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CAZyme Information: MGYG000001056_00579

You are here: Home > Sequence: MGYG000001056_00579

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 sp900556395
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900556395
CAZyme ID MGYG000001056_00579
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
523 57240.26 6.5933
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001056 3020119 MAG Spain Europe
Gene Location Start: 280;  End: 1851  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001056_00579.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 132 341 4.9e-41 0.8415841584158416

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00656 Amb_all 1.14e-35 134 344 12 190
Amb_all domain.
COG3866 PelB 4.90e-35 44 427 33 344
Pectate lyase [Carbohydrate transport and metabolism].
pfam00544 Pec_lyase_C 6.99e-22 119 314 11 186
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 4.49e-121 18 428 4 384
QNH62939.1 1.10e-38 63 427 77 378
QHJ07062.1 1.09e-37 5 427 11 369
AAR45486.1 5.03e-32 42 427 2 300
CAW79729.1 1.15e-31 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
1BN8_A 5.46e-20 17 318 2 318
BacillusSubtilis Pectate Lyase [Bacillus subtilis]
1VBL_A 7.09e-20 77 427 85 415
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
3VMV_A 8.78e-20 63 343 12 251
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]
5AMV_A 1.10e-19 167 318 150 297
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]
2BSP_A 1.32e-19 17 318 2 318
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
B1B6T1 2.29e-32 42 427 41 339
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q8GCB2 2.29e-32 42 427 41 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q65DC2 2.29e-32 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
Q5AVN4 3.24e-20 63 387 50 317
Pectate lyase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyA PE=1 SV=1
Q2TZY0 4.32e-20 63 315 45 234
Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 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
0.001577 0.995380 0.001945 0.000449 0.000332 0.000291

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001056_00579.