ID   DCUP_ALHEH              Reviewed;         365 AA.
AC   Q0A4Y2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Uroporphyrinogen decarboxylase;
DE            Short=URO-D;
DE            Short=UPD;
DE            EC=4.1.1.37;
GN   Name=hemE; OrderedLocusNames=Mlg_2765;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-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; CP000453; ABI58105.1; -; Genomic_DNA.
DR   RefSeq; YP_743595.1; -.
DR   GeneID; 4269126; -.
DR   GenomeReviews; CP000453_GR; Mlg_2765.
DR   KEGG; aeh:Mlg_2765; -.
DR   NMPDR; fig|187272.6.peg.2639; -.
DR   HOGENOM; Q0A4Y2; -.
DR   OMA; Q0A4Y2; VFTKGGG.
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    365       Uroporphyrinogen decarboxylase.
FT                                /FTId=PRO_1000023869.
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     327    327       Substrate (By similarity).
FT   SITE         77     77       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   365 AA;  40238 MW;  55E8719A1674E67C CRC64;
     MSVLKNDRLL RALQRQPVDR TPVWMMRQAG RYLPEYRELR AQAGSFMKLA GTPELACEVT
     LQPLRRFPLD AAILFSDILT IPDAMGLGLR FLPGEGPVFD HPVRSAADIE HLPVPDPEDE
     LRYVTDAVRL IRRELDGEVP LIGFAGSPWT LATYMIEGGS SKDYRRCKAM LYDEPELLHR
     LLDKVAQATT AYLNAQIAAG AQAIMIFDSW GGALAHDAYR LFSLAYMERI VRNLTREADG
     RHVPVVLFTK GGGQWLEAMA ATGCDGLGLD WTTNLGQARD RVGDRVALQG NLDPCVLYAS
     PETIRNEVAR VLADYGPGPG HVFNLGHGIH PAIPPEHAGA MIDAVHQLSP RYHEQQAEAS
     SLTQG
//