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1Y9G

Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004575molecular_functionsucrose alpha-glucosidase activity
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0005987biological_processsucrose catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0051669molecular_functionfructan beta-fructosidase activity
A0051670molecular_functioninulinase activity
Functional Information from PROSITE/UniProt
site_idPS00609
Number of Residues14
DetailsGLYCOSYL_HYDROL_F32 Glycosyl hydrolases family 32 active site. HfsPqknwMNDPNG
ChainResidueDetails
AHIS31-GLY44

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10067
ChainResidueDetails
AASP41

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU10067
ChainResidueDetails
AGLU241

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:15522299, ECO:0007744|PDB:1Y9G
ChainResidueDetails
AASN40
AASP41
AGLN57
ATRP65
ASER103
AARG188
AASP189
AGLU241
ATRP335

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN49
AASN112

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:39357631
ChainResidueDetails
AASN67

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15522299, ECO:0000269|PubMed:39357631, ECO:0007744|PDB:1Y4W, ECO:0007744|PDB:1Y9G
ChainResidueDetails
AASN111

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:39357631
ChainResidueDetails
AASN254

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15522299, ECO:0007744|PDB:1Y9M
ChainResidueDetails
AASN300

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15522299, ECO:0000269|PubMed:39357631, ECO:0007744|PDB:1Y4W, ECO:0007744|PDB:1Y9G, ECO:0007744|PDB:1Y9M
ChainResidueDetails
AASN398
AASN430

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1y9m
ChainResidueDetails
AGLU241
AASP41

site_idMCSA1
Number of Residues2
DetailsM-CSA 827
ChainResidueDetails
AASP41covalently attached, nucleofuge, nucleophile
AGLU241activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor

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PDB entries from 2025-06-18

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