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CAZyme Information: MGYG000004725_00752

You are here: Home > Sequence: MGYG000004725_00752

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 UBA9475 sp900554075
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA9475; UBA9475 sp900554075
CAZyme ID MGYG000004725_00752
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
857 92487.97 5.0852
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004725 2206830 MAG Denmark Europe
Gene Location Start: 6490;  End: 9063  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004725_00752.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 232 422 1.3e-40 0.8366336633663366

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 1.23e-27 235 424 99 278
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 2.67e-24 236 421 15 188
Amb_all domain.
pfam00544 Pec_lyase_C 8.34e-18 302 419 89 211
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
ADU23076.1 7.75e-176 28 505 759 1237
ACR71161.1 6.27e-155 31 503 46 558
BBF42492.1 3.44e-113 31 512 41 509
CDR31241.1 1.06e-99 31 507 334 809
ADZ82421.1 4.15e-61 29 515 39 489

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 1.80e-16 237 503 79 321
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]
5AMV_A 6.83e-15 123 401 12 300
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 7.87e-15 123 401 33 321
BacillusSubtilis Pectate Lyase [Bacillus subtilis]
2BSP_A 1.85e-14 123 401 33 321
ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis]
2NZM_A 3.82e-14 123 401 12 300
ChainA, Pectate lyase [Bacillus subtilis],2O04_A Chain A, Pectate lyase [Bacillus subtilis],2O0V_A Chain A, Pectate lyase [Bacillus subtilis],2O0W_A Chain A, Pectate lyase [Bacillus subtilis],2O17_A Chain A, Pectate lyase [Bacillus subtilis],2O1D_A Chain A, 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
P39116 4.31e-14 123 401 33 321
Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 SV=1
P04959 7.35e-14 189 503 64 361
Pectate lyase B OS=Dickeya chrysanthemi OX=556 GN=pelB PE=3 SV=1
P0C1C1 9.78e-13 189 428 64 286
Pectate lyase 2 OS=Pectobacterium carotovorum OX=554 GN=pel2 PE=3 SV=1
Q6CZT3 1.30e-12 189 428 64 286
Pectate lyase 2 OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=pel2 PE=1 SV=1
Q65DC2 2.36e-12 266 503 122 335
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

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
0.000329 0.998764 0.000248 0.000220 0.000208 0.000193

TMHMM  Annotations      download full data without filtering help

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