ID   DCUP_ALCBS              Reviewed;         353 AA.
AC   Q0VMC3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-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=ABO_2227;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL17675.1; -; Genomic_DNA.
DR   RefSeq; YP_693947.1; -.
DR   GeneID; 4212185; -.
DR   GenomeReviews; AM286690_GR; ABO_2227.
DR   KEGG; abo:ABO_2227; -.
DR   NMPDR; fig|393595.12.peg.2227; -.
DR   HOGENOM; Q0VMC3; -.
DR   OMA; Q0VMC3; VFTKGGG.
DR   BioCyc; ABOR393595:ABO_2227-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_0000325620.
FT   REGION       29     33       Substrate binding (By similarity).
FT   BINDING      79     79       Substrate (By similarity).
FT   BINDING     156    156       Substrate (By similarity).
FT   BINDING     211    211       Substrate (By similarity).
FT   BINDING     329    329       Substrate (By similarity).
FT   SITE         79     79       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   353 AA;  38968 MW;  1C23D2AA76CFFD4F CRC64;
     MTFAPLQNDR FLRALNRETV DRTPIWMMRQ AGRYLPEYRA AREHAGSFMD LCKNADLACE
     VTLQPLERYP LDAAILFSDI LTIPDAMGLG LYFETGEGPK FRKVVRTEAD VAALPIPDAE
     SDLGYVMNAV STIRGALNGR VPLIGFSGSP WTLATYMVEG GSSKDFRHLK AMVYSQPELA
     HAMLDKLAQS VTGYLNAQIR HGAQAVQIFD TWGGALSAEA YKEFSLRYMQ QIVDGLIRDN
     EGRKVPVILF TKNGGLWLES MAATGCDALG LDWTINIGDA RRRVGDKVAL QGNMDPAVLY
     ASPQAIRAEV KRILDDFGDH PGHIFNLGHG ITPQVDPEHA KVFIEAVVEL SQK
//