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CAZyme Information: MGYG000000425_00618

You are here: Home > Sequence: MGYG000000425_00618

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
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; ;
CAZyme ID MGYG000000425_00618
CAZy Family GT51
CAZyme Description Penicillin-binding protein 1A/1B
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
740 82312.78 5.4518
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000425 1738291 MAG Sweden Europe
Gene Location Start: 1071;  End: 3293  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000425_00618.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT51 104 282 5.8e-60 0.9548022598870056

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02074 PBP_1a_fam 4.89e-169 110 686 1 526
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 5.49e-165 30 739 1 640
Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009 MrcA 5.63e-143 43 728 5 758
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
TIGR02071 PBP_1b 5.02e-88 106 738 142 730
penicillin-binding protein 1B. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
pfam00912 Transgly 8.15e-74 107 283 9 177
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AXA81016.1 8.06e-198 46 737 58 801
ATL89188.1 5.78e-195 46 737 43 786
CBL02306.1 9.48e-195 47 737 54 796
AXB28952.1 1.50e-194 47 737 69 811
ATO98888.1 4.61e-194 46 737 43 786

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ZG8_B 1.14e-68 202 662 3 433
CrystalStructure of Penicillin Binding Protein 4 from Listeria monocytogenes in the Ampicillin bound form [Listeria monocytogenes],3ZG9_B Crystal Structure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the Cefuroxime bound form [Listeria monocytogenes],3ZGA_B Crystal Structure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the Carbenicillin bound form [Listeria monocytogenes]
7U4H_A 4.43e-68 103 734 32 807
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 7.41e-63 78 736 12 771
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]
3ZG7_B 1.36e-61 202 662 3 433
CrystalStructure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the apo form [Listeria monocytogenes]
3UDF_A 1.12e-56 114 681 42 708
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
A7GHV1 1.40e-93 89 704 58 659
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) OX=441772 GN=pbpA PE=3 SV=1
A5I6G4 1.48e-93 89 704 58 659
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) OX=441771 GN=pbpA PE=3 SV=1
A7FY32 1.48e-93 89 704 58 659
Penicillin-binding protein 1A OS=Clostridium botulinum (strain ATCC 19397 / Type A) OX=441770 GN=pbpA PE=3 SV=1
Q891X1 1.93e-86 111 740 80 713
Penicillin-binding protein 1A OS=Clostridium tetani (strain Massachusetts / E88) OX=212717 GN=pbpA PE=3 SV=1
Q0TNZ8 1.52e-83 29 726 14 703
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

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
0.999910 0.000115 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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