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1OIM

Family 1 b-glucosidase from Thermotoga maritima

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008152biological_processmetabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016052biological_processcarbohydrate catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
A0102483molecular_functionscopolin beta-glucosidase activity
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008152biological_processmetabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016052biological_processcarbohydrate catabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030245biological_processcellulose catabolic process
B0102483molecular_functionscopolin beta-glucosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NOJ A1447
ChainResidue
AGLN20
ATRP406
AHOH2274
AHIS121
AASN165
AGLU166
ATYR295
ATRP324
AGLU351
ATRP398
AGLU405

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NOJ B1447
ChainResidue
BGLN20
BHIS121
BASN165
BGLU166
BTYR295
BTRP324
BGLU351
BTRP398
BGLU405
BTRP406
BHOH2101

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. VYITENGAA
ChainResidueDetails
AVAL347-ALA355

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGvAtASYQiEgS
ChainResidueDetails
APHE10-SER24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255
ChainResidueDetails
AGLU166
BGLU166

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055
ChainResidueDetails
AGLU351
BGLU351

218853

PDB entries from 2024-04-24

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