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CAZyme Information: MGYG000000852_01232

You are here: Home > Sequence: MGYG000000852_01232

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 Prevotella sp900545525
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900545525
CAZyme ID MGYG000000852_01232
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
521 MGYG000000852_12|CGC1 56860.97 6.8381
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000852 2918004 MAG China Asia
Gene Location Start: 27457;  End: 29022  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000852_01232.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 133 342 1.1e-40 0.8415841584158416

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 2.86e-37 74 428 56 344
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 9.07e-34 135 343 12 190
Amb_all domain.
pfam00544 Pec_lyase_C 1.42e-21 174 315 45 186
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
QUT75310.1 2.37e-116 43 474 23 433
QHJ07062.1 1.52e-38 66 428 66 369
AAR45486.1 7.52e-34 43 428 2 300
AYQ18433.1 9.29e-34 43 428 41 339
QFY40851.1 9.29e-34 43 428 41 339

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 3.89e-24 64 344 12 251
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]
2QXZ_A 8.28e-21 210 427 110 326
ChainA, pectate lyase II [Xanthomonas campestris pv. campestris],2QXZ_B Chain B, pectate lyase II [Xanthomonas campestris pv. campestris]
2QY1_A 8.28e-21 210 427 110 326
ChainA, Pectate lyase II [Xanthomonas campestris pv. campestris],2QY1_B Chain B, Pectate lyase II [Xanthomonas campestris pv. campestris]
3ZSC_A 5.75e-20 65 428 20 331
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
2QX3_A 1.24e-19 210 427 110 326
Structureof pectate lyase II from Xanthomonas campestris pv. campestris str. ATCC 33913 [Xanthomonas campestris pv. campestris],2QX3_B Structure of pectate lyase II from Xanthomonas campestris pv. campestris str. ATCC 33913 [Xanthomonas campestris pv. campestris]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q65DC2 3.53e-34 43 428 41 339
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 3.53e-34 43 428 41 339
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
B1B6T1 3.53e-34 43 428 41 339
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
P04959 1.21e-21 219 427 155 364
Pectate lyase B OS=Dickeya chrysanthemi OX=556 GN=pelB PE=3 SV=1
B1L969 3.91e-20 65 428 45 356
Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA 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
0.006949 0.804305 0.187554 0.000434 0.000400 0.000342

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000852_01232.