DCUP_LISMO
ID DCUP_LISMO Reviewed; 353 AA.
AC Q8Y564;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=lmo2212;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL591982; CAD00290.1; -; Genomic_DNA.
DR PIR; AD1351; AD1351.
DR RefSeq; NP_465736.1; NC_003210.1.
DR RefSeq; WP_003731891.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y564; -.
DR SMR; Q8Y564; -.
DR STRING; 169963.lmo2212; -.
DR PaxDb; Q8Y564; -.
DR EnsemblBacteria; CAD00290; CAD00290; CAD00290.
DR GeneID; 984388; -.
DR KEGG; lmo:lmo2212; -.
DR PATRIC; fig|169963.11.peg.2264; -.
DR eggNOG; COG0407; Bacteria.
DR HOGENOM; CLU_040933_0_1_9; -.
DR OMA; LWLMRQA; -.
DR PhylomeDB; Q8Y564; -.
DR BioCyc; LMON169963:LMO2212-MON; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000000817; 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: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..353
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187613"
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 321
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 353 AA; 39928 MW; A00EAC09D68190F2 CRC64;
MTKITNDLFL KAARKEQVDR IPVWYMRQAG RSQPEYRKLK EKYSLFEITH QPEICAYVTK
LPVDQYGVDA AILYKDIMTP LPGMGVDVEI KSGIGPVIHN PIRSFQDVEK LTIFKPEIEV
PYVLDTIKLL ADDMLDVPLI GFAGAPFTLA SYMIEGGPSK NYHQTKSFMY REPEVWAILM
EKLGRMTANY LIAQINAGAS AVQLFDSWVG ALSRADYAEY IRPVIEMIVR EVKAVHPTTP
IIMQAVGASH LLEEWETMPL DVVGVDWRET ITSARKKVPT KAIQGNLDPS TLLAPEKCLK
EANRILQEGV LEPGYIFNLG HGVFPEVPPE MLKQLTNYIH ERSEILLKKD DIK
