1 391
BAR03946.1 1.36e-275 16 406 1 391

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1F0K_A 3.15e-40 15 399 1 350
The1.9 Angstrom Crystal Structure Of E. Coli Murg [Escherichia coli],1F0K_B The 1.9 Angstrom Crystal Structure Of E. Coli Murg [Escherichia coli],1NLM_A Crystal Structure Of Murg:glcnac Complex [Escherichia coli],1NLM_B Crystal Structure Of Murg:glcnac Complex [Escherichia coli]
7D1I_A 8.24e-33 17 360 7 324
ChainA, UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase [Acinetobacter baumannii],7D1I_B Chain B, UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase [Acinetobacter baumannii],7D1I_C Chain C, UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase [Acinetobacter baumannii]
3S2U_A 2.90e-31 21 383 4 335
Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A1A2E9 3.69e-247 16 405 1 390
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) OX=367928 GN=murG PE=3 SV=1
Q8CY50 3.60e-196 21 404 7 390
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Bifidobacterium longum (strain NCC 2705) OX=206672 GN=murG PE=3 SV=1
B3DQN1 3.60e-196 21 404 7 390
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Bifidobacterium longum (strain DJO10A) OX=205913 GN=murG PE=3 SV=1
B7GQ78 4.18e-195 21 404 7 390
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) OX=391904 GN=murG PE=3 SV=1
B0RIJ3 2.78e-105 23 406 5 359
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1) OX=31964 GN=murG PE=3 SV=1

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
1.000061 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001490_01252.