ID   DCUP_CHRSD              Reviewed;         353 AA.
AC   Q1R1C8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Uroporphyrinogen decarboxylase;
DE            Short=URO-D;
DE            Short=UPD;
DE            EC=4.1.1.37;
GN   Name=hemE; OrderedLocusNames=Csal_0116;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
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., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-2006) 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; CP000285; ABE57480.1; -; Genomic_DNA.
DR   RefSeq; YP_572179.1; -.
DR   GeneID; 4027042; -.
DR   GenomeReviews; CP000285_GR; Csal_0116.
DR   KEGG; csa:Csal_0116; -.
DR   NMPDR; fig|290398.4.peg.447; -.
DR   HOGENOM; Q1R1C8; -.
DR   OMA; Q1R1C8; VFTKGGG.
DR   BioCyc; CSAL290398:CSAL_0116-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    353       Uroporphyrinogen decarboxylase.
FT                                /FTId=PRO_0000325633.
FT   REGION       26     30       Substrate binding (By similarity).
FT   BINDING      76     76       Substrate (By similarity).
FT   BINDING     153    153       Substrate (By similarity).
FT   BINDING     208    208       Substrate (By similarity).
FT   BINDING     326    326       Substrate (By similarity).
FT   SITE         76     76       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   353 AA;  39041 MW;  83C5FDBF155A9CEA CRC64;
     MPLQNDRLLR ALARQPVDRT PVWMMRQAGR YLPEYRETRG QAGSFMDLCR NAELACEVTM
     QPLRRYALDA AILFSDILTI PDAMDLGLYF ETGEGPKFRK TVRSAEAVDA LPVPDAERDL
     DYVMNAVRTI RHELADSVPL IGFSGSPWTL ATYMIEGGSS KDFRHAKALM YGDPAAMHAL
     LDKLARSVTD YLNAQIRAGA QIVQIFDTWG GVLSTPAYRE FSLAYMARIV EGLIREHEGR
     HVPVILFTKQ GGQWLETIAD SGADAVGLDW TTELSDARAR VGDRVALQGN LDPNVLFASP
     QAIRDEVARI LASYGSGPGH VFNLGHGVSQ FTDPDHVAAF IEALHELSPR YHG
//