ID   DCUP_ACISJ              Reviewed;         370 AA.
AC   A1WCJ3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Ajs_3861;
OS   Acidovorax sp. (strain JS42).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX   NCBI_TaxID=232721;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS42;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000539; ABM43968.1; -; Genomic_DNA.
DR   RefSeq; WP_011806948.1; NC_008782.1.
DR   AlphaFoldDB; A1WCJ3; -.
DR   SMR; A1WCJ3; -.
DR   STRING; 232721.Ajs_3861; -.
DR   EnsemblBacteria; ABM43968; ABM43968; Ajs_3861.
DR   KEGG; ajs:Ajs_3861; -.
DR   eggNOG; COG0407; Bacteria.
DR   HOGENOM; CLU_040933_0_0_4; -.
DR   OMA; LWLMRQA; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000000645; 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..370
FT                   /note="Uroporphyrinogen decarboxylase"
FT                   /id="PRO_1000023866"
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         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         342
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   370 AA;  40219 MW;  42F197052F743C98 CRC64;
     MSFAPLQNDT FLRACRRQAT DYTPLWLMRQ AGRYLPEYKA TRAKAGSFMG LATNVEYATE
     VTLQPLERFP LDAAILFSDI LTVPDAMGLG LSFAEGEGPR FAKAVRDEAD VAALAVPDLD
     KLRYVFDAVT SIRRALNGRV PLIGFSGSPW TLACYMVEGK GSDDYRLVKT LMYSRPDLMH
     RILAVNADAV AAYLNAQIDA GAQAVMVFDS WGGVLADGCF QQFSLEYTRR VLAQLKRTGV
     DGQDVPRIVF TKGGGIWLDD MKDIDCEVLG LDWTAHLGKA RAIVGGQVGG PGKALQGNID
     PNVLFAPPEA VAAQVRAVLD SFGTPHTDKT TTGPTHIFNL GHGISQFTPP EHVAALVEAV
     HGYSRSLRQR