ID   DCUP_ANAVT              Reviewed;         350 AA.
AC   Q3MC76;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Uroporphyrinogen decarboxylase;
DE            Short=URO-D;
DE            Short=UPD;
DE            EC=4.1.1.37;
GN   Name=hemE; OrderedLocusNames=Ava_1788;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
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., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-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.
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DR   EMBL; CP000117; ABA21410.1; -; Genomic_DNA.
DR   RefSeq; YP_322305.1; -.
DR   GeneID; 3682072; -.
DR   GenomeReviews; CP000117_GR; Ava_1788.
DR   KEGG; ava:Ava_1788; -.
DR   NMPDR; fig|240292.3.peg.2868; -.
DR   HOGENOM; Q3MC76; -.
DR   OMA; Q3MC76; VFTKGGG.
DR   BioCyc; AVAR240292:AVA_1788-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    350       Uroporphyrinogen decarboxylase.
FT                                /FTId=PRO_1000023870.
FT   REGION       28     32       Substrate binding (By similarity).
FT   BINDING      78     78       Substrate (By similarity).
FT   BINDING     155    155       Substrate (By similarity).
FT   BINDING     210    210       Substrate (By similarity).
FT   BINDING     325    325       Substrate (By similarity).
FT   SITE         78     78       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   350 AA;  38823 MW;  5BF7EBC98A08B687 CRC64;
     MGVTSTAPHL LRAARGEIVD RPPVWMMRQA GRYMKAYRDL REKYPSFRDR SEIPEVAIEV
     SLQPWKAFQP DGVILFSDIV TPLPGLGIEM DIAEGKGPII HAPIRTQAQI EQLRPLEPEA
     ALPFIKTILQ ALRQEVGHQS TVLGFVGAPW TLAAYAVEGK GSKTYSIIKN LAFSEPAILH
     QLLTKLADAI AIYARYQIDS GAQVVQMFDS WAGQLSPQDY DTFALPYQQR VFQQIKQTHP
     DTPLILLVSG SAGVLERMGQ SGADIVTVDW TVDMADARAR LGKQMKVQGN LDPGVLYASK
     QFIRDRIIDT VRKAGNWGHI LNLGHGVLPD TPEENVAFFF ETAKQLNVLV
//