ID   DCUP_GEOTN              Reviewed;         345 AA.
AC   A4IKU7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=GTNG_0569;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO65951.1; -; Genomic_DNA.
DR   RefSeq; WP_011886872.1; NC_009328.1.
DR   AlphaFoldDB; A4IKU7; -.
DR   SMR; A4IKU7; -.
DR   STRING; 420246.GTNG_0569; -.
DR   EnsemblBacteria; ABO65951; ABO65951; GTNG_0569.
DR   KEGG; gtn:GTNG_0569; -.
DR   eggNOG; COG0407; Bacteria.
DR   HOGENOM; CLU_040933_0_1_9; -.
DR   OMA; LWLMRQA; -.
DR   OrthoDB; 1104410at2; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000001578; 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.
FT   CHAIN           1..345
FT                   /note="Uroporphyrinogen decarboxylase"
FT                   /id="PRO_1000023908"
FT   BINDING         27..31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   SITE            76
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ   SEQUENCE   345 AA;  38872 MW;  206115AFB0F809A4 CRC64;
     MTRRINDTFL RACRGEKTAY VPVWYMRQAG RSQPEYRALK EKYSLFEITH QPELCAYVTR
     LPVEQYGVDA AILYKDIMTP LPAIGVDVEI RGGVGPVIAN PIRSLHDVER LGEIDPEHDV
     PYVLETIRLL VNEQLDVPLI GFAGAPFTLA SYMIEGGPSK NYHKTKAFMY AEPKAWFALM
     DKLAEMTIRY VKAQIQAGAS AVQIFDSWVG AVNADDYRTF IKPAMARIFA ALREEGAPLI
     MFGVGASHLA HEWNDLPLDV IGLDWRLSIR EARRRGITKA IQGNLDPAVL LAPWDVIEER
     VKRILDEGME QPGYIFNLGH GIFPDVQPAT LKRLTAFIHD YTSTK