ID   DCUP_CHLTA              Reviewed;         336 AA.
AC   Q3KKU6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Uroporphyrinogen decarboxylase;
DE            Short=URO-D;
DE            Short=UPD;
DE            EC=4.1.1.37;
GN   Name=hemE; OrderedLocusNames=CTA_0813;
OS   Chlamydia trachomatis (strain A/HAR-13 / ATCC VR-571B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177312; DOI=10.1128/IAI.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(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; CP000051; AAX51026.1; -; Genomic_DNA.
DR   RefSeq; YP_328574.1; -.
DR   GeneID; 3687539; -.
DR   GenomeReviews; CP000051_GR; CTA_0813.
DR   KEGG; cta:CTA_0813; -.
DR   HOGENOM; Q3KKU6; -.
DR   OMA; Q3KKU6; VFTKGGG.
DR   BioCyc; CTRA315277-1:CTA_0813-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    336       Uroporphyrinogen decarboxylase.
FT                                /FTId=PRO_1000023897.
FT   REGION       24     28       Substrate binding (By similarity).
FT   BINDING      73     73       Substrate (By similarity).
FT   BINDING     142    142       Substrate (By similarity).
FT   BINDING     197    197       Substrate (By similarity).
FT   BINDING     312    312       Substrate (By similarity).
FT   SITE         73     73       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   336 AA;  37703 MW;  B982F3661DD00859 CRC64;
     MPMTGFYETI SPRDQQRPPI WFLRQVGRYI PQYQELKRNR SLKDFFLDTE SIVEATLLGP
     SLLGVDAAIV FADILSILEG FSVDYRFAPG PEVSYSPHEP LIFTKDPQET FSFLLEAIQQ
     LTKRLTVPLI AFAASPFTLA SYLIEGGASR DYPKTIAFLY QYPDRFKALL DEITLGTATY
     LQMQVQAGAA AIQLFESSSL RLPPHLFAKY VVAPNTKLIR QIKQTGNPPI SLFCRCFYQE
     FLSLYAIGAD TLHPDYHVEL PEVYRQIHSP GSIQGNFDPA LLLLPQDALI AHLEAYLAPL
     KQQSHYIFNL GHGILPQTPI ENVQAVVSCL TSISTS
//