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CAZyme Information: MGYG000003993_01603

You are here: Home > Sequence: MGYG000003993_01603

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 Alistipes sp900550925
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900550925
CAZyme ID MGYG000003993_01603
CAZy Family GT51
CAZyme Description Penicillin-binding protein 1A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
805 91181.57 7.6918
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003993 1895769 MAG United Kingdom Europe
Gene Location Start: 49811;  End: 52228  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003993_01603.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT51 68 270 1.3e-55 0.9943502824858758

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0744 MrcB 4.78e-132 46 736 40 577
Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
TIGR02074 PBP_1a_fam 5.10e-131 102 729 8 500
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 1.54e-129 16 803 3 758
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
PRK11636 mrcA 6.44e-79 46 734 32 747
penicillin-binding protein 1a; Provisional
TIGR02071 PBP_1b 9.47e-74 96 732 149 659
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]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBL01595.1 0.0 15 792 11 789
AFL77271.1 0.0 15 791 11 788
BBL09453.1 0.0 28 792 5 770
BBL12246.1 0.0 28 792 5 770
BBL13842.1 0.0 15 792 11 789

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4OON_A 6.08e-76 51 785 10 743
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]
3UDF_A 6.40e-64 97 758 40 714
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]
5U2G_A 7.22e-55 45 786 5 779
2.6Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20],5U2G_B 2.6 Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20]
5FGZ_A 4.14e-41 59 740 122 679
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 4.72e-41 59 740 143 700
CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [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
Q07806 5.79e-77 46 785 32 770
Penicillin-binding protein 1A OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=mrcA PE=1 SV=2
O87579 2.54e-75 35 752 23 698
Penicillin-binding protein 1A OS=Neisseria lactamica OX=486 GN=mrcA PE=3 SV=1
O05131 1.27e-74 25 752 17 698
Penicillin-binding protein 1A OS=Neisseria gonorrhoeae OX=485 GN=mrcA PE=1 SV=3
Q5FAC7 1.27e-74 25 752 17 698
Penicillin-binding protein 1A OS=Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) OX=242231 GN=mrcA PE=3 SV=3
O87626 1.75e-74 24 756 16 701
Penicillin-binding protein 1A OS=Neisseria flavescens OX=484 GN=mrcA 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
1.000053 0.000007 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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