ID   DCUP_MAIZE              Reviewed;         393 AA.
AC   O81220;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Uroporphyrinogen decarboxylase, chloroplastic;
DE            Short=UPD;
DE            Short=URO-D;
DE            EC=4.1.1.37;
DE   Flags: Precursor;
GN   Name=LES22;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9668130; DOI=10.2307/3870714;
RA   Hu G., Yalpani N., Briggs S.P., Johal G.S.;
RT   "A porphyrin pathway impairment is responsible for the phenotype of a
RT   dominant disease lesion mimic mutant of maize.";
RL   Plant Cell 10:1095-1105(1998).
CC   -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of
CC       uroporphyrinogen-III to yield coproporphyrinogen-III. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen
CC         III; Xref=Rhea:RHEA:19865, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57308, ChEBI:CHEBI:57309; EC=4.1.1.37;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AF058763; AAC31883.1; -; mRNA.
DR   PIR; T01653; T01653.
DR   AlphaFoldDB; O81220; -.
DR   SMR; O81220; -.
DR   PRIDE; O81220; -.
DR   eggNOG; KOG2872; Eukaryota.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; O81220; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00717; URO-D; 1.
DR   Gene3D; 3.20.20.210; -; 1.
DR   HAMAP; MF_00218; URO_D; 1.
DR   InterPro; IPR038071; UROD/MetE-like_sf.
DR   InterPro; IPR006361; Uroporphyrinogen_deCO2ase_HemE.
DR   InterPro; IPR000257; Uroporphyrinogen_deCOase.
DR   Pfam; PF01208; URO-D; 1.
DR   SUPFAM; SSF51726; SSF51726; 1.
DR   TIGRFAMs; TIGR01464; hemE; 1.
DR   PROSITE; PS00906; UROD_1; 1.
DR   PROSITE; PS00907; UROD_2; 1.
PE   2: Evidence at transcript level;
KW   Chlorophyll biosynthesis; Chloroplast; Decarboxylase; Lyase; Plastid;
KW   Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..393
FT                   /note="Uroporphyrinogen decarboxylase, chloroplastic"
FT                   /id="PRO_0000036330"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         73..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            123
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   393 AA;  43397 MW;  4B41910819168CAB CRC64;
     MATACPPLSL PSTSLFRGRS ARAGPNAGSS RPSAAAPSER RSWRRPRPDG GRAAAGERNQ
     REEVERPPVW LMRQAGRYMK SYQLLCERYP SFRERSENVD LVVEISLQPW KVFKPDGVIL
     FSDILTPLPG MNIPFDIVKG KGPVIYDPLR TAAAVNEVRE FVPEEWVPYV GQALNILRQE
     VKNEAAVLGF VGAPFTLASY CVEGGSSKNF TLIKKMAFSE PAILHNLLQK FTTSMANYIK
     YQADNGAQAV QIFDSWATEL SPADFEEFSL PYLKQIVDSV RETHPDLPLI LYASGSGGLL
     ERLPLTGVDV VSLDWTVDMA EGRKRLGSNT AVQGNVDPGV LFGSKEFITR RIYDTVQKAG
     NVGHVLNLGH GIKVGTPEEN VAHFFEVAKG IRY