DCUP_SYNE7
ID DCUP_SYNE7 Reviewed; 354 AA.
AC P16891; Q31PA3;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 132.
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=Synpcc7942_1086;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1339332; DOI=10.3109/10425179209020822;
RA Kiel J.A.K.W., ten Berge A.M., Venema G.;
RT "Nucleotide sequence of the Synechococcus sp. PCC7942 hemE gene encoding
RT the homologue of mammalian uroporphyrinogen decarboxylase.";
RL DNA Seq. 2:415-418(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
RX PubMed=2142668; DOI=10.1016/0378-1119(90)90208-9;
RA Kiel J.A.K.W., Boels J.M., Beldman G., Venema G.;
RT "Nucleotide sequence of the Synechococcus sp. PCC7942 branching enzyme gene
RT (glgB): expression in Bacillus subtilis.";
RL Gene 89:77-84(1990).
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 + coproporphyrinogen
CC III; Xref=Rhea:RHEA:19865, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57308, ChEBI:CHEBI:57309; EC=4.1.1.37;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00218};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
CC {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}.
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DR EMBL; Z11705; CAA77766.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57116.1; -; Genomic_DNA.
DR EMBL; M31544; AAB39039.1; -; Genomic_DNA.
DR PIR; A56609; A56609.
DR RefSeq; WP_011242775.1; NC_007604.1.
DR AlphaFoldDB; P16891; -.
DR SMR; P16891; -.
DR STRING; 1140.Synpcc7942_1086; -.
DR PRIDE; P16891; -.
DR EnsemblBacteria; ABB57116; ABB57116; Synpcc7942_1086.
DR KEGG; syf:Synpcc7942_1086; -.
DR eggNOG; COG0407; Bacteria.
DR HOGENOM; CLU_040933_0_2_3; -.
DR OMA; LWLMRQA; -.
DR OrthoDB; 1104410at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1086-MON; -.
DR UniPathway; UPA00251; UER00321.
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;
KW Cytoplasm; Decarboxylase; Lyase; Porphyrin biosynthesis.
FT CHAIN 1..354
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187650"
FT BINDING 28..32
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT SITE 78
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ SEQUENCE 354 AA; 39278 MW; 3F6846658734C1E9 CRC64;
MVASSSLPRL LRAARGEVLD RPPVWMMRQA GRYMKVYRDL RDKYPGFRER SETPELAIEI
SLQPFRAFKP DGVILFSDIL TPLPGMGIPF DIIESKGPIL EPPIRTAEQV AAVHDLDPEE
ATPFIRPILE TLRQEVGNEA AVLGFAGAPW TLAAYAIEGK SSKTYANIKH LAFSEPTILH
ELLGKLADNI AIYLCHQIDC GAQVVQLFDS WAGQLSPIDY DTFALPYQQR VFQQVKAKHP
EVPLILYISG SAGVLERMGQ SGCDIVSVDW TVDLLDARRR LGPDIGLQGN IDPGVLFGSQ
DFIRDRILDT VRKAGNQRHI LNLGHGILPG TPEDNARHFF ETAKNLDQLL AASH
