DCUP_RAT
ID DCUP_RAT Reviewed; 364 AA.
AC P32362;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000305};
DE Short=UPD;
DE Short=URO-D;
DE EC=4.1.1.37 {ECO:0000250|UniProtKB:P06132};
DE Flags: Fragment;
GN Name=Urod {ECO:0000312|RGD:3946};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3658690; DOI=10.1093/nar/15.17.7211;
RA Romana M., le Boulch P., Romeo P.-H.;
RT "Rat uroporphyrinogen decarboxylase cDNA: nucleotide sequence and
RT comparison to human uroporphyrinogen decarboxylase.";
RL Nucleic Acids Res. 15:7211-7211(1987).
RN [2]
RP PROTEIN SEQUENCE OF 118-139, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
CC -!- FUNCTION: Catalyzes the sequential decarboxylation of the four acetate
CC side chains of uroporphyrinogen to form coproporphyrinogen and
CC participates in the fifth step in the heme biosynthetic pathway. Isomer
CC I or isomer III of uroporphyrinogen may serve as substrate, but only
CC coproporphyrinogen III can ultimately be converted to heme. In vitro
CC also decarboxylates pentacarboxylate porphyrinogen I.
CC {ECO:0000250|UniProtKB:P06132}.
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 Evidence={ECO:0000250|UniProtKB:P06132};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19866;
CC Evidence={ECO:0000250|UniProtKB:P06132};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 H(+) + uroporphyrinogen I = 4 CO2 + coproporphyrinogen I;
CC Xref=Rhea:RHEA:31239, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:62626, ChEBI:CHEBI:62631;
CC Evidence={ECO:0000250|UniProtKB:P06132};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31240;
CC Evidence={ECO:0000250|UniProtKB:P06132};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
CC {ECO:0000250|UniProtKB:P06132}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; Y00350; CAB50784.1; -; mRNA.
DR AlphaFoldDB; P32362; -.
DR SMR; P32362; -.
DR STRING; 10116.ENSRNOP00000024719; -.
DR jPOST; P32362; -.
DR PaxDb; P32362; -.
DR PRIDE; P32362; -.
DR UCSC; RGD:3946; rat.
DR RGD; 3946; Urod.
DR eggNOG; KOG2872; Eukaryota.
DR InParanoid; P32362; -.
DR PhylomeDB; P32362; -.
DR Reactome; R-RNO-189451; Heme biosynthesis.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0008198; F:ferrous iron binding; IDA:RGD.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IDA:RGD.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; IEP:RGD.
DR GO; GO:0006783; P:heme biosynthetic process; ISO:RGD.
DR GO; GO:0042168; P:heme metabolic process; ISO:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IDA:RGD.
DR GO; GO:0006787; P:porphyrin-containing compound catabolic process; ISS:UniProtKB.
DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; ISO:RGD.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0014075; P:response to amine; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0060992; P:response to fungicide; IEP:RGD.
DR GO; GO:0010039; P:response to iron ion; IEP:RGD.
DR GO; GO:0046689; P:response to mercury ion; IEP:RGD.
DR GO; GO:0051597; P:response to methylmercury; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0046502; P:uroporphyrinogen III metabolic process; IDA:RGD.
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 1: Evidence at protein level;
KW Cytoplasm; Decarboxylase; Direct protein sequencing; Heme biosynthesis;
KW Lyase; Porphyrin biosynthesis; Reference proteome.
FT CHAIN <1..364
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187571"
FT BINDING 34..38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 83
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 364 AA; 40453 MW; 5D97D1BEA914F41E CRC64;
NGLGLQNFPE LKNDTFLRAA WGEETDYTPV WCMRQAGRYL PEFRETRAAQ DFFSTCRSPE
ACCELTLEPV RRFPLDAAII FSDILVVPQA LAMEVTMVPG KGPSFPEPLR EERDLERLRD
PAAVASELGY VFQAITLTRQ QLAGRVPLIG FAGAPWTLMT YMVEGGSFKT MAQAKRWLYQ
KPVASHKLLG ILTHALVPYL IGQVAAGAQA LQLFESHAGH LGSELFSKFA LPYIRDVAKR
VKAGLQKAGL TRMPMIIFAK DGHFALEELA QAGYEVVGLD WTVAPKKARE PVGKTVTLQG
ELDPCALYAS EEEIGRLVQQ MLNDFGPQRY IANLGHGLYP DMDPEHVGAF LDAVHKHSRL
LRQN
