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   16-JUN-2009, entry version 25.
DE   RecName: Full=Uroporphyrinogen decarboxylase;
DE            Short=URO-D;
DE            Short=UPD;
DE            EC=4.1.1.37;
GN   Name=hemE; OrderedLocusNames=BTH_I3304;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of
CC       uroporphyrinogen-III to yield coproporphyrinogen-III (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Uroporphyrinogen III = coproporphyrinogen + 4
CC       CO(2).
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis;
CC       coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
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DR   EMBL; CP000086; ABC37811.1; -; Genomic_DNA.
DR   RefSeq; YP_443796.1; -.
DR   GeneID; 3849034; -.
DR   GenomeReviews; CP000086_GR; BTH_I3304.
DR   KEGG; bte:BTH_I3304; -.
DR   TIGR; BTH_I3304; -.
DR   HOGENOM; Q2STF3; -.
DR   OMA; Q2STF3; VFTKGGG.
DR   BioCyc; BTHA271848:BTH_I3304-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:HAMAP.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00218; -; 1.
DR   InterPro; IPR006361; Uroporphyrinogen_deCO2ase_HemE.
DR   InterPro; IPR000257; Uroporphyrinogen_deCOase.
DR   PANTHER; PTHR21091:SF2; HemE; 1.
DR   Pfam; PF01208; URO-D; 1.
DR   ProDom; PD003225; Uro_decarbxyls; 1.
DR   TIGRFAMs; TIGR01464; hemE; 1.
DR   PROSITE; PS00906; UROD_1; 1.
DR   PROSITE; PS00907; UROD_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Decarboxylase; Lyase;
KW   Porphyrin biosynthesis.
FT   CHAIN         1    364       Uroporphyrinogen decarboxylase.
FT                                /FTId=PRO_1000023885.
FT   REGION       28     32       Substrate binding (By similarity).
FT   BINDING      78     78       Substrate (By similarity).
FT   BINDING     160    160       Substrate (By similarity).
FT   BINDING     215    215       Substrate (By similarity).
FT   BINDING     333    333       Substrate (By similarity).
FT   SITE         78     78       Transition state stabilizer (By
FT                                similarity).
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
//