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CAZyme Information: MGYG000003100_00335

You are here: Home > Sequence: MGYG000003100_00335

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 UMGS946 sp900547135
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-138; UMGS946; UMGS946 sp900547135
CAZyme ID MGYG000003100_00335
CAZy Family GT51
CAZyme Description Monofunctional biosynthetic peptidoglycan transglycosylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
927 MGYG000003100_9|CGC1 102223.32 4.9555
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003100 1865341 MAG Spain Europe
Gene Location Start: 13420;  End: 16203  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003100_00335.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT51 112 279 1.3e-61 0.9096045197740112

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02074 PBP_1a_fam 7.52e-177 124 707 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]
COG0744 MrcB 6.68e-172 51 722 5 614
Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009 MrcA 2.85e-133 63 741 4 751
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
COG4953 PbpC 3.68e-69 68 729 7 586
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis].
pfam00912 Transgly 1.63e-68 112 273 1 162
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
QWT55823.1 4.92e-241 44 872 51 863
QTE72383.1 9.86e-234 53 903 111 974
QTE73372.1 9.86e-234 53 903 111 974
QUC66968.1 1.15e-233 53 845 111 899
QUA52775.1 8.25e-232 30 847 77 890

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7U4H_A 1.71e-72 104 762 19 809
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 1.34e-60 108 701 23 719
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]
3DWK_A 1.60e-58 108 680 10 561
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 4.50e-54 108 680 19 570
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]
3UDF_A 2.59e-53 108 707 23 718
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A5I6G4 3.60e-113 59 781 13 716
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) OX=441771 GN=pbpA PE=3 SV=1
A7FY32 3.60e-113 59 781 13 716
Penicillin-binding protein 1A OS=Clostridium botulinum (strain ATCC 19397 / Type A) OX=441770 GN=pbpA PE=3 SV=1
A7GHV1 6.52e-113 59 781 13 716
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) OX=441772 GN=pbpA PE=3 SV=1
Q0TNZ8 1.44e-110 62 767 28 724
Penicillin-binding protein 1A OS=Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) OX=195103 GN=pbpA PE=3 SV=1
Q0SRL7 8.37e-110 62 767 28 724
Penicillin-binding protein 1A OS=Clostridium perfringens (strain SM101 / Type A) OX=289380 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
0.999696 0.000289 0.000001 0.000000 0.000000 0.000006

TMHMM  Annotations      download full data without filtering help

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