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CAZyme Information: MGYG000003680_00882

You are here: Home > Sequence: MGYG000003680_00882

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 Prevotella sp000433175
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp000433175
CAZyme ID MGYG000003680_00882
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
520 57831.88 6.4487
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003680 2339843 MAG Italy Europe
Gene Location Start: 13701;  End: 15263  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003680_00882.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 131 341 8.5e-44 0.8465346534653465

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 6.29e-43 19 427 5 344
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 2.41e-37 134 342 12 190
Amb_all domain.
pfam00544 Pec_lyase_C 1.28e-24 169 338 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 5.21e-122 23 438 8 391
SCA88301.1 1.35e-37 24 427 10 334
QAT67521.1 1.35e-37 24 427 10 334
QNH62939.1 1.40e-37 63 427 77 378
ASB86827.1 7.34e-36 42 427 41 339

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1VBL_A 2.34e-23 132 427 124 415
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
3VMV_A 6.06e-23 63 338 12 246
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]
3ZSC_A 7.49e-23 64 427 20 331
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
5AMV_A 2.14e-22 222 427 191 398
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 2.64e-22 222 427 212 419
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
Q65DC2 1.33e-34 42 427 41 339
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
B1B6T1 1.33e-34 42 427 41 339
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q8GCB2 1.33e-34 42 427 41 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
B1L969 1.73e-22 24 427 14 356
Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1
Q9WYR4 2.40e-22 24 427 16 358
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
0.000376 0.998822 0.000248 0.000186 0.000172 0.000156

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003680_00882.