DCUP_HORVU
ID DCUP_HORVU Reviewed; 330 AA.
AC Q42855;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Uroporphyrinogen decarboxylase;
DE Short=UPD;
DE Short=URO-D;
DE EC=4.1.1.37;
DE Flags: Fragment;
GN Name=DCUP;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=7599310; DOI=10.1007/bf00020244;
RA Mock H.-P., Trainotti L., Kruse E., Grimm B.;
RT "Isolation, sequencing and expression of cDNA sequences encoding
RT uroporphyrinogen decarboxylase from tobacco and barley.";
RL Plant Mol. Biol. 28:245-256(1995).
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; X82832; CAA58039.1; -; mRNA.
DR PIR; S55733; S55733.
DR AlphaFoldDB; Q42855; -.
DR SMR; Q42855; -.
DR EnsemblPlants; HORVU.MOREX.r2.4HG0314380.1; HORVU.MOREX.r2.4HG0314380.1; HORVU.MOREX.r2.4HG0314380.
DR EnsemblPlants; HORVU.MOREX.r2.4HG0314380.1.mrna1; HORVU.MOREX.r2.4HG0314380.1.mrna1; HORVU.MOREX.r2.4HG0314380.1.
DR Gramene; HORVU.MOREX.r2.4HG0314380.1; HORVU.MOREX.r2.4HG0314380.1; HORVU.MOREX.r2.4HG0314380.
DR Gramene; HORVU.MOREX.r2.4HG0314380.1.mrna1; HORVU.MOREX.r2.4HG0314380.1.mrna1; HORVU.MOREX.r2.4HG0314380.1.
DR UniPathway; UPA00251; UER00321.
DR ExpressionAtlas; Q42855; 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.
FT CHAIN <1..330
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187575"
FT BINDING 10..14
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 60
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 330 AA; 36667 MW; DB2C5CA27154BC90 CRC64;
VERPPVWLMR QAGRYMKSYQ NLCEKYPLFR ERSENVDLVV EISLQPWKVF KPDGVILFSD
ILTPLPGMNI PFDIVKGKGP VIYDPLRTAA AVNEVREFVP EEWVPYVGQA LNLLRGEVKN
EAAVLGFVGA PFTLASYCVE GGSSKNFSKI KRMAFAEPAI LHNLLQKFTT SMANYIKYQA
DNGAQAVQIF DSWATELSPV DFEEFSLPYL KQIVDSVKET HPDLPLILYA SGSGGLLERL
PLTGVDVVSL DWTVDMAEGR KRLGSNIAVQ GNVDPGVLFG SKEFITKRIY DTVQKAGSQG
HVLNLGHGIK VGTPEENVAH FFEVAKGIRY