ID   DCUP_CYTH3              Reviewed;         344 AA.
AC   Q11X05;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
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=CHU_0774;
OS   Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469).
OC   Bacteria; Bacteroidetes; Sphingobacteria; Sphingobacteriales;
OC   Flexibacteraceae; Cytophaga.
OX   NCBI_TaxID=269798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17400776; DOI=10.1128/AEM.00225-07;
RA   Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C.,
RA   Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P.,
RA   Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B.,
RA   Wilson D.B., McBride M.J.;
RT   "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT   hutchinsonii.";
RL   Appl. Environ. Microbiol. 73:3536-3546(2007).
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; CP000383; ABG58061.1; -; Genomic_DNA.
DR   RefSeq; YP_677401.1; -.
DR   GeneID; 4184144; -.
DR   GenomeReviews; CP000383_GR; CHU_0774.
DR   KEGG; chu:CHU_0774; -.
DR   NMPDR; fig|269798.12.peg.736; -.
DR   HOGENOM; Q11X05; -.
DR   OMA; Q11X05; VFTKGGG.
DR   BioCyc; CHUT269798:CHU_0774-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    344       Uroporphyrinogen decarboxylase.
FT                                /FTId=PRO_0000325635.
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     319    319       Substrate (By similarity).
FT   SITE         76     76       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   344 AA;  38377 MW;  063E4CE96C62932F CRC64;
     MQYQNDLILR AARGEAVERT PVWLMRQAGR ILPEYRAVRE KLSGFIELCT TPALAAEVTI
     QPVDILGVDA AIIFSDILVI PEAMGLPYEM QESKGPFFPK VITSAADIDA LLATDAADHL
     TYVYDAIELA VKELNGRVPL IGFAGAPFTI LAYMIEGQGS KTFSKARRFL YTEPVLAHRL
     LEKITLATIA YLKRQVQAGA AMYQIFDSWA GVLPPDQYRE FSLRYIKQIC EAVPQVPRTV
     FSKGAFFVRE DFNNFPCETV GLDWNMDIGE SKKIIGPHKT LQGNMDPCAL YLSEEQIRVK
     AKEMLDAFGT QSHIANLGHG LYPDTDKTKV KCFVDAVKEF GVKK
//