DCUP_FRAT1
ID DCUP_FRAT1 Reviewed; 344 AA.
AC Q14K23;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, 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=FTF0047;
OS Francisella tularensis subsp. tularensis (strain FSC 198).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=393115;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSC 198;
RX PubMed=17406676; DOI=10.1371/journal.pone.0000352;
RA Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J.,
RA Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E.,
RA Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.;
RT "Genome sequencing shows that European isolates of Francisella tularensis
RT subspecies tularensis are almost identical to US laboratory strain Schu
RT S4.";
RL PLoS ONE 2:E352-E352(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; AM286280; CAL08063.1; -; Genomic_DNA.
DR RefSeq; WP_003022918.1; NC_008245.1.
DR AlphaFoldDB; Q14K23; -.
DR SMR; Q14K23; -.
DR KEGG; ftf:FTF0047; -.
DR HOGENOM; CLU_040933_0_0_6; -.
DR OMA; LWLMRQA; -.
DR UniPathway; UPA00251; UER00321.
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..344
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000325644"
FT BINDING 23..27
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 204
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 73
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ SEQUENCE 344 AA; 38875 MW; 657743CFFAEA67EF CRC64;
MRKLFLDAFG EKKLDKPPVW IMRQAGRYLP EYRAVRAKFD NFMDMCRNAD ACCEVALHPL
QRYDLDAAIV FSDILTIPEA MGMDLKFIKG TGPVFSEPIQ SQKDLDKLKS IEDSIGSLDY
VYNAVKTTSS AINVPLIGFT GSPWTLAAYM IEGSGSKQFN KLRKMMYANP QLMHSLLQRL
ADITIIYLLE QVKAGASSVM IFDTWGGILP LEHYKNFSLK YMEYIAKNVK QKINIPIVFF
TKGGSNFFEE IKDKSCDGVG VDWSVTLKQA RHRIGVGKVL QGNFDPAFLY GSKQSIRETV
RANIEFIQSD KLNNYIVNLG HGIYPDIDPD SVRVMIDAIR EFSA