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CAZyme Information: MGYG000001240_00796

You are here: Home > Sequence: MGYG000001240_00796

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 sp900557405
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900557405
CAZyme ID MGYG000001240_00796
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
510 MGYG000001240_17|CGC1 56150.04 6.6233
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001240 2497614 MAG Austria Europe
Gene Location Start: 28050;  End: 29582  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001240_00796.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 120 330 3.4e-39 0.8465346534653465

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00656 Amb_all 3.42e-32 123 304 12 162
Amb_all domain.
COG3866 PelB 7.26e-32 1 416 1 344
Pectate lyase [Carbohydrate transport and metabolism].
pfam00544 Pec_lyase_C 3.61e-21 123 303 30 186
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 1.26e-119 31 420 23 387
QHJ07062.1 4.54e-37 54 416 66 369
QNH62939.1 4.17e-36 38 416 64 378
SCA88301.1 7.01e-29 31 416 36 334
QAT67521.1 7.01e-29 31 416 36 334

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 4.04e-21 53 416 13 325
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 2.99e-20 52 311 19 220
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
1VBL_A 1.60e-19 123 304 128 300
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
5AMV_A 3.64e-17 209 307 189 297
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 4.21e-17 209 307 210 318
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
B1B6T1 1.39e-28 31 416 41 339
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q8GCB2 1.39e-28 31 416 41 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q65DC2 1.39e-28 31 416 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
B1L969 6.71e-20 52 311 44 245
Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1
Q9WYR4 4.11e-19 52 311 46 247
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
0.000311 0.998872 0.000311 0.000183 0.000175 0.000163

TMHMM  Annotations      download full data without filtering help

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