ID DCUP_CAMJ8 Reviewed; 340 AA. AC A8FMU8; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 02-SEP-2026, entry version 88. 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}; GN OrderedLocusNames=C8J_1186; OS Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / OS NCTC 11828). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Campylobacteraceae; Campylobacter. OX NCBI_TaxID=407148; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=81116 / NCTC 11828; RX PubMed=17873037; DOI=10.1128/jb.01404-07; RA Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M., RA van Vliet A.H.M.; RT "The complete genome sequence of Campylobacter jejuni strain 81116 RT (NCTC11828)."; RL J. Bacteriol. 189:8402-8403(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=uroporphyrinogen III + 4 H(+) = coproporphyrinogen III + 4 CC CO2; 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; CP000814; ABV52785.1; -; Genomic_DNA. DR RefSeq; WP_002866238.1; NC_009839.1. DR AlphaFoldDB; A8FMU8; -. DR SMR; A8FMU8; -. DR KEGG; cju:C8J_1186; -. DR HOGENOM; CLU_040933_0_0_7; -. DR UniPathway; UPA00251; UER00321. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006783; P:heme biosynthetic process; IEA:TreeGrafter. DR CDD; cd00717; URO-D; 1. DR FunFam; 3.20.20.210:FF:000007; Uroporphyrinogen decarboxylase; 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 NCBIfam; TIGR01464; hemE; 1. DR PANTHER; PTHR21091; METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED; 1. DR PANTHER; PTHR21091:SF169; UROPORPHYRINOGEN DECARBOXYLASE; 1. DR Pfam; PF01208; URO-D; 1. DR SUPFAM; SSF51726; UROD/MetE-like; 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..340 FT /note="Uroporphyrinogen decarboxylase" FT /id="PRO_1000071752" FT BINDING 21..25 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218" FT BINDING 71 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218" FT BINDING 148 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218" FT BINDING 203 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 71 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218" SQ SEQUENCE 340 AA; 38980 MW; 74137E54547C9F75 CRC64; MIFIDACFKK PTPYTPIWMM RQAGRYLPEY MEVRKQAGDF LSLCKDYKKA SEVSLQPIDI LDVDAAIIFS DILVVPLEMG MNLRFEKGEG PVFDNPISTL EDLEKLDDQN AHKKLNYVYD ALKLTREKLS QNKALIGFCG SPWTIATYMI EGSGSKNYAK CKKMLYQNPE LLHKILNKLT QVLKLYLEEQ IKAGANAIQI FDSWASALEY DKFFEFSFNY MLEISNFIKS KYPNIPVILF PKGISGYLDR IDGNFDVFGV DWSTPLDLAR DKLSHKYTLQ GNMEPCRLYD KNAIKEGVEK ILKTMQNKAH IFNLGHGILP DIPVENAKYF IKLVQESSAK //