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CAZyme Information: MGYG000001151_01319

You are here: Home > Sequence: MGYG000001151_01319

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 Ruminococcus_C sp000433635
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C sp000433635
CAZyme ID MGYG000001151_01319
CAZy Family GH5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
909 MGYG000001151_158|CGC1 99877.6 4.104
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001151 2508735 MAG China Asia
Gene Location Start: 16932;  End: 19661  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.78

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 68 388 8.1e-96 0.986159169550173
CBM23 535 698 1.8e-46 0.9938271604938271

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3934 COG3934 2.07e-39 44 421 4 312
Endo-1,4-beta-mannosidase [Carbohydrate transport and metabolism].
cd14256 Dockerin_I 1.82e-15 845 901 1 57
Type I dockerin repeat domain. 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 I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
pfam03425 CBM_11 1.46e-12 536 698 7 173
Carbohydrate binding domain (family 11).
pfam03442 CBM_X2 4.44e-10 441 521 1 83
Carbohydrate binding domain X2. This domain binds to cellulose and to bacterial cell walls. It is found in glycosyl hydrolases and in scaffolding proteins of cellulosomes (multiprotein glycosyl hydrolase complexes). In the cellulosome it may aid cellulose degradation by anchoring the cellulosome to the bacterial cell wall and by binding it to its substrate. This domain has an Ig-like fold.
pfam03442 CBM_X2 1.51e-09 712 774 4 68
Carbohydrate binding domain X2. This domain binds to cellulose and to bacterial cell walls. It is found in glycosyl hydrolases and in scaffolding proteins of cellulosomes (multiprotein glycosyl hydrolase complexes). In the cellulosome it may aid cellulose degradation by anchoring the cellulosome to the bacterial cell wall and by binding it to its substrate. This domain has an Ig-like fold.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL33682.1 5.90e-219 2 789 6 883
ADZ85047.1 1.94e-218 1 548 1 555
QEH70547.1 7.58e-218 1 548 1 555
CBK97477.1 5.50e-214 2 789 6 883
CCO04515.1 1.13e-193 1 780 5 876

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3PZ9_A 2.69e-83 45 407 21 365
Nativestructure of endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3PZG_A I222 crystal form of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3PZI_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 in complex with beta-D-glucose [Thermotoga petrophila RKU-1],3PZM_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with three glycerol molecules [Thermotoga petrophila RKU-1],3PZN_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with citrate and glycerol [Thermotoga petrophila RKU-1],3PZO_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 in complex with three maltose molecules [Thermotoga petrophila RKU-1],3PZQ_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with maltose and glycerol [Thermotoga petrophila RKU-1]
4QP0_A 3.58e-81 36 403 4 344
CrystalStructure Analysis of the Endo-1,4-beta-mannanase from Rhizomucor miehei [Rhizomucor miehei]
6TN6_A 2.70e-80 45 407 7 351
X-raystructure of the endo-beta-1,4-mannanase from Thermotoga petrophila [Thermotoga petrophila RKU-1]
3ZIZ_A 1.02e-64 22 409 2 338
ChainA, Gh5 Endo-beta-1,4-mannanase [Podospora anserina]
3WH9_A 3.42e-64 36 409 2 326
Theligand-free structure of ManBK from Aspergillus niger BK01 [Aspergillus niger],3WH9_B The ligand-free structure of ManBK from Aspergillus niger BK01 [Aspergillus niger]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B8NVK8 4.19e-71 1 412 1 369
Probable mannan endo-1,4-beta-mannosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=manA PE=3 SV=2
Q2TXJ2 8.05e-71 1 412 1 369
Probable mannan endo-1,4-beta-mannosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=manA PE=3 SV=1
A1D8Y6 2.67e-68 36 427 26 368
Probable mannan endo-1,4-beta-mannosidase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=manA PE=3 SV=1
Q00012 5.53e-67 11 409 8 356
Mannan endo-1,4-beta-mannosidase A OS=Aspergillus aculeatus OX=5053 GN=manA PE=1 SV=1
Q4WBS1 2.12e-66 36 409 97 422
Mannan endo-1,4-beta-mannosidase F OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=manF PE=1 SV=2

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
0.000731 0.997860 0.000467 0.000372 0.000277 0.000250

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001151_01319.