DCUP_ROSCS
ID DCUP_ROSCS Reviewed; 352 AA.
AC A7NKU6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Rcas_2028;
OS Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=383372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13941 / HLO8;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL Submitted (AUG-2007) 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; CP000804; ABU58116.1; -; Genomic_DNA.
DR RefSeq; WP_012120540.1; NC_009767.1.
DR AlphaFoldDB; A7NKU6; -.
DR SMR; A7NKU6; -.
DR STRING; 383372.Rcas_2028; -.
DR EnsemblBacteria; ABU58116; ABU58116; Rcas_2028.
DR KEGG; rca:Rcas_2028; -.
DR eggNOG; COG0407; Bacteria.
DR HOGENOM; CLU_040933_0_0_0; -.
DR OMA; LWLMRQA; -.
DR OrthoDB; 1104410at2; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000000263; 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.
FT CHAIN 1..352
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_1000078083"
FT BINDING 24..28
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 150
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 324
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 352 AA; 38935 MW; 6277E14A29DBE933 CRC64;
MTLHRFLAAC RRQPTDATPV WFMRQAGRYM PEYRAIRERY GFLDMVKTPE LAAEITMQPL
LAFPVDAAII FADILPLLEG IGLQLTYEQG EGPVIHNPLR SSADIAALRD ADPRETVAYT
IQAIRLVKRE LEERAPLIGF SGAPFTLAAY AVEGGSSRDH RLTKALMYAE PQAWRDLMER
LTTQVSAYLI AQIEAGADAV QLFDSWAGAL APGDYAEYVL PFVQQCIINV RAGCGVVPPP
PIIYFGVGMS GMLGMLRQTD ADVIGLDWRI YLDDGWAQVG PGVAVQGNLD PHTLLAPWSD
VRRRAADILD RAASRPGHIF NLGHGIVPET PVDTVRRLAE FVHEYSAEET YD
