(data stored in ACNUC7421 zone)

SWISSPROT: DCUP_PSEU2

ID   DCUP_PSEU2              Reviewed;         354 AA.
AC   Q4ZZD8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000255|HAMAP-Rule:MF_00218};
DE            Short=UPD {ECO:0000255|HAMAP-Rule:MF_00218};
DE            Short=URO-D {ECO:0000255|HAMAP-Rule:MF_00218};
DE            EC=4.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00218};
GN   Name=hemE {ECO:0000255|HAMAP-Rule:MF_00218};
GN   OrderedLocusNames=Psyr_0414;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of
CC       uroporphyrinogen-III to yield coproporphyrinogen-III.
CC       {ECO:0000255|HAMAP-Rule:MF_00218}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 H(+) + uroporphyrinogen III = 4 CO2 +
CC         coproporphyrinogen III; Xref=Rhea:RHEA:19865, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57308, ChEBI:CHEBI:57309;
CC         EC=4.1.1.37; Evidence={ECO:0000255|HAMAP-Rule:MF_00218};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate:
CC       step 4/4. {ECO:0000255|HAMAP-Rule:MF_00218}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00218}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00218}.
CC   -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00218}.
DR   EMBL; CP000075; AAY35484.1; -; Genomic_DNA.
DR   RefSeq; WP_003403024.1; NC_007005.1.
DR   RefSeq; YP_233522.1; NC_007005.1.
DR   SMR; Q4ZZD8; -.
DR   STRING; 205918.Psyr_0414; -.
DR   EnsemblBacteria; AAY35484; AAY35484; Psyr_0414.
DR   GeneID; 3365890; -.
DR   KEGG; psb:Psyr_0414; -.
DR   PATRIC; fig|205918.7.peg.430; -.
DR   eggNOG; ENOG4105CFZ; Bacteria.
DR   eggNOG; COG0407; LUCA.
DR   HOGENOM; HOG000253896; -.
DR   KO; K01599; -.
DR   OMA; GSSKDFR; -.
DR   BioCyc; PSYR205918:G1G4J-415-MONOMER; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00717; URO-D; 1.
DR   Gene3D; 3.20.20.210; -; 1.
DR   HAMAP; MF_00218; URO_D; 1.
DR   InterPro; IPR038071; UROD/MetE-like_sf.
DR   InterPro; IPR006361; Uroporphyrinogen_deCO2ase_HemE.
DR   InterPro; IPR000257; Uroporphyrinogen_deCOase.
DR   Pfam; PF01208; URO-D; 1.
DR   SUPFAM; SSF51726; SSF51726; 1.
DR   TIGRFAMs; TIGR01464; hemE; 1.
DR   PROSITE; PS00906; UROD_1; 1.
DR   PROSITE; PS00907; UROD_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4ZZD8.
DR   SWISS-2DPAGE; Q4ZZD8.
KW   Complete proteome; Cytoplasm; Decarboxylase; Lyase;
KW   Porphyrin biosynthesis.
FT   CHAIN         1    354       Uroporphyrinogen decarboxylase.
FT                                /FTId=PRO_1000023953.
FT   REGION       27     31       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00218}.
FT   BINDING      77     77       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00218}.
FT   BINDING     154    154       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00218}.
FT   BINDING     209    209       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00218}.
FT   BINDING     327    327       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00218}.
FT   SITE         77     77       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00218}.
SQ   SEQUENCE   354 AA;  38657 MW;  1DEF6252CF41A53A CRC64;
     MTALKNDRFL RALLKQPVDV TPVWMMRQAG RYLPEYRASR ASAGDFMSLC KNPQFACEVT
     LQPLDRYPLD AAILFSDILT IPDAMGQGLY FETGEGPRFR KTVSTLADIE ALPIPDAQQD
     LGYVMDAVST IRRELNGRVP LIGFAGSPWT LATYMVEGGS SKDFRKSKAM LYDNPQAMHL
     LLDKLAQSVT SYLNGQILAG AQAVQIFDSW GGSLSSAAYQ EFSLAYMRKI VSGLIRENDG
     RKVPVIVFTK GGGLWLESIA DIGADTLGLD WTCDIGEARQ RVGSKVSLQG NMDPTVLYAR
     PEAIRQEVAR ILASYGSGTG HVFNLGHGIT PEVDPANAGA FINAVHELSA QYHV
//

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