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1R3R

Uroporphyrinogen Decarboxylase with mutation D86N

Functional Information from GO Data
ChainGOidnamespacecontents
A0004853molecular_functionuroporphyrinogen decarboxylase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0006778biological_processporphyrin-containing compound metabolic process
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0006783biological_processheme biosynthetic process
A0006784biological_processheme A biosynthetic process
A0006785biological_processheme B biosynthetic process
A0006787biological_processporphyrin-containing compound catabolic process
A0016829molecular_functionlyase activity
A0016831molecular_functioncarboxy-lyase activity
A0042168biological_processheme metabolic process
Functional Information from PROSITE/UniProt
site_idPS00906
Number of Residues10
DetailsUROD_1 Uroporphyrinogen decarboxylase signature 1. PVWCMRQAGR
ChainResidueDetails
APRO32-ARG41

site_idPS00907
Number of Residues17
DetailsUROD_2 Uroporphyrinogen decarboxylase signature 2. IGFAGaPWTLmtYmv.EG
ChainResidueDetails
AILE152-GLY168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14633982","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1R3W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R3Y","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14633982","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1R3T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R3W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R3Y","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14633982","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1R3Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R3S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14633982","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1R3Y","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14633982","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1R3T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R3W","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"14633982","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1uro
ChainResidueDetails
ATYR164
AASN86

site_idMCSA1
Number of Residues5
DetailsM-CSA 914
ChainResidueDetails
AARG37proton shuttle (general acid/base)
AARG41electrostatic stabiliser
AARG50proton shuttle (general acid/base)
AASN86enhance reactivity, modifies pKa, transition state stabiliser
ATYR164electrostatic stabiliser

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PDB entries from 2025-10-08

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