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CAZyme Information: MGYG000002657_00942

You are here: Home > Sequence: MGYG000002657_00942

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; Lachnospiraceae; CAG-95;
CAZyme ID MGYG000002657_00942
CAZy Family GH94
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
897 MGYG000002657_16|CGC1 102146.69 5.6012
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002657 2838774 MAG United Republic of Tanzania Africa
Gene Location Start: 6495;  End: 9188  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.31

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH94 43 879 1.7e-150 0.6959459459459459

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11749 GH94N_LBP_like 8.45e-119 72 299 1 229
N-terminal-like domain of Paenibacillus sp. YM-1 Laminaribiose Phosphorylase and similar proteins. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes bacterial laminaribiose phosphorylase. This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Bacterial laminaribiose phosphorylase phosphorolyzes laminaribiose into alpha-glucose 1-phosphate and glucose, but does not phosphorolyze other glucobioses; it slightly phosphorolyzed laminaritriose and higher laminarioligosaccharides. The GH64N domain, as represented by this model, is also found at the N-terminus of GH94 members with uncharacterized specificities.
COG3459 COG3459 5.72e-39 102 897 367 1055
Cellobiose phosphorylase [Carbohydrate transport and metabolism].
pfam17167 Glyco_hydro_36 1.58e-22 319 808 1 425
Glycosyl hydrolase 36 superfamily, catalytic domain. This is the catalytic region of the superfamily of enzymes referred to as GH36. UniProtKB:Q76IQ9 is a chitobiose phosphorylase that catalyzes the reversible phosphorolysis of chitobiose into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration. The full-length enzyme comprises a beta sandwich domain and an (alpha/alpha)(6) barrel domain. The alpha-helical barrel component of the domain, this family, is the catalytic region.
cd11746 GH94N_like 1.45e-08 101 289 19 179
N-terminal domain of glycoside hydrolase family 94 and related domains. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. This GH64N domain also occurs in tandem repeat arrangements (not at the N-terminus) in cyclic beta 1-2 glucan synthetase and related proteins, and as a standalone domain in distantly related proteins of unknown function.
cd11751 GH94N_like_4 3.95e-06 116 295 47 223
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function. The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. The GH64N domain, as represented by this model, is found near the N-terminus of GH94 members and related proteins with uncharacterized specificities.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCJ95915.1 0.0 1 896 1 898
BCN29268.1 0.0 1 897 1 899
AEN96608.1 0.0 3 896 4 908
QHQ63065.1 0.0 1 867 1 868
QEH67127.1 0.0 1 893 1 894

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6GGY_A 3.50e-303 2 896 6 908
Paenibacillussp. YM1 laminaribiose phosphorylase with sulphate bound [Paenibacillus sp. YM1],6GGY_B Paenibacillus sp. YM1 laminaribiose phosphorylase with sulphate bound [Paenibacillus sp. YM1],6GH2_A Paenibacillus sp. YM1 laminaribiose phosphorylase with alpha-glc-1-phosphate bound [Paenibacillus sp. YM1],6GH2_B Paenibacillus sp. YM1 laminaribiose phosphorylase with alpha-glc-1-phosphate bound [Paenibacillus sp. YM1],6GH3_A Paenibacillus sp. YM1 laminaribiose phosphorylase with alpha-man-1-phosphate bound [Paenibacillus sp. YM1],6GH3_B Paenibacillus sp. YM1 laminaribiose phosphorylase with alpha-man-1-phosphate bound [Paenibacillus sp. YM1]
3QDE_A 7.59e-27 123 869 113 795
ChainA, Cellobiose phosphorylase [Acetivibrio thermocellus],3QDE_B Chain B, Cellobiose phosphorylase [Acetivibrio thermocellus]
3S4C_A 1.82e-15 126 820 116 761
Lactosephosphorylase in complex with sulfate [Cellulomonas uda],3S4D_A Lactose phosphorylase in a ternary complex with cellobiose and sulfate [Cellulomonas uda]
3RRS_A 5.46e-15 126 820 116 761
Crystalstructure analysis of cellobiose phosphorylase from Cellulomonas uda [Cellulomonas uda],3RRS_B Crystal structure analysis of cellobiose phosphorylase from Cellulomonas uda [Cellulomonas uda],3RSY_A Cellobiose phosphorylase from Cellulomonas uda in complex with sulfate and glycerol [Cellulomonas uda],3RSY_B Cellobiose phosphorylase from Cellulomonas uda in complex with sulfate and glycerol [Cellulomonas uda],3S4A_A Cellobiose phosphorylase from Cellulomonas uda in complex with cellobiose [Cellulomonas uda],3S4A_B Cellobiose phosphorylase from Cellulomonas uda in complex with cellobiose [Cellulomonas uda],3S4B_A Cellobiose phosphorylase from Cellulomonas uda in complex with glucose [Cellulomonas uda],3S4B_B Cellobiose phosphorylase from Cellulomonas uda in complex with glucose [Cellulomonas uda]
2CQS_A 2.87e-14 273 820 273 781
CrystalStructure of Cellvibrio gilvus Cellobiose Phosphorylase Crystallized from Ammonium Sulfate [Cellulomonas gilvus],2CQS_B Crystal Structure of Cellvibrio gilvus Cellobiose Phosphorylase Crystallized from Ammonium Sulfate [Cellulomonas gilvus],2CQT_A Crystal Structure of Cellvibrio gilvus Cellobiose Phosphorylase Crystallized from Sodium/Potassium Phosphate [Cellulomonas gilvus],2CQT_B Crystal Structure of Cellvibrio gilvus Cellobiose Phosphorylase Crystallized from Sodium/Potassium Phosphate [Cellulomonas gilvus],3QFY_A Crystal Structure of Cellvibrio gilvus Cellobiose Phosphorylase Complexed with Sulfate and Isofagomine [Cellulomonas gilvus],3QFY_B Crystal Structure of Cellvibrio gilvus Cellobiose Phosphorylase Complexed with Sulfate and Isofagomine [Cellulomonas gilvus],3QFZ_A Crystal Structure of Cellvibrio gilvus Cellobiose Phosphorylase Complexed with Sulfate and 1-Deoxynojirimycin [Cellulomonas gilvus],3QFZ_B Crystal Structure of Cellvibrio gilvus Cellobiose Phosphorylase Complexed with Sulfate and 1-Deoxynojirimycin [Cellulomonas gilvus],3QG0_A Crystal Structure of Cellvibrio gilvus Cellobiose Phosphorylase Complexed with Phosphate and 1-Deoxynojirimycin [Cellulomonas gilvus],3QG0_B Crystal Structure of Cellvibrio gilvus Cellobiose Phosphorylase Complexed with Phosphate and 1-Deoxynojirimycin [Cellulomonas gilvus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B9K7M6 4.20e-20 187 892 176 808
Cellobiose phosphorylase OS=Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E) OX=309803 GN=cbpA PE=1 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
1.000023 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002657_00942.