ID   DCUP_NAUPA              Reviewed;         340 AA.
AC   B9L8M1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=NAMH_0563;
OS   Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales; Nautiliaceae;
OC   Nautilia.
OX   NCBI_TaxID=598659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1463 / DSM 18972 / AmH;
RX   PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA   Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K.,
RA   Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT   "Adaptations to submarine hydrothermal environments exemplified by the
RT   genome of Nautilia profundicola.";
RL   PLoS Genet. 5:E1000362-E1000362(2009).
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; CP001279; ACM92401.1; -; Genomic_DNA.
DR   RefSeq; WP_012663772.1; NC_012115.1.
DR   AlphaFoldDB; B9L8M1; -.
DR   SMR; B9L8M1; -.
DR   STRING; 598659.NAMH_0563; -.
DR   EnsemblBacteria; ACM92401; ACM92401; NAMH_0563.
DR   KEGG; nam:NAMH_0563; -.
DR   eggNOG; COG0407; Bacteria.
DR   HOGENOM; CLU_040933_0_0_7; -.
DR   OMA; LWLMRQA; -.
DR   OrthoDB; 1104410at2; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000000448; 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..340
FT                   /note="Uroporphyrinogen decarboxylase"
FT                   /id="PRO_1000197531"
FT   BINDING         21..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   SITE            71
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ   SEQUENCE   340 AA;  38857 MW;  48DAC15542A6A95D CRC64;
     MIFVDACFGK ETEYTPVWMM RQAGRYLPEY MEVRRKIGNF LDMTRNPEVV AEVTIQPIDI
     LDVDAAILFS DILNLPMEMG LPLRFEKGVG PVFDKTIDTE EDIEALDSSA DEKLEYVYKG
     VKLIRERLPE EKALIGFAGS PWTIATYMVE GRGSKQYAKI KKMVYSNPMM LHRLLAFNTK
     ETIEYLSKQI DAGANAVMVF DSWGGALEKE KFFEFSWNYM KEIAKNIKAK YPHIPVILFS
     KGVGLYMDEM DGEFDVVGVD WATPIDHALR IFKDNYTLQG NMEPTRLYSK TATKEAVEKI
     AGIMKGHRHI FNLGHGILPD VPVENAKYFV NLCKELTRRG