logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004253_00574

You are here: Home > Sequence: MGYG000004253_00574

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 Desulfovibrio piger_A
Lineage Bacteria; Desulfobacterota; Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae; Desulfovibrio; Desulfovibrio piger_A
CAZyme ID MGYG000004253_00574
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
345 MGYG000004253_7|CGC1 36231.05 9.3639
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004253 2386728 MAG China Asia
Gene Location Start: 65096;  End: 66133  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004253_00574.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT28 182 339 1.9e-52 0.9681528662420382

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK00726 murG 1.65e-134 1 327 1 328
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
cd03785 GT28_MurG 3.54e-123 3 328 1 329
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.
TIGR01133 murG 2.35e-108 3 327 2 325
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]
COG0707 MurG 5.97e-99 3 327 2 328
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis].
pfam04101 Glyco_tran_28_C 6.24e-38 182 327 2 147
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
SFV72770.1 3.25e-238 1 340 1 340
VZH35140.1 7.47e-154 3 334 4 335
AMD89940.1 1.42e-151 1 339 1 339
QTO41588.1 2.72e-148 1 339 1 339
ATD81105.1 6.46e-143 3 339 4 340

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3S2U_A 9.68e-75 3 339 4 340
Crystalstructure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex [Pseudomonas aeruginosa PAO1]
7D1I_A 1.77e-58 2 321 10 334
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]
1F0K_A 3.41e-58 2 313 7 315
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q728U8 2.14e-119 1 334 1 338
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough) OX=882 GN=murG PE=3 SV=1
A1VBE8 3.03e-119 1 334 1 338
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Desulfovibrio vulgaris subsp. vulgaris (strain DP4) OX=391774 GN=murG PE=3 SV=1
B8DP79 1.22e-117 1 341 1 360
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F) OX=883 GN=murG PE=3 SV=1
Q313Q3 3.62e-112 1 339 1 343
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20) OX=207559 GN=murG PE=3 SV=1
Q1MPB9 5.24e-99 3 340 4 343
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase OS=Lawsonia intracellularis (strain PHE/MN1-00) OX=363253 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
1.000031 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004253_00574.