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CAZyme Information: MGYG000003431_01035

You are here: Home > Sequence: MGYG000003431_01035

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; HUN007;
CAZyme ID MGYG000003431_01035
CAZy Family CBM35
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
639 70994.91 4.1276
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003431 2512610 MAG Fiji Oceania
Gene Location Start: 3016;  End: 4935  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.78

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH26 187 513 6.3e-109 0.9933993399339934
CBM35 67 169 5.7e-23 0.8739495798319328

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02156 Glyco_hydro_26 1.62e-56 187 513 2 311
Glycosyl hydrolase family 26.
cd04086 CBM35_mannanase-like 5.93e-34 36 170 1 119
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.
COG4124 ManB2 1.15e-16 312 432 139 266
Beta-mannanase [Carbohydrate transport and metabolism].
cd14256 Dockerin_I 1.42e-15 572 627 1 56
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.
pfam00404 Dockerin_1 1.40e-10 573 627 1 55
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
ADU21882.1 1.33e-290 7 630 9 597
CBL18146.1 4.11e-209 30 611 29 585
AEV68433.1 1.22e-206 11 607 20 557
BAB19050.1 4.26e-205 12 594 12 546
ALX07411.1 1.71e-204 12 594 12 546

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ZM8_A 2.92e-75 71 514 33 447
ChainA, Gh26 Endo-beta-1,4-mannanase [Podospora anserina S mat+]
3WDQ_A 5.84e-58 187 515 36 353
Crystalstructure of beta-mannanase from a symbiotic protist of the termite Reticulitermes speratus [Symbiotic protist of Reticulitermes speratus],3WDR_A Crystal structure of beta-mannanase from a symbiotic protist of the termite Reticulitermes speratus complexed with gluco-manno-oligosaccharide [Symbiotic protist of Reticulitermes speratus]
6HF2_A 8.40e-56 171 498 31 329
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]
6HPF_A 1.34e-55 180 514 1 310
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 5.40e-43 185 492 4 317
Crystalstructure of the GH26 domain from PbGH26-GH5A endo-beta-mannanase/endo-beta-glucanase from Prevotella bryantii [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
P55297 2.80e-85 36 515 22 462
Mannan endo-1,4-beta-mannosidase B OS=Piromyces sp. OX=45796 GN=MANB PE=2 SV=1
P55298 2.96e-83 36 515 21 460
Mannan endo-1,4-beta-mannosidase C OS=Piromyces sp. OX=45796 GN=MANC PE=2 SV=1
P55296 1.12e-80 36 515 22 461
Mannan endo-1,4-beta-mannosidase A OS=Piromyces sp. OX=45796 GN=MANA PE=2 SV=1
G2Q4H7 3.08e-78 13 514 13 476
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 1.42e-68 36 523 17 466
Mannan endo-1,4-beta-mannosidase OS=Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) OX=518766 GN=manA PE=1 SV=3

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
0.000264 0.999045 0.000179 0.000168 0.000163 0.000145

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003431_01035.