DCUP_DANRE
ID DCUP_DANRE Reviewed; 369 AA.
AC Q9PTS2;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
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 Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF MET-38.
RX PubMed=9806541; DOI=10.1038/3041;
RA Wang H., Long Q., Marty S.D., Sassa S., Lin S.;
RT "A zebrafish model for hepatoerythropoietic porphyria.";
RL Nat. Genet. 20:239-243(1998).
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 (By
CC similarity). In vitro also decarboxylates pentacarboxylate
CC porphyrinogen I (PubMed:9806541). {ECO:0000250|UniProtKB:P06132,
CC ECO:0000269|PubMed:9806541}.
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; AF095639; AAF14346.1; -; mRNA.
DR RefSeq; NP_571422.1; NM_131347.1.
DR AlphaFoldDB; Q9PTS2; -.
DR SMR; Q9PTS2; -.
DR STRING; 7955.ENSDARP00000023867; -.
DR PaxDb; Q9PTS2; -.
DR Ensembl; ENSDART00000014568; ENSDARP00000023867; ENSDARG00000006818.
DR GeneID; 30617; -.
DR KEGG; dre:30617; -.
DR CTD; 7389; -.
DR ZFIN; ZDB-GENE-000208-18; urod.
DR eggNOG; KOG2872; Eukaryota.
DR GeneTree; ENSGT00390000018302; -.
DR HOGENOM; CLU_040933_0_0_1; -.
DR InParanoid; Q9PTS2; -.
DR OMA; LWLMRQA; -.
DR OrthoDB; 1114675at2759; -.
DR PhylomeDB; Q9PTS2; -.
DR TreeFam; TF300744; -.
DR Reactome; R-DRE-189451; Heme biosynthesis.
DR UniPathway; UPA00251; UER00321.
DR PRO; PR:Q9PTS2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000006818; Expressed in mature ovarian follicle and 28 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IDA:ZFIN.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR GO; GO:0006787; P:porphyrin-containing compound catabolic process; ISS:UniProtKB.
DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; IDA:ZFIN.
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 Cytoplasm; Decarboxylase; Heme biosynthesis; Lyase; Porphyrin biosynthesis;
KW Reference proteome.
FT CHAIN 1..369
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187572"
FT BINDING 39..43
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MUTAGEN 38
FT /note="M->R: Reduces uroporphyrinogen decarboxylase
FT activity."
FT /evidence="ECO:0000269|PubMed:9806541"
SQ SEQUENCE 369 AA; 41645 MW; D820CC69EB4E27F2 CRC64;
MMDKDSFILP KDFPELRNDT FLRAARGEEI EHIPVWCMRQ AGRYLPEFRE SRAGKDFFET
CRSPEACCEL TLQPLRRFPF DAAIIFSDIL VVPQAMGMEV QMCPGKGPTF PEPLKEPEDL
QRLKTQVDVY SELDYVFKAI TLTRHKIEGK VPLIGFTGAP WTLMSYMIEG GGSATHSKAK
RWLYRYPEAS HKLLSQLTDV IVEYLLGQVK AGAQALQVFE SHTGCLGPVE FKEFSLPYLR
DIARRVKDKI KESGLDNVPM IVFAKDGHYG LEDLSESAYE VVGLDWTIDP RSARVRTGGK
VSLQGNMDPC ALYGTKESIS EIVRRMLEGF GTKGYIANLG HGLYPDMDPE NVGAFVEAVH
NHSRQLLKR
