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CAZyme Information: MGYG000000852_01386

You are here: Home > Sequence: MGYG000000852_01386

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 sp900545525
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900545525
CAZyme ID MGYG000000852_01386
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
703 MGYG000000852_14|CGC1 77955.31 6.3423
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000852 2918004 MAG China Asia
Gene Location Start: 48797;  End: 50908  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000852_01386.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 60 261 1.2e-51 0.9752475247524752

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 4.60e-57 7 328 15 337
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 2.83e-44 83 262 3 190
Amb_all domain.
pfam00544 Pec_lyase_C 1.78e-28 71 258 8 211
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
CAW91090.1 2.17e-57 28 335 59 346
CAW61449.1 2.17e-57 28 335 59 346
CAX06650.1 2.17e-57 28 335 59 346
CAW70615.1 2.17e-57 28 335 59 346
CAW46004.1 2.17e-57 28 335 59 346

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ZSC_A 1.71e-35 28 234 8 212
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
3VMV_A 3.61e-28 39 300 13 282
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]
1PCL_A 1.52e-27 39 233 17 244
ChainA, PECTATE LYASE E [Dickeya chrysanthemi]
5AMV_A 1.66e-23 92 249 123 309
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 2.13e-23 92 249 144 330
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
Q9WYR4 8.01e-39 28 234 35 239
Pectate trisaccharide-lyase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pelA PE=1 SV=1
B1L969 1.43e-38 28 234 33 237
Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1
O59939 3.14e-33 39 274 52 281
Pectate lyase B OS=Colletotrichum gloeosporioides OX=474922 GN=PLB PE=3 SV=1
A1CYB8 2.56e-31 67 286 63 286
Probable pectate lyase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=plyA PE=3 SV=1
Q5AVN4 9.91e-31 39 274 51 277
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

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
0.024127 0.588766 0.384096 0.001969 0.000604 0.000396

TMHMM  Annotations      download full data without filtering help

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