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1JT9

Structure of the mutant F174A T form of the Glucosamine-6-Phosphate deaminase from E.coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0004342molecular_functionglucosamine-6-phosphate deaminase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006043biological_processglucosamine catabolic process
A0006044biological_processN-acetylglucosamine metabolic process
A0006046biological_processN-acetylglucosamine catabolic process
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0016787molecular_functionhydrolase activity
A0019262biological_processN-acetylneuraminate catabolic process
A0042802molecular_functionidentical protein binding
Functional Information from PROSITE/UniProt
site_idPS01161
Number of Residues19
DetailsGLC_GALNAC_ISOMERASE Glucosamine/galactosamine-6-phosphate isomerases signature. IrsyGkIhLfMgGVGnDGH
ChainResidueDetails
AILE125-HIS143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor; for enolization step => ECO:0000269|PubMed:11513596
ChainResidueDetails
AASP72

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: For ring-opening step => ECO:0000269|PubMed:11513596
ChainResidueDetails
AASP141
AGLU148

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton acceptor; for ring-opening step => ECO:0000269|PubMed:11513596
ChainResidueDetails
AHIS143

site_idSWS_FT_FI4
Number of Residues5
DetailsSITE: Part of the allosteric site
ChainResidueDetails
ASER151
AARG158
ALYS160
ATHR161
ATYR254

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1cd5
ChainResidueDetails
AHIS143
AGLU148
AASP141
AASP72

site_idMCSA1
Number of Residues4
DetailsM-CSA 60
ChainResidueDetails
AASP72electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASP141activator, hydrogen bond acceptor
AHIS143hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AGLU148activator, hydrogen bond acceptor

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PDB entries from 2024-07-17

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