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1TDJ

THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0003941molecular_functionL-serine ammonia-lyase activity
A0004794molecular_functionthreonine deaminase activity
A0006520biological_processamino acid metabolic process
A0006565biological_processL-serine catabolic process
A0006566biological_processthreonine metabolic process
A0006567biological_processthreonine catabolic process
A0009082biological_processbranched-chain amino acid biosynthetic process
A0009097biological_processisoleucine biosynthetic process
A0016597molecular_functionamino acid binding
A0016829molecular_functionlyase activity
A0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 962
ChainResidue
APHE61
AVAL242
AGLU286
ASER288
ASER315
AGLY316
AHOH614
ALYS62
AASN89
AGLY188
AGLY189
AGLY190
AGLY191
ALEU192
AGLY241

Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues14
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Edrqp.VHSFKLRGA
ChainResidueDetails
AGLU53-ALA66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:9562556
ChainResidueDetails
AASN89
AGLY188
ASER315

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:9562556
ChainResidueDetails
ALYS62

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Details
ChainResidueDetails
ASER315
ALYS62

site_idMCSA1
Number of Residues2
DetailsM-CSA 886
ChainResidueDetails
ALYS62covalent catalysis, proton shuttle (general acid/base)
ASER315electrostatic stabiliser

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PDB entries from 2024-07-10

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