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CAZyme Information: MGYG000004879_02362

You are here: Home > Sequence: MGYG000004879_02362

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; Lachnospirales; Lachnospiraceae; Clostridium_N;
CAZyme ID MGYG000004879_02362
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
789 86036.32 4.3989
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004879 3926800 MAG China Asia
Gene Location Start: 9530;  End: 11899  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 4.2.2.2

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 288 548 5.8e-32 0.8366336633663366

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00656 Amb_all 1.02e-14 289 508 10 166
Amb_all domain.
COG3866 PelB 1.71e-09 258 684 67 344
Pectate lyase [Carbohydrate transport and metabolism].
pfam00544 Pec_lyase_C 1.68e-06 292 387 34 134
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
ADL50775.1 7.31e-218 166 696 34 552
BAV13078.1 8.08e-218 166 696 37 555
QNF29855.1 2.40e-214 166 703 33 557
QYR22341.1 1.41e-208 166 696 33 552
AFH62972.1 2.76e-198 166 696 32 550

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GT5_A 8.46e-41 185 513 8 300
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 2.86e-08 318 414 90 193
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
5AMV_A 6.41e-08 210 513 34 303
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 6.82e-08 210 513 55 324
BacillusSubtilis Pectate Lyase [Bacillus subtilis]
2BSP_A 1.58e-07 210 513 55 324
ChainA, PROTEIN (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 1.54e-40 169 513 22 329
Pectate lyase B OS=Paenibacillus amylolyticus OX=1451 GN=pelB PE=1 SV=1
Q9WYR4 3.43e-10 318 414 117 220
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 1.41e-09 318 414 115 218
Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1
P39116 3.73e-07 210 513 55 324
Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 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
0.009390 0.924570 0.058385 0.006604 0.000745 0.000283

TMHMM  Annotations      download full data without filtering help

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