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3NGX

Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase / cyclohydrolase from Thermoplasma acidophilum

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processL-histidine biosynthetic process
A0003824molecular_functioncatalytic activity
A0004477molecular_functionmethenyltetrahydrofolate cyclohydrolase activity
A0004488molecular_functionmethylenetetrahydrofolate dehydrogenase (NADP+) activity
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006730biological_processone-carbon metabolic process
A0009086biological_processmethionine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016787molecular_functionhydrolase activity
A0035999biological_processtetrahydrofolate interconversion
B0000105biological_processL-histidine biosynthetic process
B0003824molecular_functioncatalytic activity
B0004477molecular_functionmethenyltetrahydrofolate cyclohydrolase activity
B0004488molecular_functionmethylenetetrahydrofolate dehydrogenase (NADP+) activity
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006730biological_processone-carbon metabolic process
B0009086biological_processmethionine biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016787molecular_functionhydrolase activity
B0035999biological_processtetrahydrofolate interconversion
Functional Information from PROSITE/UniProt
site_idPS00767
Number of Residues9
DetailsTHF_DHG_CYH_2 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 2. PGGVGPITA
ChainResidueDetails
APRO250-ALA258

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01576, ECO:0000269|PubMed:21333632
ChainResidueDetails
AASN157
ASER182
AILE223
BASN157
BSER182
BILE223

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PDB entries from 2024-07-24

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