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CAZyme Information: MGYG000003278_00547

You are here: Home > Sequence: MGYG000003278_00547

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 UMGS1487 sp900552225
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1487; UMGS1487 sp900552225
CAZyme ID MGYG000003278_00547
CAZy Family GT51
CAZyme Description Monofunctional biosynthetic peptidoglycan transglycosylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
747 MGYG000003278_48|CGC1 82944.38 4.6061
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003278 2107758 MAG United States North America
Gene Location Start: 18698;  End: 20941  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003278_00547.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT51 101 270 6.3e-59 0.9491525423728814

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02074 PBP_1a_fam 5.11e-133 108 660 4 531
penicillin-binding protein, 1A family. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
COG0744 MrcB 7.14e-131 45 667 21 606
Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009 MrcA 9.18e-84 109 731 70 781
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
pfam00912 Transgly 5.19e-73 101 271 8 177
Transglycosylase. The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.
TIGR02071 PBP_1b 2.83e-69 101 650 139 675
penicillin-binding protein 1B. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCI59848.1 5.55e-158 30 707 36 737
QNK41697.1 7.50e-143 27 707 22 705
QAT49292.1 1.18e-139 27 722 22 717
QEY34222.1 1.33e-138 33 707 23 701
CAB1249043.1 1.57e-135 36 708 33 703

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7U4H_A 2.66e-55 105 703 39 807
ChainA, Penicillin-binding protein 1A (Pbp1a) [Chlamydia trachomatis D/UW-3/CX],7U4H_B Chain B, Penicillin-binding protein 1A (Pbp1a) [Chlamydia trachomatis D/UW-3/CX]
3DWK_A 6.93e-47 103 632 24 557
ChainA, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL],3DWK_B Chain B, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL],3DWK_C Chain C, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL],3DWK_D Chain D, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL]
2OLU_A 5.10e-44 103 632 33 566
StructuralInsight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Apoenzyme [Staphylococcus aureus],2OLV_A Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex [Staphylococcus aureus],2OLV_B Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex [Staphylococcus aureus]
3ZG8_B 1.04e-41 190 632 2 432
CrystalStructure of Penicillin Binding Protein 4 from Listeria monocytogenes in the Ampicillin bound form [Listeria monocytogenes],3ZG9_B Crystal Structure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the Cefuroxime bound form [Listeria monocytogenes],3ZGA_B Crystal Structure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the Carbenicillin bound form [Listeria monocytogenes]
2JE5_A 2.44e-40 109 692 57 661
StructuralAnd Mechanistic Basis Of Penicillin Binding Protein Inhibition By Lactivicins [Streptococcus pneumoniae R6],2JE5_B Structural And Mechanistic Basis Of Penicillin Binding Protein Inhibition By Lactivicins [Streptococcus pneumoniae R6]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q0SRL7 1.31e-70 112 691 97 699
Penicillin-binding protein 1A OS=Clostridium perfringens (strain SM101 / Type A) OX=289380 GN=pbpA PE=3 SV=1
Q0TNZ8 3.44e-68 112 691 97 699
Penicillin-binding protein 1A OS=Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) OX=195103 GN=pbpA PE=3 SV=1
A7GHV1 2.23e-67 65 661 36 647
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) OX=441772 GN=pbpA PE=3 SV=1
A7FY32 4.38e-67 65 661 36 647
Penicillin-binding protein 1A OS=Clostridium botulinum (strain ATCC 19397 / Type A) OX=441770 GN=pbpA PE=3 SV=1
A5I6G4 4.38e-67 65 661 36 647
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) OX=441771 GN=pbpA 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
0.999737 0.000269 0.000001 0.000001 0.000000 0.000002

TMHMM  Annotations      download full data without filtering help

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