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CAZyme Information: MGYG000003337_00613

You are here: Home > Sequence: MGYG000003337_00613

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 Ruminococcus_C sp900765125
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C sp900765125
CAZyme ID MGYG000003337_00613
CAZy Family GT51
CAZyme Description Monofunctional biosynthetic peptidoglycan transglycosylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
903 99664.98 4.6832
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003337 2462692 MAG China Asia
Gene Location Start: 11078;  End: 13789  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003337_00613.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT51 207 389 6.5e-57 0.9491525423728814

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0744 MrcB 4.42e-139 135 809 5 600
Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
TIGR02074 PBP_1a_fam 2.49e-135 211 808 2 530
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]
COG5009 MrcA 1.87e-98 141 852 4 764
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
COG4953 PbpC 2.21e-63 211 781 58 534
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis].
pfam00912 Transgly 1.36e-60 211 389 13 177
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL16716.1 4.79e-248 133 856 63 793
CCO04758.1 5.51e-149 131 856 19 738
ADU22273.1 8.03e-140 129 852 11 734
CBL33874.1 1.82e-129 135 853 38 752
CBK97274.1 7.01e-129 135 853 38 752

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ZG8_B 3.43e-48 295 782 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]
7U4H_A 1.33e-46 174 852 8 807
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]
4OON_A 5.00e-45 179 852 12 768
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]
3ZG7_B 6.10e-43 295 782 2 432
CrystalStructure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the apo form [Listeria monocytogenes]
2JE5_A 6.96e-43 211 835 54 666
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
A7GHV1 1.78e-69 136 833 11 670
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) OX=441772 GN=pbpA PE=3 SV=1
A5I6G4 3.49e-69 136 833 11 670
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) OX=441771 GN=pbpA PE=3 SV=1
A7FY32 3.49e-69 136 833 11 670
Penicillin-binding protein 1A OS=Clostridium botulinum (strain ATCC 19397 / Type A) OX=441770 GN=pbpA PE=3 SV=1
Q8XJ01 1.17e-64 210 822 90 678
Penicillin-binding protein 1A OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=pbpA PE=3 SV=1
Q891X1 1.49e-64 211 839 80 691
Penicillin-binding protein 1A OS=Clostridium tetani (strain Massachusetts / E88) OX=212717 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
1.000053 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
138 160