DCUP_BURTA
ID DCUP_BURTA Reviewed; 364 AA.
AC Q2STF3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=BTH_I3304;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(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; CP000086; ABC37811.1; -; Genomic_DNA.
DR RefSeq; WP_009906695.1; NZ_CP008785.1.
DR PDB; 4EXQ; X-ray; 1.65 A; A=1-364.
DR PDBsum; 4EXQ; -.
DR AlphaFoldDB; Q2STF3; -.
DR SMR; Q2STF3; -.
DR PRIDE; Q2STF3; -.
DR EnsemblBacteria; ABC37811; ABC37811; BTH_I3304.
DR KEGG; bte:BTH_I3304; -.
DR HOGENOM; CLU_040933_0_0_4; -.
DR OMA; LWLMRQA; -.
DR OrthoDB; 1104410at2; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000001930; Chromosome I.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Decarboxylase; Lyase; Porphyrin biosynthesis.
FT CHAIN 1..364
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_1000023885"
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"
FT STRAND 1..3
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 9..14
FT /evidence="ECO:0007829|PDB:4EXQ"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:4EXQ"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:4EXQ"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:4EXQ"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4EXQ"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 181..205
FT /evidence="ECO:0007829|PDB:4EXQ"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:4EXQ"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:4EXQ"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 281..288
FT /evidence="ECO:0007829|PDB:4EXQ"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 307..321
FT /evidence="ECO:0007829|PDB:4EXQ"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:4EXQ"
FT HELIX 341..358
FT /evidence="ECO:0007829|PDB:4EXQ"
SQ SEQUENCE 364 AA; 39497 MW; 20BF248D8BFA8136 CRC64;
MAQTLINDTF LRALLREPTD YTPIWLMRQA GRYLPEYNAT RARAGSFLGL AKHPDYATEV
TLQPLERFPL DAAILFSDIL TIPDAMGLGL DFAAGEGPKF AHPVRTEADV AKLAVPDIGA
TLGYVTDAVR EIRRALTDGE GRQRVPLIGF SGSPWTLACY MVEGGGSDDF RTVKSMAYAR
PDLMHRILDV NAQAVAAYLN AQIEAGAQAV MIFDTWGGAL ADGAYQRFSL DYIRRVVAQL
KREHDGARVP AIAFTKGGGL WLEDLAATGV DAVGLDWTVN LGRARERVAG RVALQGNLDP
TILFAPPEAI RAEARAVLDS YGNHPGHVFN LGHGISQFTP PEHVAELVDE VHRHSRAIRS
GTGS
