DCUP_SHEEP
ID DCUP_SHEEP Reviewed; 367 AA.
AC Q8HY31;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000250|UniProtKB:P06132};
DE Short=UPD;
DE Short=URO-D;
DE EC=4.1.1.37 {ECO:0000250|UniProtKB:P06132};
GN Name=UROD {ECO:0000250|UniProtKB:P06132};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PCT PRO-131.
RX PubMed=16026339; DOI=10.1111/j.1365-2052.2005.01301.x;
RA Nezamzadeh R., Seubert A., Pohlenz J., Brenig B.;
RT "Identification of a mutation in the ovine uroporphyrinogen decarboxylase
RT (UROD) gene associated with a type of porphyria.";
RL Anim. Genet. 36:297-302(2005).
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 {ECO:0000250}.
CC -!- DISEASE: Note=Defects in UROD are the cause of porphyria cutanea tarda
CC (PCT). PCT has been identified in a flock of German Blackface sheep. It
CC is characterized by photosensitivity and porphyrinuria.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; AJ295031; CAC82649.1; -; Genomic_DNA.
DR RefSeq; NP_001012341.1; NM_001012341.1.
DR AlphaFoldDB; Q8HY31; -.
DR SMR; Q8HY31; -.
DR STRING; 9940.ENSOARP00000001535; -.
DR Ensembl; ENSOART00000001578; ENSOARP00000001535; ENSOARG00000001472.
DR Ensembl; ENSOART00020005698; ENSOARP00020004689; ENSOARG00020003627.
DR GeneID; 497117; -.
DR KEGG; oas:497117; -.
DR CTD; 7389; -.
DR eggNOG; KOG2872; Eukaryota.
DR HOGENOM; CLU_040933_0_0_1; -.
DR OMA; LWLMRQA; -.
DR OrthoDB; 1114675at2759; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000002356; Chromosome 1.
DR Bgee; ENSOARG00000001472; Expressed in metanephros cortex and 52 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0006787; P:porphyrin-containing compound catabolic process; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Decarboxylase; Disease variant; Heme biosynthesis;
KW Lyase; Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..367
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000279746"
FT BINDING 37..41
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 86
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P06132"
FT VARIANT 131
FT /note="L -> P (in FCT)"
FT /evidence="ECO:0000269|PubMed:16026339"
SQ SEQUENCE 367 AA; 40812 MW; B62FA2B1A1A98D4B CRC64;
MEAKESRPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR
SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREERDLER
LRDPATVASE LGYVFQAITL TRQQLAGRVP LIGFAGAPWT LMTYMVEGGG SSTMSQAKRW
LYQRPQASHQ LLRILTDALV PYLVGQVAAG AQALQLFESH AGHLGPQLFS KFALPYIRDV
SKRVKAGLQE AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPEK ARERVGKTVT
LQGNLDPCAL YASEEEIGKL VQQMLNDFGP QRYIANLGHG LYPDMDPEHV GAFVDAVHKH
SRLLRQN
