ID   DCUP_COLP3              Reviewed;         355 AA.
AC   Q489Q8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, 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=CPS_0448;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ27556.1; -; Genomic_DNA.
DR   RefSeq; YP_267206.1; -.
DR   GeneID; 3521815; -.
DR   GenomeReviews; CP000083_GR; CPS_0448.
DR   KEGG; cps:CPS_0448; -.
DR   NMPDR; fig|167879.3.peg.566; -.
DR   TIGR; CPS_0448; -.
DR   HOGENOM; Q489Q8; -.
DR   OMA; Q489Q8; VFTKGGG.
DR   BioCyc; CPSY167879:CPS_0448-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    355       Uroporphyrinogen decarboxylase.
FT                                /FTId=PRO_1000023899.
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     328    328       Substrate (By similarity).
FT   SITE         77     77       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   355 AA;  39354 MW;  39A164DDE1D10587 CRC64;
     MTELKNDTYL RALLKQPVDY TPVWMMRQAG RYLPEYREVR KNAGDFMSVC KNAELACEVT
     IQPLRRFPLD AAILFSDILT IPDAMGLGLY FETGEGPKFE RPITCKADVD KIAVPDPEDE
     LGYVMNAVRT IRKELKGEVP LIGFSGSPWT LATYMIEGGS SKAFTKIKKM MFAEPQTLHL
     LLDKLADSVI SYLNAQIAAG AQSVMVFDTW GGVLSPRDYN EFSLQYMAKI VDGLTRHNEG
     RQVPVTLFTK NGGMWLESIA ATGCDAVGLD WTIDIENAKA RVGDKVALQG NMDPSMLYAP
     LPRIEQEVSK ILSGFGEGGT GHVFNLGHGI HPDVNPDHAG HFIESVHRLS KPYHK
//