DCUP_BURVG
ID DCUP_BURVG Reviewed; 364 AA.
AC A4JA40;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 87.
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=Bcep1808_0120;
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABO53143.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000614; ABO53143.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A4JA40; -.
DR SMR; A4JA40; -.
DR STRING; 269482.Bcep1808_0120; -.
DR EnsemblBacteria; ABO53143; ABO53143; Bcep1808_0120.
DR KEGG; bvi:Bcep1808_0120; -.
DR eggNOG; COG0407; Bacteria.
DR HOGENOM; CLU_040933_0_0_4; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000002287; Chromosome 1.
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;
KW Reference proteome.
FT CHAIN 1..364
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000325631"
FT BINDING 28..32
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT SITE 78
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ SEQUENCE 364 AA; 39543 MW; 4175A316A5C3167A CRC64;
MAHTLLNDTF LRALLREPTD YTPIWLMRQA GRYLPEYNAT RARAGSFLGL AKNPDYATEV
TLQPLDRFPL DAAILFSDIL TIPDAMGLGL DFQAGEGPKF AHPVRTEADV AKLAVPDIDE
TLGYVTGAVR EIRRALTDGQ GRQRVPLIGF SGSPWTLACY MVEGGGSDDF RTVKSMAYSR
PDLMHRILDV NAQAVAAYLN AQIEAGAQAV MIFDTWGGAL ADGAYQRFSL DYIRRVVAQL
KREHDGERVP VITFTKGGGL WLEEIAATGV DAVGLDWTVN LGAARERVAG RVALQGNLDP
TILFAPPAAV REQARAVLDS YGNHPGHVFN LGHGISQFTS PDHVAELVDE VHGYSRKLRS
GAAG