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CAZyme Information: MGYG000002881_00574

You are here: Home > Sequence: MGYG000002881_00574

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; Oscillospirales; Ruminococcaceae; Ruminococcus;
CAZyme ID MGYG000002881_00574
CAZy Family GH26
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
591 66468.16 4.073
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002881 1270591 MAG United States North America
Gene Location Start: 20;  End: 1795  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.78

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH26 87 485 8e-83 0.9933993399339934

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02156 Glyco_hydro_26 6.18e-32 88 458 2 288
Glycosyl hydrolase family 26.
COG4124 ManB2 1.80e-09 303 398 178 266
Beta-mannanase [Carbohydrate transport and metabolism].
cd14256 Dockerin_I 1.48e-08 518 574 1 54
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.
cd04086 CBM35_mannanase-like 4.07e-07 1 71 49 118
Carbohydrate Binding Module 35 (CBM35); appended to several carbohydrate binding enzymes, including several glycoside hydrolase (GH) family 26 mannanase domains. This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes, including periplasmic component of ABC-type sugar transport system involved in carbohydrate transport and metabolism, and several glycoside hydrolase (GH) domains, including GH26. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. Examples of proteins having CMB35s belonging to this family are mannanase A from Clostridium thermocellum (GH26), Man26B from Paenibacillus sp. BME-14 (GH26), and the multifunctional Cel44C-Man26A from Paenibacillus polymyxa GS01 (which has two GH domains, GH44 and GH26). GH26 mainly includes mannan endo-1,4-beta-mannosidase which hydrolyzes 1,4-beta-D-linkages in mannans, galacto-mannans, glucomannans, and galactoglucomannans, but displays little activity towards other plant cell wall polysaccharides. A few proteins belonging to this family have additional CBM3 domains; these CBM3s are not found in the CBM6-CBM35-CBM36_like superfamily.
pfam00404 Dockerin_1 6.41e-04 519 574 1 53
Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QIN54096.1 5.07e-167 1 488 78 501
ADU21037.1 8.11e-160 1 499 86 532
AZK49093.1 2.56e-146 1 488 85 508
QKS59949.1 3.26e-146 1 503 98 530
APO46210.1 3.81e-146 1 488 85 508

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ZM8_A 6.49e-45 1 487 61 447
ChainA, Gh26 Endo-beta-1,4-mannanase [Podospora anserina S mat+]
6HPF_A 7.85e-36 188 487 36 310
Structureof Inactive E165Q mutant of fungal non-CBM carrying GH26 endo-b-mannanase from Yunnania penicillata in complex with alpha-62-61-di-galactosyl-mannotriose [Yunnania penicillata]
6D2X_A 8.24e-34 189 453 42 309
Crystalstructure of the GH26 domain from PbGH26-GH5A endo-beta-mannanase/endo-beta-glucanase from Prevotella bryantii [Prevotella bryantii B14]
6HF2_A 1.11e-33 197 454 91 316
Thestructure of BoMan26B, a GH26 beta-mannanase from Bacteroides ovatus [Bacteroides ovatus ATCC 8483],6HF4_A The structure of BoMan26B, a GH26 beta-mannanase from Bacteroides ovatus, complexed with G1M4 [Bacteroides ovatus ATCC 8483]
6D2W_A 2.50e-32 58 453 67 400
Crystalstructure of Prevotella bryantii endo-beta-mannanase/endo-beta-glucanase PbGH26A-GH5A [Prevotella bryantii B14],6D2W_B Crystal structure of Prevotella bryantii endo-beta-mannanase/endo-beta-glucanase PbGH26A-GH5A [Prevotella bryantii B14]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
G2Q4H7 5.91e-45 1 487 90 476
Mannan endo-1,4-beta-mannosidase OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=Man26A PE=1 SV=1
P49425 2.03e-36 17 488 76 458
Mannan endo-1,4-beta-mannosidase OS=Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) OX=518766 GN=manA PE=1 SV=3
P55298 1.21e-34 1 489 69 461
Mannan endo-1,4-beta-mannosidase C OS=Piromyces sp. OX=45796 GN=MANC PE=2 SV=1
P55297 2.08e-32 1 489 71 463
Mannan endo-1,4-beta-mannosidase B OS=Piromyces sp. OX=45796 GN=MANB PE=2 SV=1
Q5AWB7 3.76e-31 188 487 61 350
Probable mannan endo-1,4-beta-mannosidase E OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=manE PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000060 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002881_00574.