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CAZyme Information: MGYG000003514_02125

You are here: Home > Sequence: MGYG000003514_02125

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 Fibrobacter_A intestinalis
Lineage Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae; Fibrobacter_A; Fibrobacter_A intestinalis
CAZyme ID MGYG000003514_02125
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
596 61926.07 6.5008
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003514 2933446 MAG Fiji Oceania
Gene Location Start: 72259;  End: 74049  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003514_02125.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 71 255 7.6e-53 0.8465346534653465

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 1.16e-51 7 306 8 329
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 1.67e-41 64 258 3 190
Amb_all domain.
pfam00544 Pec_lyase_C 1.27e-22 76 254 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
ADL26594.1 1.61e-177 11 464 21 487
ACX73788.1 1.61e-177 11 464 21 487
AEW00861.1 1.15e-81 9 329 8 323
AYN03314.1 2.57e-67 29 328 58 363
QZK90224.1 1.43e-66 29 328 55 364

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ZSC_A 1.02e-25 15 247 7 225
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
3VMV_A 1.47e-25 29 323 6 321
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 2.40e-22 20 230 1 246
ChainA, PECTATE LYASE E [Dickeya chrysanthemi]
1VBL_A 2.88e-21 76 254 128 330
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
5AMV_A 1.14e-18 106 253 149 324
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GCB2 7.91e-29 24 305 41 323
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
B1B6T1 7.91e-29 24 305 41 323
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q65DC2 7.91e-29 24 305 41 323
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
Q60140 4.64e-24 2 299 10 357
Pectate lyase OS=Pseudomonas viridiflava OX=33069 GN=pel PE=3 SV=1
Q59671 6.27e-24 13 302 20 351
Pectate lyase OS=Pseudomonas fluorescens OX=294 GN=pel 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
0.000202 0.999168 0.000153 0.000160 0.000143 0.000134

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003514_02125.