ID   DCUP_DECAR              Reviewed;         355 AA.
AC   Q47K40;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Uroporphyrinogen decarboxylase;
DE            Short=URO-D;
DE            Short=UPD;
DE            EC=4.1.1.37;
GN   Name=hemE; OrderedLocusNames=Daro_0032;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K.,
RA   Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT   "Complete sequence of Dechloromonas aromatica RCB.";
RL   Submitted (AUG-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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000089; AAZ44791.1; -; Genomic_DNA.
DR   RefSeq; YP_283261.1; -.
DR   GeneID; 3567794; -.
DR   GenomeReviews; CP000089_GR; Daro_0032.
DR   KEGG; dar:Daro_0032; -.
DR   NMPDR; fig|159087.4.peg.136; -.
DR   HOGENOM; Q47K40; -.
DR   OMA; Q47K40; VFTKGGG.
DR   BioCyc; DARO159087:DARO_0032-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    355       Uroporphyrinogen decarboxylase.
FT                                /FTId=PRO_1000023901.
FT   REGION       27     31       Substrate binding (By similarity).
FT   BINDING      77     77       Substrate (By similarity).
FT   BINDING     154    154       Substrate (By similarity).
FT   BINDING     209    209       Substrate (By similarity).
FT   BINDING     328    328       Substrate (By similarity).
FT   SITE         77     77       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   355 AA;  39370 MW;  3A25ED4B2760E098 CRC64;
     MSRPKNDTFL RALLKEPTEY TPLWLMRQAG RYLPEYCETR KRAGNFLNLC KSPTMACEVT
     LQPLARYDLD AAILFSDILT VPDAMGLGLY FAEGEGPKFE RPLREEWAIN NLTVTDPYEH
     LGYVMDAVSE IRRALDNSVP LIGFSGSPYT LACYMVEGEG SSDFRNIKAM LYNRPDLLHR
     ILSVTADSVI AYLNAQIDSG AQAVMIFDTW GGSLSNAAYE EFSLQYMRRI VAGLKKEKDG
     QRIPSIVFTK NGGLWLEKIA DIGCDAVGLD WTIDIGEARR RVGDKVALQG NLDPNVLFAQ
     PEIVAAEAKK VLDSFGPANT GHVFNLGHGI SQFTPPESVT ALVEAVHSHS RLSRK
//