ID   DCUP_PSEF5              Reviewed;         355 AA.
AC   Q4KJI4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=PFL_0455;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY95864.1; -; Genomic_DNA.
DR   RefSeq; WP_011058829.1; NC_004129.6.
DR   AlphaFoldDB; Q4KJI4; -.
DR   SMR; Q4KJI4; -.
DR   STRING; 220664.PFL_0455; -.
DR   PRIDE; Q4KJI4; -.
DR   EnsemblBacteria; AAY95864; AAY95864; PFL_0455.
DR   GeneID; 57473444; -.
DR   KEGG; pfl:PFL_0455; -.
DR   PATRIC; fig|220664.5.peg.466; -.
DR   eggNOG; COG0407; Bacteria.
DR   HOGENOM; CLU_040933_0_0_6; -.
DR   OMA; LWLMRQA; -.
DR   OrthoDB; 1104410at2; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000008540; 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..355
FT                   /note="Uroporphyrinogen decarboxylase"
FT                   /id="PRO_1000023948"
FT   BINDING         27..31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         78
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         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   SITE            78
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ   SEQUENCE   355 AA;  38940 MW;  228C205BE8B09969 CRC64;
     MTALKNDRFL RALLKQPVDV TPVWMMRQAG RYLPEYRASR ANAGDFMSLC MNPEFACEVT
     LQPLDRYPQL DAAILFSDIL TIPDAMGQGL YFETGEGPRF KKVVSTLADI EALPIPDPHK
     DLGYVMDAVS TIRRELNGRV PLIGFSGSPW TLATYMVEGG SSKDFRKSKA MLYDNPQAMH
     LLLDKLAQSV TAYLNGQIRA GAQAVQIFDS WGGSLSAAAY QEFSLAYMRK IVSGLIREHD
     GRKVPVILFT KGGGLWLESI ADAGADSLGL DWTCDIGEAR RRVGSKVSLQ GNMDPTVLYA
     NPQAIRSEVA RILASYGKGS GHVFNLGHGI TPEVKPEHAG AFLEAVHELS AQYHE