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2ZY2

dodecameric L-aspartate beta-decarboxylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0006520biological_processamino acid metabolic process
A0006523biological_processalanine biosynthetic process
A0006531biological_processaspartate metabolic process
A0008483molecular_functiontransaminase activity
A0008652biological_processamino acid biosynthetic process
A0009058biological_processbiosynthetic process
A0016831molecular_functioncarboxy-lyase activity
A0016847molecular_function1-aminocyclopropane-1-carboxylate synthase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042218biological_process1-aminocyclopropane-1-carboxylate biosynthetic process
A0042802molecular_functionidentical protein binding
A0047688molecular_functionaspartate 4-decarboxylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP A 900
ChainResidue
AARG37
ATYR289
ASER312
ALYS315
AARG323
ATYR134
AGLY173
AGLY174
ATHR175
APHE204
ATYR207
AASN256
AASP286

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKyfGAtGWRLG
ChainResidueDetails
ASER312-GLY325

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY115
AASN256
AARG497

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:19368885, ECO:0007744|PDB:2ZY2
ChainResidueDetails
ALYS315

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
APHE204
AASP286
ALYS315

225946

PDB entries from 2024-10-09

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