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CAZyme Information: MGYG000000024_01234

You are here: Home > Sequence: MGYG000000024_01234

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 Paraclostridium bifermentans
Lineage Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Paraclostridium; Paraclostridium bifermentans
CAZyme ID MGYG000000024_01234
CAZy Family CBM50
CAZyme Description Trifunctional nucleotide phosphoesterase protein YfkN
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1217 MGYG000000024_1|CGC16 135232.35 5.0488
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000024 3641600 Isolate United Kingdom Europe
Gene Location Start: 1273995;  End: 1277648  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000024_01234.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK09420 cpdB 0.0 31 657 16 649
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
PRK09418 PRK09418 0.0 4 664 2 662
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
TIGR01390 CycNucDiestase 0.0 39 620 1 583
2',3'-cyclic-nucleotide 2'-phosphodiesterase. 2',3'-cyclic-nucleotide 2'-phosphodiesterase is a bifunctional enzyme localized to the periplasm of Gram-negative bacteria. 2',3'-cyclic-nucleotide 2'-phosphodiesters are intermediates formed during the hydrolysis of RNA by the ribonuclease I, which is also found to the periplasm, and other enzymes of the RNAse T2 family. Bacteria are unable to transport 2',3'-cyclic-nucleotides into the cytoplasm. 2',3'-cyclic-nucleotide 2'-phosphodiesterase contains 2 active sites which catalyze the reactions that convert the 2',3'-cyclic-nucleotide into a 3'-nucleotide, which is then converted into nucleic acid and phosphate. Both final products can be transported into the cytoplasm. Thus, it has been suggested that 2',3'-cyclic-nucleotide 2'-phosphodiesterase has a 'scavenging' function. Experimental evidence indicates that 2',3'-cyclic-nucleotide 2'-phosphodiesterase enables Yersinia enterocolitica O:8 to grow on 2'3'-cAMP as a sole source of carbon and energy (). [Purines, pyrimidines, nucleosides, and nucleotides, Other]
PRK09419 PRK09419 0.0 2 1192 5 1143
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
PRK11907 PRK11907 0.0 24 634 94 702
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ANF95373.1 1.36e-141 4 657 9 666
AYQ74930.1 3.04e-138 4 655 6 662
QJD88116.1 7.45e-135 23 643 21 642
QHE51294.1 1.53e-134 8 666 12 676
ANY70674.1 7.32e-134 8 658 8 658

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3GVE_A 1.70e-59 39 371 10 341
Crystalstructure of calcineurin-like phosphoesterase YfkN from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],3GVE_B Crystal structure of calcineurin-like phosphoesterase YfkN from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
5EQV_A 3.12e-53 37 331 6 299
1.45Angstrom Crystal Structure of Bifunctional 2',3'-cyclic Nucleotide 2'-phosphodiesterase/3'-Nucleotidase Periplasmic Precursor Protein from Yersinia pestis with Phosphate bound to the Active site [Yersinia pestis CO92]
3JYF_A 2.60e-52 37 371 5 339
ChainA, 2',3'-cyclic nucleotide 2'-phosphodiesterase/3'-nucleotidase bifunctional periplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578],3JYF_B Chain B, 2',3'-cyclic nucleotide 2'-phosphodiesterase/3'-nucleotidase bifunctional periplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]
2Z1A_A 9.97e-39 669 1197 32 534
Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
3ZTV_A 1.69e-30 665 1195 11 570
Structureof Haemophilus influenzae NAD nucleotidase (NadN) [Haemophilus influenzae Rd KW20],3ZU0_A Structure of Haemophilus influenzae NAD nucleotidase (NadN) [Haemophilus influenzae Rd KW20],3ZU0_B Structure of Haemophilus influenzae NAD nucleotidase (NadN) [Haemophilus influenzae Rd KW20]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34313 5.24e-192 39 1184 43 1162
Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P08331 7.86e-132 31 614 14 598
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P26265 5.00e-125 31 614 14 598
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=cpdB PE=3 SV=2
P53052 4.51e-121 37 611 25 600
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1
P44764 1.41e-120 31 620 24 614
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=cpdB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000291 0.998927 0.000206 0.000194 0.000184 0.000151

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000024_01234.