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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
A0016829molecular_functionlyase activity
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 Residues9
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00218","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00218","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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

247536

PDB entries from 2026-01-14

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