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1GPE

GLUCOSE OXIDASE FROM PENICILLIUM AMAGASAKIENSE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0046562molecular_functionbeta-D-glucose oxidase activity
A0050660molecular_functionflavin adenine dinucleotide binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0046562molecular_functionbeta-D-glucose oxidase activity
B0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. TAAQLAAGHSF
ChainResidueDetails
ATHR154-PHE164

site_idPS00623
Number of Residues24
DetailsGMC_OXRED_1 GMC oxidoreductases signature 1. GKgLGGSTlINgdsWtrPdkvqiD
ChainResidueDetails
AGLY101-ASP124

site_idPS00624
Number of Residues15
DetailsGMC_OXRED_2 GMC oxidoreductases signature 2. GSaiSPlILeySGIG
ChainResidueDetails
AGLY294-GLY308

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P13006
ChainResidueDetails
AALA538
BALA538

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0007744|PDB:1GPE
ChainResidueDetails
ALEU52
AASN272
AMET571
ATYR583
BLEU52
BVAL53
BTYR73
BGLY101
BVAL121
BSER125
BVAL129
AVAL53
BPHE130
BMET132
BASN272
BMET571
BTYR583
ATYR73
AGLY101
AVAL121
ASER125
AVAL129
APHE130
AMET132

site_idSWS_FT_FI3
Number of Residues10
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN111
BTRP519
AMET190
ATHR335
ATHR375
ATRP519
BASN111
BMET190
BTHR335
BTHR375

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0007744|PDB:1GPE
ChainResidueDetails
AGLY183
AGLU410
BGLY183
BGLU410

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1gal
ChainResidueDetails
AGLU416
AHIS520
AHIS563

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1gal
ChainResidueDetails
BGLU416
BHIS520
BHIS563

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gal
ChainResidueDetails
AHIS520
AHIS563

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gal
ChainResidueDetails
BHIS520
BHIS563

237735

PDB entries from 2025-06-18

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