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2V9D

Crystal Structure of YagE, a prophage protein belonging to the dihydrodipicolinic acid synthase family from E. coli K12

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0016829molecular_functionlyase activity
A0042802molecular_functionidentical protein binding
A0046176biological_processaldonic acid catabolic process
A0047440molecular_function2-dehydro-3-deoxy-D-pentonate aldolase activity
A0061677molecular_function2-dehydro-3-deoxy-D-gluconate aldolase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0016829molecular_functionlyase activity
B0042802molecular_functionidentical protein binding
B0046176biological_processaldonic acid catabolic process
B0047440molecular_function2-dehydro-3-deoxy-D-pentonate aldolase activity
B0061677molecular_function2-dehydro-3-deoxy-D-gluconate aldolase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0016829molecular_functionlyase activity
C0042802molecular_functionidentical protein binding
C0046176biological_processaldonic acid catabolic process
C0047440molecular_function2-dehydro-3-deoxy-D-pentonate aldolase activity
C0061677molecular_function2-dehydro-3-deoxy-D-gluconate aldolase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0016829molecular_functionlyase activity
D0042802molecular_functionidentical protein binding
D0046176biological_processaldonic acid catabolic process
D0047440molecular_function2-dehydro-3-deoxy-D-pentonate aldolase activity
D0061677molecular_function2-dehydro-3-deoxy-D-gluconate aldolase activity
Functional Information from PROSITE/UniProt
site_idPS00665
Number of Residues18
DetailsDHDPS_1 Dihydrodipicolinate synthase signature 1. GLFflGSGGEFsqlgaeE
ChainResidueDetails
AGLY50-GLU67

site_idPS00666
Number of Residues32
DetailsDHDPS_2 Dihydrodipicolinate synthase signature 2. YNFPalTgqdLtpalvktladsrsnIiGIKDT
ChainResidueDetails
ATYR145-THR176

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:21294156
ChainResidueDetails
ASER56
ATYR119
BSER56
BTYR119
CSER56
CTYR119
DSER56
DTYR119

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:21294156
ChainResidueDetails
ATYR145
BTYR145
CTYR145
DTYR145

site_idSWS_FT_FI3
Number of Residues4
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000305|PubMed:21294156
ChainResidueDetails
ALYS174
BLYS174
CLYS174
DLYS174

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fdy
ChainResidueDetails
ASER56
ALYS174
AGLY57

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fdy
ChainResidueDetails
BSER56
BLYS174
BGLY57

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fdy
ChainResidueDetails
CSER56
CLYS174
CGLY57

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fdy
ChainResidueDetails
DSER56
DLYS174
DGLY57

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PDB entries from 2024-07-17

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