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CAZyme Information: MGYG000000251_02229

You are here: Home > Sequence: MGYG000000251_02229

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 Fusicatenibacter saccharivorans
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Fusicatenibacter; Fusicatenibacter saccharivorans
CAZyme ID MGYG000000251_02229
CAZy Family GT51
CAZyme Description Monofunctional biosynthetic peptidoglycan transglycosylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
251 MGYG000000251_8|CGC1 28470.77 8.9514
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000251 3784614 Isolate China Asia
Gene Location Start: 30286;  End: 31041  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000251_02229.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT51 58 226 1.3e-65 0.9548022598870056

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00912 Transgly 3.22e-82 49 226 3 177
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.
TIGR02074 PBP_1a_fam 7.90e-73 62 237 2 177
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 1.16e-72 19 235 22 250
Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009 MrcA 3.39e-60 19 251 9 252
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
COG4953 PbpC 6.32e-47 64 251 60 242
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
QNM09777.1 2.25e-77 5 240 2 241
QUO38940.1 4.01e-73 28 240 20 232
ASB42272.1 3.40e-71 19 239 18 237
ANU54501.1 3.40e-71 19 239 18 237
QQR31552.1 3.40e-71 19 239 18 237

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3NB6_A 6.89e-43 64 231 22 189
Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
2OQO_A 9.72e-43 64 231 22 189
Crystalstructure of a peptidoglycan glycosyltransferase from a class A PBP: insight into bacterial cell wall synthesis [Aquifex aeolicus VF5],3D3H_A Crystal structure of a complex of the peptidoglycan glycosyltransferase domain from Aquifex aeolicus and neryl moenomycin A [Aquifex aeolicus],3NB7_A Crystal structure of Aquifex Aeolicus Peptidoglycan Glycosyltransferase in complex with Decarboxylated Neryl Moenomycin [Aquifex aeolicus]
5U2G_A 3.79e-35 65 250 43 224
2.6Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20],5U2G_B 2.6 Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20]
3UDF_A 1.15e-34 65 248 42 221
ChainA, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDF_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii]
4OON_A 1.48e-33 70 233 47 210
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P70997 2.90e-45 64 240 76 252
Penicillin-binding protein 2D OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpG PE=2 SV=3
P38050 1.16e-43 22 235 10 240
Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
Q07259 2.05e-43 23 240 8 224
Putative transglycosylase H16_A0665 OS=Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) OX=381666 GN=H16_A0665 PE=3 SV=2
O66874 2.08e-38 64 231 65 232
Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
P39793 7.23e-38 42 235 75 269
Penicillin-binding protein 1A/1B OS=Bacillus subtilis (strain 168) OX=224308 GN=ponA PE=1 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
0.913715 0.000869 0.000473 0.000008 0.000004 0.084964

TMHMM  Annotations      download full data without filtering help

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