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CAZyme Information: MGYG000004067_01379

You are here: Home > Sequence: MGYG000004067_01379

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; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; ;
CAZyme ID MGYG000004067_01379
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
691 74423.9 4.1075
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004067 1958521 MAG United Kingdom Europe
Gene Location Start: 646;  End: 2721  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004067_01379.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 230 400 2.8e-42 0.8415841584158416

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 1.26e-55 134 405 34 280
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 3.52e-33 235 402 14 190
Amb_all domain.
pfam00544 Pec_lyase_C 5.86e-20 204 398 1 211
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
BCJ94010.1 1.82e-142 38 555 40 563
ACZ98651.1 2.84e-131 1 575 10 567
AGF55382.1 4.23e-131 25 555 71 593
AQR94278.1 1.31e-129 25 555 71 593
AIQ21570.1 3.03e-129 13 580 5 573

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 4.97e-25 195 512 38 321
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]
1VBL_A 5.51e-18 234 398 129 330
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
1PCL_A 5.73e-17 173 476 4 335
ChainA, PECTATE LYASE E [Dickeya chrysanthemi]
5AMV_A 6.49e-17 238 459 128 384
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 7.63e-17 238 459 149 405
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
Q65DC2 1.06e-24 185 406 64 280
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
Q8GCB2 1.06e-24 185 406 64 280
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
B1B6T1 1.06e-24 185 406 64 280
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
P04959 2.07e-17 155 404 26 285
Pectate lyase B OS=Dickeya chrysanthemi OX=556 GN=pelB PE=3 SV=1
Q6CZT2 2.84e-16 232 404 106 284
Pectate lyase 3 OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=pel3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000216 0.227342 0.772130 0.000120 0.000100 0.000078

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004067_01379.