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CAZyme Information: MGYG000001805_00877

You are here: Home > Sequence: MGYG000001805_00877

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 MGYG000001805_00877
CAZy Family PL1
CAZyme Description Pectate trisaccharide-lyase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
521 MGYG000001805_24|CGC1 57120.49 4.5561
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001805 1812910 MAG Denmark Europe
Gene Location Start: 20403;  End: 21968  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001805_00877.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 131 341 2.7e-42 0.8465346534653465

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 2.37e-43 17 428 1 344
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 2.34e-36 134 338 12 186
Amb_all domain.
pfam00544 Pec_lyase_C 2.69e-21 134 318 30 190
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
QUT75310.1 4.34e-113 42 463 23 423
QHJ07062.1 2.91e-38 65 428 66 369
QNH62939.1 4.89e-36 49 428 61 378
AUX34030.1 1.66e-31 63 429 127 410
QEI14009.1 1.24e-28 61 354 15 256

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ZSC_A 4.08e-27 47 428 8 331
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
3VMV_A 1.73e-21 61 338 10 246
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]
1VBL_A 8.94e-21 132 428 124 415
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
5AMV_A 4.75e-19 222 428 191 398
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 5.63e-19 222 428 212 419
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 2.58e-27 28 428 22 339
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 2.58e-27 28 428 22 339
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q8GCB2 2.58e-27 28 428 22 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
B1L969 3.36e-26 12 428 1 356
Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1
Q9WYR4 6.41e-26 12 428 3 358
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
0.000302 0.998857 0.000301 0.000179 0.000171 0.000158

TMHMM  Annotations      download full data without filtering help

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