DCUP_GEOSM
ID DCUP_GEOSM Reviewed; 339 AA.
AC C6E7R9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=GM21_0015;
OS Geobacter sp. (strain M21).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter; unclassified Geobacter.
OX NCBI_TaxID=443144;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M21;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Lovley D.;
RT "Complete sequence of Geobacter sp. M21.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001661; ACT16102.1; -; Genomic_DNA.
DR RefSeq; WP_012773730.1; NC_012918.1.
DR AlphaFoldDB; C6E7R9; -.
DR SMR; C6E7R9; -.
DR STRING; 443144.GM21_0015; -.
DR EnsemblBacteria; ACT16102; ACT16102; GM21_0015.
DR KEGG; gem:GM21_0015; -.
DR eggNOG; COG0407; Bacteria.
DR HOGENOM; CLU_040933_0_1_7; -.
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..339
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_1000204232"
FT BINDING 23..27
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT SITE 72
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ SEQUENCE 339 AA; 37591 MW; 58B7FD44FF037962 CRC64;
MNTRFLDACW GKPVDTVPVW LMRQAGRYLP DYMRVRSKCT FLELCKTPEL ATEVTVQPVD
ILGVDAAILF SDILTPIEPM GMELDFTPGP VFAKPIRTMA DVEALKIPKM ETDVPYVLDA
VKLLRKELAA KVPLIGFGGA PFTLACYMVE GKGSKDFAAL KKMMYADPEV YAALMEKITT
MDMEYLNAQI KAGAQAIQIF DTWGGMLSPA DYERYVLPYT QRLINGLDRT NIPVIHFVKG
AGTMLEIVKQ AGGDVMGLDW HVNLGKARDI LGDMAVQGNL DPTVLFAPNE IIEREVKRVL
DENAGRPGLI FNLGHGILPT VPPEKAIFMV DCVHRLSRK