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CAZyme Information: MGYG000001543_02471

You are here: Home > Sequence: MGYG000001543_02471

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 Lachnoclostridium sp900078195
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnoclostridium; Lachnoclostridium sp900078195
CAZyme ID MGYG000001543_02471
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
552 MGYG000001543_7|CGC10 61772.34 6.0786
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001543 4599950 Isolate not provided not provided
Gene Location Start: 925364;  End: 927022  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 4.2.2.2

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 150 405 1.4e-31 0.8118811881188119

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00656 Amb_all 2.66e-13 155 366 19 167
Amb_all domain.
COG3866 PelB 6.46e-10 90 365 52 251
Pectate lyase [Carbohydrate transport and metabolism].
pfam00544 Pec_lyase_C 0.008 175 364 59 190
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
QNF29855.1 2.51e-314 1 551 1 551
QGH35942.1 2.16e-308 1 549 1 549
QYR22341.1 1.97e-281 3 550 2 552
ADL50775.1 3.55e-270 16 551 17 553
BAV13078.1 3.94e-270 16 551 20 556

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GT5_A 2.82e-45 52 550 8 446
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 4.13e-09 151 377 52 228
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
5AMV_A 9.32e-09 55 366 15 299
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 9.92e-09 55 366 36 320
BacillusSubtilis Pectate Lyase [Bacillus subtilis]
3KRG_A 2.18e-08 55 366 15 299
ChainA, 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 2.53e-45 70 379 56 339
Pectate lyase B OS=Paenibacillus amylolyticus OX=1451 GN=pelB PE=1 SV=1
Q9WYR4 1.13e-10 151 377 79 255
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 4.67e-10 151 377 77 253
Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1
Q59671 2.71e-08 163 398 120 314
Pectate lyase OS=Pseudomonas fluorescens OX=294 GN=pel PE=3 SV=1
P39116 5.43e-08 55 366 36 320
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
0.001284 0.778420 0.219512 0.000307 0.000248 0.000215

TMHMM  Annotations      download full data without filtering help

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