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CAZyme Information: MGYG000004708_01203

You are here: Home > Sequence: MGYG000004708_01203

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 MGYG000004708_01203
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
703 76358.74 6.0364
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004708 1820911 MAG China Asia
Gene Location Start: 2435;  End: 4546  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004708_01203.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 79 258 1.6e-50 0.8811881188118812

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 8.86e-57 18 308 29 324
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 1.65e-45 91 259 14 190
Amb_all domain.
pfam00544 Pec_lyase_C 6.97e-29 68 255 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.
pfam16656 Pur_ac_phosph_N 0.005 339 412 37 94
Purple acid Phosphatase, N-terminal domain. This domain is found at the N-terminus of Purple acid phosphatase proteins.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CAW91090.1 1.12e-56 17 325 51 341
CAW61449.1 1.12e-56 17 325 51 341
CAX06650.1 1.12e-56 17 325 51 341
CAW70615.1 1.12e-56 17 325 51 341
CAW46004.1 1.12e-56 17 325 51 341

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ZSC_A 8.03e-35 24 230 7 211
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
3VMV_A 3.39e-26 29 258 7 249
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 4.15e-26 36 230 17 244
ChainA, PECTATE LYASE E [Dickeya chrysanthemi]
5AMV_A 2.48e-21 80 246 113 309
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 3.09e-21 80 246 134 330
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 2.79e-38 5 230 13 238
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 4.99e-38 5 230 11 236
Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1
O59939 1.68e-29 36 269 52 279
Pectate lyase B OS=Colletotrichum gloeosporioides OX=474922 GN=PLB PE=3 SV=1
Q9C2Z0 3.01e-28 14 325 24 318
Pectate lyase A OS=Aspergillus niger OX=5061 GN=plyA PE=1 SV=1
A2QV36 3.01e-28 14 325 24 318
Probable pectate lyase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=plyA 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
0.000800 0.550953 0.447352 0.000342 0.000289 0.000256

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004708_01203.