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CAZyme Information: MGYG000002414_02564

You are here: Home > Sequence: MGYG000002414_02564

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 Paenibacillus odorifer
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus odorifer
CAZyme ID MGYG000002414_02564
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
551 MGYG000002414_1|CGC58 58729.61 5.6407
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002414 6802552 Isolate South Korea Asia
Gene Location Start: 2923542;  End: 2925197  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002414_02564.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 199 423 2.5e-44 0.8217821782178217

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00656 Amb_all 1.45e-29 199 392 6 160
Amb_all domain.
COG3866 PelB 1.21e-25 209 537 108 344
Pectate lyase [Carbohydrate transport and metabolism].
pfam00544 Pec_lyase_C 8.70e-20 207 434 41 208
Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AWV33413.1 0.0 1 551 1 551
ANY66001.1 4.74e-255 107 549 274 716
ANY65996.1 3.02e-242 109 547 253 691
ASA26290.1 5.31e-230 105 549 17 462
AEI39060.1 1.16e-229 111 549 35 474

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GT5_A 4.27e-224 109 549 5 446
Structuralbasis of the specific activity and thermostability of pectate lyase (pelN) from Paenibacillus sp. 0602 [Paenibacillus sp. 0602],5GT5_B Structural basis of the specific activity and thermostability of pectate lyase (pelN) from Paenibacillus sp. 0602 [Paenibacillus sp. 0602]
3ZSC_A 5.96e-21 206 392 71 210
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
1VBL_A 2.68e-18 211 392 141 298
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
5AMV_A 5.91e-15 116 392 17 292
Structuralinsights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168]
1BN8_A 6.69e-15 116 392 38 313
BacillusSubtilis Pectate Lyase [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
D3JTC2 5.43e-179 109 463 34 388
Pectate lyase B OS=Paenibacillus amylolyticus OX=1451 GN=pelB PE=1 SV=1
Q9WYR4 1.04e-20 206 392 98 237
Pectate trisaccharide-lyase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pelA PE=1 SV=1
B1L969 3.34e-20 206 392 96 235
Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1
Q56806 4.72e-16 110 392 31 275
Pectate lyase OS=Xanthomonas campestris pv. malvacearum OX=86040 PE=3 SV=1
Q59671 2.78e-15 115 392 40 278
Pectate lyase OS=Pseudomonas fluorescens OX=294 GN=pel 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
1.000049 0.000013 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002414_02564.