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CAZyme Information: MGYG000002574_00905

You are here: Home > Sequence: MGYG000002574_00905

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 ulcerans_A
Lineage Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae; Fusobacterium_A; Fusobacterium_A ulcerans_A
CAZyme ID MGYG000002574_00905
CAZy Family GT51
CAZyme Description Penicillin-binding protein 1C
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
758 MGYG000002574_34|CGC1 87260.17 9.8622
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002574 3729499 MAG China Asia
Gene Location Start: 4382;  End: 6658  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002574_00905.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT51 60 222 2.2e-50 0.9265536723163842

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4953 PbpC 0.0 9 750 8 731
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis].
TIGR02073 PBP_1c 0.0 34 751 5 727
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]
PRK11240 PRK11240 4.90e-108 2 562 6 562
penicillin-binding protein 1C; Provisional
COG0744 MrcB 6.07e-102 6 577 23 611
Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
TIGR02074 PBP_1a_fam 4.07e-89 67 536 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
SQJ06920.1 0.0 1 758 1 758
AVQ26788.1 0.0 1 758 1 758
AVQ31509.1 0.0 1 758 1 758
VEH39720.1 0.0 1 758 1 758
BBA50599.1 0.0 1 758 1 758

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5FGZ_A 1.39e-34 70 587 165 717
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 1.51e-34 70 587 186 738
CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [Escherichia coli K-12]
4OON_A 5.15e-34 69 535 47 694
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 1.21e-33 65 616 58 675
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]
3FWL_A 1.79e-32 70 587 169 721
CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [Escherichia coli]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P76577 3.75e-85 32 573 34 573
Penicillin-binding protein 1C OS=Escherichia coli (strain K12) OX=83333 GN=pbpC PE=1 SV=1
P38050 6.82e-48 40 608 48 623
Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
P40750 1.71e-41 40 548 67 609
Penicillin-binding protein 4 OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpD PE=1 SV=2
A7GHV1 2.52e-40 34 551 52 630
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) OX=441772 GN=pbpA PE=3 SV=1
A5I6G4 1.45e-39 34 551 52 630
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) OX=441771 GN=pbpA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.389938 0.039566 0.568008 0.000262 0.000202 0.002039

TMHMM  Annotations      download full data without filtering help

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