ID   DCUP_ANADE              Reviewed;         346 AA.
AC   Q2IPY2;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Uroporphyrinogen decarboxylase;
DE            Short=URO-D;
DE            Short=UPD;
DE            EC=4.1.1.37;
GN   Name=hemE; OrderedLocusNames=Adeh_1088;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
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., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-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; CP000251; ABC80863.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_464300.1; -.
DR   GeneID; 3887035; -.
DR   GenomeReviews; CP000251_GR; Adeh_1088.
DR   KEGG; ade:Adeh_1088; -.
DR   HOGENOM; Q2IPY2; -.
DR   BioCyc; ADEH290397:ADEH_1088-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    346       Uroporphyrinogen decarboxylase.
FT                                /FTId=PRO_0000325621.
FT   REGION       23     27       Substrate binding (By similarity).
FT   BINDING      72     72       Substrate (By similarity).
FT   BINDING     155    155       Substrate (By similarity).
FT   BINDING     209    209       Substrate (By similarity).
FT   BINDING     322    322       Substrate (By similarity).
FT   SITE         72     72       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   346 AA;  37690 MW;  299F9BFF86711BAA CRC64;
     MTHRFLAACR REPVDRVPVW MMRQAGRYQP SYRAVRQKVS FLELCRSPEL IAQVTVAPID
     EFGFDAAILF SDILVHLPAM GLDLTFEKGE KGKGDGGPKI GNPVRTRADV DALRVPVPKK
     DLPYVLDGVR AIRTALADRV PLIGFVGGPF TVASYAVEGG SQGFTRLKTM LYAEPATAHA
     LFEKLTQAAI VQIEEQVAAG AQAAQIFESW LGELAREDLE EFSFPYLARI AEAVRKTGVP
     SIIFSTGTTA HLERMAKLGY DVVSVDWRIP IDEARARLPG VAVQGNYDST LLLGPREVAV
     ARAQQLLRAA GPTPGYIFNL GHGIQVGTPT ENVKAVVDAV HAFGWK
//