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CAZyme Information: MGYG000003293_01174

You are here: Home > Sequence: MGYG000003293_01174

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 CAG-110 sp900544405
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-110; CAG-110 sp900544405
CAZyme ID MGYG000003293_01174
CAZy Family GT51
CAZyme Description Monofunctional biosynthetic peptidoglycan transglycosylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
915 MGYG000003293_70|CGC1 102132.38 4.4392
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003293 2030729 MAG Mongolia Asia
Gene Location Start: 38336;  End: 41083  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003293_01174.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT51 109 278 2e-57 0.943502824858757

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02074 PBP_1a_fam 4.78e-132 116 716 5 526
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 1.24e-131 79 721 45 599
Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009 MrcA 3.24e-86 52 754 10 754
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
pfam00912 Transgly 1.02e-61 108 279 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.
COG4953 PbpC 2.24e-49 119 718 64 561
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUO33826.1 1.77e-145 68 840 55 795
BCK80539.1 8.04e-141 45 827 31 777
BAK99350.1 1.15e-136 49 799 36 749
BCK78565.1 2.43e-132 44 799 56 779
QNL43378.1 1.01e-131 68 799 51 726

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7U4H_A 1.79e-52 95 771 24 815
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]
3ZG8_B 2.75e-52 196 696 3 436
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]
3ZG7_B 2.34e-49 196 696 3 436
CrystalStructure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the apo form [Listeria monocytogenes]
4OON_A 5.35e-43 118 698 44 701
Crystalstructure of PBP1a in complex with compound 17 ((4Z,8S,11E,14S)-5-(2-amino-1,3-thiazol-4-yl)-14-(5,6-dihydroxy-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-8-formyl-2-methyl-6-oxo-3,10-dioxa-4,7,11-triazatetradeca-4,11-diene-2,12,14-tricarboxylic acid) [Pseudomonas aeruginosa PAO1]
2JE5_A 2.39e-39 117 698 58 613
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
A5I6G4 1.95e-68 87 755 54 680
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) OX=441771 GN=pbpA PE=3 SV=1
A7FY32 1.95e-68 87 755 54 680
Penicillin-binding protein 1A OS=Clostridium botulinum (strain ATCC 19397 / Type A) OX=441770 GN=pbpA PE=3 SV=1
A7GHV1 1.22e-67 87 755 54 680
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) OX=441772 GN=pbpA PE=3 SV=1
Q891X1 3.35e-67 86 753 57 693
Penicillin-binding protein 1A OS=Clostridium tetani (strain Massachusetts / E88) OX=212717 GN=pbpA PE=3 SV=1
Q0SRL7 1.23e-61 119 755 97 702
Penicillin-binding protein 1A OS=Clostridium perfringens (strain SM101 / Type A) OX=289380 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
0.999987 0.000029 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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