DCUP_WOLTR
ID DCUP_WOLTR Reviewed; 347 AA.
AC Q5GTT1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Wbm0001;
OS Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=292805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRS;
RX PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA Koonin E., Slatko B.;
RT "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT human pathogenic nematode.";
RL PLoS Biol. 3:599-614(2005).
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; AE017321; AAW70593.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5GTT1; -.
DR SMR; Q5GTT1; -.
DR STRING; 292805.Wbm0001; -.
DR EnsemblBacteria; AAW70593; AAW70593; Wbm0001.
DR KEGG; wbm:Wbm0001; -.
DR eggNOG; COG0407; Bacteria.
DR HOGENOM; CLU_040933_0_0_5; -.
DR OMA; LWLMRQA; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000000534; 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..347
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000325710"
FT BINDING 36..40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 86
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 212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT SITE 86
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ SEQUENCE 347 AA; 38676 MW; F7C4AFC8E981E388 CRC64;
MKEESELARI KSSKAVVSKT IKEGKQGRKI PIWLMRQAGR SLPEYRRAVK DTSSFMEICY
NTDLVVELTL QPVARFSMDA AIIFSDILIV ADVLGCDVDF IRGVGPTIKP VKNFKELRNP
QKIETKTLPI LNAIRKVRDK LPEEKSLIGF AGGPWTVASY IIEGRSSKTF SKVLNLHPSS
LEQIIEQITE VTISYLVKQI EFGADVIQLF DSNAGVLSGE LFEECVIKPT KKIVSAIKGK
FPDFPIIGFP KSAGSLYKDY CEKTGVSAVS IDYNVPIEWA KENLKIPLQG NLNPSLLAYN
KMEAIKETKR IIDCFRDLPF IFNLGHGVLP NTPIENIAAL VDLVKSQ