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CAZyme Information: MGYG000000953_01023

You are here: Home > Sequence: MGYG000000953_01023

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 Fusobacterium_A sp900549465
Lineage Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae; Fusobacterium_A; Fusobacterium_A sp900549465
CAZyme ID MGYG000000953_01023
CAZy Family GT51
CAZyme Description Monofunctional biosynthetic peptidoglycan transglycosylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
748 MGYG000000953_43|CGC1 86418.18 9.4462
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000953 1995240 MAG Spain Europe
Gene Location Start: 10453;  End: 12699  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000953_01023.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT51 65 222 2.3e-49 0.8983050847457628

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4953 PbpC 0.0 38 746 35 733
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis].
TIGR02073 PBP_1c 0.0 37 744 9 726
penicillin-binding protein 1C. This subfamily of the penicillin binding proteins includes the member from E. coli designated penicillin-binding protein 1C. Members have both transglycosylase and transpeptidase domains and are involved in forming cross-links in the late stages of peptidoglycan biosynthesis. All members of this subfamily are presumed to have the same basic function. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
COG0744 MrcB 2.21e-113 1 535 9 571
Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
PRK11240 PRK11240 1.38e-111 75 534 77 535
penicillin-binding protein 1C; Provisional
TIGR02074 PBP_1a_fam 6.54e-94 66 535 8 501
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]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AVQ18978.1 0.0 1 748 1 747
QNM15576.1 0.0 3 748 7 750
AVQ31509.1 4.06e-313 15 748 16 754
VEH39720.1 4.06e-313 15 748 16 754
SQJ06920.1 5.76e-313 22 748 23 754

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3DWK_A 3.57e-35 42 534 10 556
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 2.11e-33 33 534 10 565
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]
2JE5_A 4.83e-33 45 545 40 614
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]
4OON_A 1.35e-30 67 585 46 747
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]
5FGZ_A 8.54e-30 69 542 165 675
E.coli PBP1b in complex with FPI-1465 [Escherichia coli K-12],5HL9_A E. coli PBP1b in complex with acyl-ampicillin and moenomycin [Escherichia coli K-12],5HLA_A E. coli PBP1b in complex with acyl-cephalexin and moenomycin [Escherichia coli K-12],5HLB_A E. coli PBP1b in complex with acyl-aztreonam and moenomycin [Escherichia coli K-12],5HLD_A E. coli PBP1b in complex with acyl-CENTA and moenomycin [Escherichia coli K-12],6YN0_A Structure of E. coli PBP1b with a FtsN peptide activating transglycosylase activity [Escherichia coli K-12],7LQ6_A Chain A, Penicillin-binding protein 1B [Escherichia coli K-12]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P76577 1.12e-83 39 561 42 564
Penicillin-binding protein 1C OS=Escherichia coli (strain K12) OX=83333 GN=pbpC PE=1 SV=1
P38050 1.57e-49 32 556 41 591
Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
P40750 4.38e-45 44 537 60 599
Penicillin-binding protein 4 OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpD PE=1 SV=2
A7GHV1 9.17e-43 41 559 58 641
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) OX=441772 GN=pbpA PE=3 SV=1
A7FY32 5.38e-42 41 559 58 641
Penicillin-binding protein 1A OS=Clostridium botulinum (strain ATCC 19397 / Type A) OX=441770 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
0.947010 0.049025 0.002661 0.000208 0.000129 0.000985

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000953_01023.