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CAZyme Information: MGYG000001509_01531

You are here: Home > Sequence: MGYG000001509_01531

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 Flaviflexus massiliensis
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Flaviflexus; Flaviflexus massiliensis
CAZyme ID MGYG000001509_01531
CAZy Family GT51
CAZyme Description Monofunctional biosynthetic peptidoglycan transglycosylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
769 82365.23 4.0377
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001509 2631133 Isolate not provided not provided
Gene Location Start: 761862;  End: 764171  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001509_01531.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT51 77 266 3.7e-64 0.9943502824858758

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0744 MrcB 6.58e-141 30 689 22 606
Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
TIGR02074 PBP_1a_fam 3.90e-136 88 682 1 531
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]
COG5009 MrcA 6.32e-83 54 641 30 690
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
pfam00912 Transgly 8.27e-79 77 266 1 177
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.
PRK09506 mrcB 4.70e-54 87 712 209 789
bifunctional glycosyl transferase/transpeptidase; Reviewed

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AZQ77718.1 0.0 1 713 34 747
AZN30434.1 0.0 1 713 1 712
VEI13165.1 6.41e-279 14 680 5 695
AZR01450.1 1.49e-268 14 718 12 739
AJC70246.1 3.34e-268 14 718 5 732

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5FGZ_A 5.35e-43 87 712 154 735
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]
3VMA_A 6.18e-43 87 712 175 756
CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [Escherichia coli K-12]
3FWL_A 1.94e-40 87 712 158 739
CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [Escherichia coli]
4OON_A 5.90e-38 73 641 23 694
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 3.07e-37 68 646 32 611
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
A0R7G2 1.09e-56 71 704 111 708
Penicillin-binding protein 1A OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=ponA1 PE=3 SV=1
P71707 4.02e-56 68 699 170 765
Penicillin-binding protein 1A OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=ponA1 PE=1 SV=3
P70997 4.14e-54 69 642 53 581
Penicillin-binding protein 2D OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpG PE=2 SV=3
P38050 4.28e-52 71 642 49 570
Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
P39793 2.89e-49 71 644 77 616
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
0.994191 0.004509 0.000189 0.000035 0.000017 0.001099

TMHMM  Annotations      download full data without filtering help

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