ID   DCUP_IDILO              Reviewed;         358 AA.
AC   Q5QVW3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000255|HAMAP-Rule:MF_00218};
DE            Short=UPD {ECO:0000255|HAMAP-Rule:MF_00218};
DE            Short=URO-D {ECO:0000255|HAMAP-Rule:MF_00218};
DE            EC=4.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00218};
GN   Name=hemE {ECO:0000255|HAMAP-Rule:MF_00218}; OrderedLocusNames=IL2306;
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC   -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of
CC       uroporphyrinogen-III to yield coproporphyrinogen-III.
CC       {ECO:0000255|HAMAP-Rule:MF_00218}.
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:0000255|HAMAP-Rule:MF_00218};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
CC       {ECO:0000255|HAMAP-Rule:MF_00218}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00218}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00218}.
CC   -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00218}.
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DR   EMBL; AE017340; AAV83138.1; -; Genomic_DNA.
DR   RefSeq; WP_011235532.1; NC_006512.1.
DR   AlphaFoldDB; Q5QVW3; -.
DR   SMR; Q5QVW3; -.
DR   STRING; 283942.IL2306; -.
DR   EnsemblBacteria; AAV83138; AAV83138; IL2306.
DR   KEGG; ilo:IL2306; -.
DR   eggNOG; COG0407; Bacteria.
DR   HOGENOM; CLU_040933_0_0_6; -.
DR   OMA; LWLMRQA; -.
DR   OrthoDB; 1104410at2; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000001171; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cytoplasm; Decarboxylase; Lyase; Porphyrin biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..358
FT                   /note="Uroporphyrinogen decarboxylase"
FT                   /id="PRO_0000325656"
FT   BINDING         29..33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   SITE            79
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ   SEQUENCE   358 AA;  39158 MW;  FC1FD32C0A31AD32 CRC64;
     MTAPALKNDR YLRALAKQPV DRTPVWMMRQ AGRYLPEYKE VRGQAGDFMS LCRNTELACE
     VTMQPLRRFD LDAAILFSDI LTIPDAMGLG LYFEAGEGPK FKDPVRSMAA IKNLAVPDME
     DELGYVMDAV RAIRRELNGS VPLIGFSGSP WTLATYMVEG GSTKNFSKVK QLMFADPEAM
     HTLLNVLAES VTQYLNAQIA AGAQSVMIFD TWGGVLSPRD YKAFSLAYME KIVAGLTREA
     DGRKVPVTLF TKNGGQWLEA MAASGADALG VDWTTDLSDA RARVGGQVAL QGNMDPSVLY
     AKPARIEEEV QSILQSYGSG TGHVFNLGHG IHPEVDPEHA AAFIEAIHKY SPAFHSND