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CAZyme Information: MGYG000003383_01307

You are here: Home > Sequence: MGYG000003383_01307

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 scardovii
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium scardovii
CAZyme ID MGYG000003383_01307
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
389 MGYG000003383_17|CGC6 40902.82 7.4412
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003383 3123324 MAG United States North America
Gene Location Start: 250636;  End: 251805  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003383_01307.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT28 205 376 1.7e-45 0.9872611464968153

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK00726 murG 7.64e-123 6 389 2 356
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785 GT28_MurG 7.52e-105 7 381 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 1.43e-84 8 389 3 356
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
TIGR01133 murG 2.18e-77 8 381 3 345
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 1.78e-34 204 380 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
BAQ31904.1 1.18e-271 1 389 1 389
AQM43335.1 5.37e-206 1 389 1 390
AHJ19624.1 5.37e-206 1 389 1 390
AZI16890.1 5.37e-206 1 389 1 390
AUD85381.1 3.10e-205 1 389 1 390

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1F0K_A 1.12e-40 1 389 2 355
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 8.10e-32 3 332 7 311
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 2.14e-31 7 389 4 356
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
Q8CY50 1.62e-204 1 388 1 389
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 1.62e-204 1 388 1 389
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 2.67e-203 1 388 1 389
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
A1A2E9 3.35e-185 1 387 1 387
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
B0RIJ3 1.77e-104 9 384 5 352
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
1.000046 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003383_01307.