ID   DCUP_GEOSL              Reviewed;         340 AA.
AC   Q746R5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, 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=GSU3453;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR36843.1; -; Genomic_DNA.
DR   RefSeq; NP_954493.1; NC_002939.5.
DR   RefSeq; WP_010944063.1; NC_002939.5.
DR   AlphaFoldDB; Q746R5; -.
DR   SMR; Q746R5; -.
DR   STRING; 243231.GSU3453; -.
DR   EnsemblBacteria; AAR36843; AAR36843; GSU3453.
DR   KEGG; gsu:GSU3453; -.
DR   PATRIC; fig|243231.5.peg.3476; -.
DR   eggNOG; COG0407; Bacteria.
DR   HOGENOM; CLU_040933_0_0_7; -.
DR   InParanoid; Q746R5; -.
DR   OMA; LWLMRQA; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019353; P:protoporphyrinogen IX biosynthetic process from glutamate; IBA:GO_Central.
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_0000325649"
FT   BINDING         23..27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         72
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         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   SITE            72
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ   SEQUENCE   340 AA;  37815 MW;  1967BF5C3A36E1F9 CRC64;
     MNNRFLDACW GKPVDRTPVW LMRQAGRYLP EYMAVRSKCT FLELCKTPEL AAEVTIQPID
     ILNVDAAILF SDILTPVEPM GLKLDFVPGP VFEHPVRTMA DVEKLRIPNP EEDVPYVLDT
     IKILRRELAG RVPLIGFGGA PFTLACYMVE GKGSKDWANI KRMMYAAPDV YAALMDKVTM
     MDMEYLNAQI KAGAQAIQIF DTWGGVLSPT DYEKYVLPYT TKLINGLNRQ NTPVIHFVKG
     AGTMLETVQK AGGDVMGLDW HVNLGKARDV LGQNMAVQGN LDPTVLYAPK EVIEAEVKRV
     LDENAGRPGH IFNLGHGILP TVPPENAIHM VECVHRLSQK