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CAZyme Information: MGYG000004429_00081

You are here: Home > Sequence: MGYG000004429_00081

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 MGYG000004429_00081
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
936 98991.28 5.0183
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004429 2352873 MAG Israel Asia
Gene Location Start: 7980;  End: 10790  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004429_00081.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM77 588 692 6.4e-37 0.9805825242718447
PL1 250 435 4e-34 0.8217821782178217

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam18283 CBM77 1.27e-34 585 694 1 108
Carbohydrate binding module 77. This domain is the non-catalytic carbohydrate binding module 77 (CBM77) present in Ruminococcus flavefaciens. CBMs fulfil a critical targeting function in plant cell wall depolymerisation. In CBM77, a cluster of conserved basic residues (Lys1092, Lys1107 and Lys1162) confer calcium-independent recognition of homogalacturonan.
COG3866 PelB 1.26e-26 250 438 98 278
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 1.27e-17 254 437 17 190
Amb_all domain.
pfam00544 Pec_lyase_C 9.43e-11 232 433 9 211
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.
cd08547 Type_II_cohesin 1.56e-07 750 839 14 107
Type II cohesin domain, interaction partner of dockerin. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type II cohesins; their interactions with dockerin mediate attachment of the cellulosome complex to the bacterial cell wall.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBF42492.1 8.90e-134 2 535 5 504
ACR71161.1 4.30e-102 33 704 41 900
ADU23076.1 1.34e-91 27 535 751 1239
BCJ94010.1 5.81e-80 23 694 32 712
CDR31241.1 6.29e-80 38 543 334 817

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5FU5_A 8.07e-35 581 700 3 117
Thecomplexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition [Ruminococcus flavefaciens]
3VMV_A 2.99e-19 209 435 45 248
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 1.51e-13 254 433 133 330
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
5AMV_A 5.65e-13 228 417 102 302
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 6.36e-13 228 417 123 323
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
P0C1C3 4.31e-17 210 443 71 288
Pectate lyase 3 OS=Pectobacterium carotovorum subsp. carotovorum OX=555 GN=pel3 PE=3 SV=1
B1B6T1 9.46e-17 202 440 61 279
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q65DC2 9.46e-17 202 440 61 279
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 9.46e-17 202 440 61 279
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q6CZT2 1.86e-16 210 443 71 288
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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000281 0.998973 0.000192 0.000203 0.000169 0.000155

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004429_00081.