ID   DCUP_PONAB              Reviewed;         367 AA.
AC   Q5RDK5;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; CR857901; CAH90152.1; -; mRNA.
DR   RefSeq; NP_001129018.1; NM_001135546.1.
DR   AlphaFoldDB; Q5RDK5; -.
DR   SMR; Q5RDK5; -.
DR   STRING; 9601.ENSPPYP00000001644; -.
DR   GeneID; 100190859; -.
DR   KEGG; pon:100190859; -.
DR   CTD; 7389; -.
DR   eggNOG; KOG2872; Eukaryota.
DR   InParanoid; Q5RDK5; -.
DR   OrthoDB; 1114675at2759; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Decarboxylase; Heme biosynthesis; Lyase;
KW   Porphyrin biosynthesis; Reference proteome.
FT   CHAIN           1..367
FT                   /note="Uroporphyrinogen decarboxylase"
FT                   /id="PRO_0000230308"
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"
SQ   SEQUENCE   367 AA;  40721 MW;  D3F6FA4B646B06F9 CRC64;
     MEANGLGPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR
     SPEACCEPTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREEQDLEC
     LRDPEVVASE LDYVFQAITL TRQRLAGRVP LIGFAGAPWT LMTYMVEGGG SSTMAQAKRW
     LYQRPQASHQ LLRILTDALV PYLVGQVAAG AQALQLFESH AGHLGPQLFS KFALPYIRDV
     AKQVKARLRE AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARECVGKTVT
     LQGNLDPCAL YASEEEIGQL VKQMLDDFGP HRYIANLGHG LYPDMDPEHV GAFVDAVHKH
     SRLLRQN