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4A0H

Structure of bifunctional DAPA aminotransferase-DTB synthetase from Arabidopsis thaliana bound to 7-keto 8-amino pelargonic acid (KAPA)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004015molecular_functionadenosylmethionine-8-amino-7-oxononanoate transaminase activity
A0004141molecular_functiondethiobiotin synthase activity
A0005524molecular_functionATP binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0008483molecular_functiontransaminase activity
A0009102biological_processbiotin biosynthetic process
A0016874molecular_functionligase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004015molecular_functionadenosylmethionine-8-amino-7-oxononanoate transaminase activity
B0004141molecular_functiondethiobiotin synthase activity
B0005524molecular_functionATP binding
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0008483molecular_functiontransaminase activity
B0009102biological_processbiotin biosynthetic process
B0016874molecular_functionligase activity
B0030170molecular_functionpyridoxal phosphate binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE KAP A 1808
ChainResidue
APHE326
APLP1644
BGLY678
BHIS679
BSER680
ATRP369
ATRP370
ATYR473
AALA587
ALYS644
AARG775
APRO776
ALEU777

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE KAP B 1808
ChainResidue
AGLY678
BTRP369
BTRP370
BTYR473
BALA587
BLYS644
BARG775
BPRO776
BPLP1644

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE KAP A 1809
ChainResidue
AGLY223
AILE225
ASER226
BTHR24
BTHR59
BSER143
BSER195
BTLA1810

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE KAP B 1809
ChainResidue
ATHR24
ATHR59
AALA141
AILE142
ASER195
ATLA1810
BLEU222
BGLY223
BGLY224
BILE225
BSER226

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TLA A 1810
ChainResidue
AASN23
ATHR24
ASER25
ALYS28
ALYS55
AASP66
ATHR189
AALA190
AGLY191
BKAP1809

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TLA B 1810
ChainResidue
AKAP1809
BASN23
BTHR24
BSER25
BLYS28
BLYS55
BASP66
BGLU188
BGLY191

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP A 1644
ChainResidue
ATRP370
AASN430
AGLY431
ASER432
ATYR473
AHIS474
AGLU581
AASP615
AVAL617
APHE618
ALYS644
AKAP1808
BHIS679
BSER680

site_idAC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP B 1644
ChainResidue
AHIS679
ASER680
BTRP370
BASN430
BGLY431
BSER432
BTYR473
BHIS474
BGLU581
BASP615
BVAL617
BPHE618
BLYS644
BKAP1808

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. VIfDEVft.GFwRlGvetttellgckp....DIAcfAKlltGG
ChainResidueDetails
AVAL612-GLY649

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13000
ChainResidueDetails
BPRO496
BGLU523
ASER25
AASP75
AGLU248
APRO496
AGLU523
BSER25
BASP75
BGLU248

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0G
ChainResidueDetails
ATHR29
AASP66
AGLU188
BTHR29
BASP66
BGLU188

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0R
ChainResidueDetails
ATHR59
BTHR59

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0H
ChainResidueDetails
AARG775
BTRP369
BTYR473
BLYS644
BGLY678
BARG775
ATYR473
ATRP369
ALYS644
AGLY678

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0G, ECO:0007744|PDB:4A0H, ECO:0007744|PDB:4A0R
ChainResidueDetails
AGLY431
AASP615
AHIS679
BGLY431
BASP615
BHIS679

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM => ECO:0000250|UniProtKB:P12995
ChainResidueDetails
APHE326
BPHE326

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0F, ECO:0007744|PDB:4A0G, ECO:0007744|PDB:4A0H, ECO:0007744|PDB:4A0R
ChainResidueDetails
ALYS644
BLYS644

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PDB entries from 2024-06-12

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