ID   DCUP_LEIXX              Reviewed;         377 AA.
AC   Q6AHF5;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Lxx01040;
OS   Leifsonia xyli subsp. xyli (strain CTCB07).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia.
OX   NCBI_TaxID=281090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTCB07;
RX   PubMed=15305603; DOI=10.1094/mpmi.2004.17.8.827;
RA   Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P.,
RA   Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D.,
RA   de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R.,
RA   Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L.,
RA   El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA   Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA   Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA   Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA   Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT   "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli
RT   subsp. xyli.";
RL   Mol. Plant Microbe Interact. 17:827-836(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016822; AAT88190.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6AHF5; -.
DR   SMR; Q6AHF5; -.
DR   STRING; 281090.Lxx01040; -.
DR   EnsemblBacteria; AAT88190; AAT88190; Lxx01040.
DR   KEGG; lxx:Lxx01040; -.
DR   eggNOG; COG0407; Bacteria.
DR   HOGENOM; CLU_040933_0_1_11; -.
DR   OMA; LWLMRQA; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000001306; 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..377
FT                   /note="Uroporphyrinogen decarboxylase"
FT                   /id="PRO_0000187610"
FT   BINDING         40..44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   SITE            89
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ   SEQUENCE   377 AA;  40155 MW;  9E187D7DDE2E43EF CRC64;
     MIVTALDPTH PLAAGLTHAS RLVRSYQGER QEVTPVWFMR QAGRSLPEYR DLRVGTRMLD
     VCLDPAMASE ITLQPVRRHG VDAGIFFSDI VVPLKLAGVE VEIQPGKGPV FERAVRTSAD
     VDRLSAVDPA ALAADTFAAV QEAVRLTTAE LNETPLIGFA GAPFTLAAYL VEGGPSKDHL
     RARTLMHAAP GAWARLMDWT ADLSGAFLRA QVLAGASAAQ LFDSWAGSLS LRDYAEHAAP
     ASARAFSHVR DLTYTVPSAD PDGEAVVRAV PIVHFGVGTG ELLPAMHEAG ADAIGVDHRT
     LLDEASRRLG HIVPLQGNAD PAMLAAPWEV LSGHALDVLD RGRAAPAHVF NLGHGVPPET
     DPAVLTRVVE LVHGWRA