logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004009_01076

You are here: Home > Sequence: MGYG000004009_01076

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; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella;
CAZyme ID MGYG000004009_01076
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
520 57964.92 5.9609
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004009 2059820 MAG United Kingdom Europe
Gene Location Start: 6024;  End: 7586  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 4.2.2.2 4.2.2.9

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 131 341 2e-42 0.8465346534653465

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 9.50e-40 25 427 14 344
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 1.19e-34 134 342 12 190
Amb_all domain.
pfam00544 Pec_lyase_C 1.67e-21 169 338 41 211
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
QUT75310.1 8.84e-120 42 462 23 423
QNH62939.1 3.83e-38 63 427 77 378
QHJ07062.1 5.26e-37 44 427 55 369
SCA88301.1 2.98e-33 42 427 36 334
QAT67521.1 2.98e-33 42 427 36 334

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ZSC_A 2.52e-22 47 427 8 331
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
5AMV_A 4.20e-21 167 319 150 298
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 5.10e-21 167 319 171 319
BacillusSubtilis Pectate Lyase [Bacillus subtilis]
3VMV_A 7.78e-21 63 361 12 260
Crystalstructure of pectate lyase Bsp165PelA from Bacillus sp. N165 [Bacillus sp. N16-5],3VMW_A Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with trigalacturonate [Bacillus sp. N16-5]
2BSP_A 1.24e-20 167 319 171 319
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
Q8GCB2 9.10e-34 29 427 27 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
B1B6T1 9.10e-34 29 427 27 339
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q65DC2 9.10e-34 29 427 27 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=BLi04129 PE=3 SV=1
B1L969 1.43e-21 47 427 33 356
Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1
Q9WYR4 3.62e-21 47 427 35 358
Pectate trisaccharide-lyase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pelA 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
0.000407 0.998651 0.000308 0.000213 0.000204 0.000180

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004009_01076.