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3CYV

Crystal structure of uroporphyrinogen decarboxylase from Shigella flexineri: new insights into its catalytic mechanism

Functional Information from GO Data
ChainGOidnamespacecontents
A0004853molecular_functionuroporphyrinogen decarboxylase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006778biological_processporphyrin-containing compound metabolic process
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0006783biological_processheme biosynthetic process
A0016831molecular_functioncarboxy-lyase activity
A0019353biological_processprotoporphyrinogen IX biosynthetic process from glutamate
Functional Information from PROSITE/UniProt
site_idPS00906
Number of Residues10
DetailsUROD_1 Uroporphyrinogen decarboxylase signature 1. PVWMMRQAGR
ChainResidueDetails
APRO22-ARG31

site_idPS00907
Number of Residues17
DetailsUROD_2 Uroporphyrinogen decarboxylase signature 2. IGFSGsPWTLatYmv.EG
ChainResidueDetails
AILE142-GLY158

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00218
ChainResidueDetails
AARG27
APHE46
AASP77
ATYR154
ATHR209
AHIS327

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00218
ChainResidueDetails
AASP77

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1uro
ChainResidueDetails
ATYR154
AASP77

223790

PDB entries from 2024-08-14

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