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CAZyme Information: MGYG000001927_02164

You are here: Home > Sequence: MGYG000001927_02164

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 sp900547005
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900547005
CAZyme ID MGYG000001927_02164
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
507 MGYG000001927_50|CGC1 55231.88 6.1282
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001927 2803818 MAG Denmark Europe
Gene Location Start: 8203;  End: 9726  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001927_02164.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 118 328 9e-41 0.8465346534653465

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 8.48e-37 60 414 56 344
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 9.06e-35 121 329 12 190
Amb_all domain.
pfam00544 Pec_lyase_C 5.08e-24 121 325 30 211
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 1.34e-128 4 502 2 475
QHJ07062.1 3.02e-36 31 414 55 369
QQQ79948.1 1.07e-31 4 415 6 327
AAR45486.1 1.50e-31 29 414 2 300
CAW79729.1 1.80e-31 8 414 15 339

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 2.94e-21 50 327 12 248
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 3.57e-21 51 414 20 331
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
5AMV_A 7.56e-20 154 305 150 297
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]
1BN8_A 9.02e-20 154 305 171 318
BacillusSubtilis Pectate Lyase [Bacillus subtilis]
1VBL_A 1.17e-19 119 302 124 300
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B1B6T1 3.59e-32 8 414 15 339
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q8GCB2 3.59e-32 8 414 15 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q65DC2 3.59e-32 8 414 15 339
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
Q00645 2.95e-20 50 327 45 260
Pectate lyase plyB OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyB PE=1 SV=1
Q9WYR4 5.00e-20 51 414 47 358
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
0.001298 0.996705 0.000581 0.000484 0.000474 0.000420

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001927_02164.