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Database: UniProt
Entry: DCUP_JANMA
LinkDB: DCUP_JANMA
Original site: DCUP_JANMA 
ID   DCUP_JANMA              Reviewed;         360 AA.
AC   A6T450;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
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}; OrderedLocusNames=mma_3607;
OS   Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=375286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marseille;
RX   PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA   Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA   Drancourt M.;
RT   "Genome analysis of Minibacterium massiliensis highlights the convergent
RT   evolution of water-living bacteria.";
RL   PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR88675.1; -; Genomic_DNA.
DR   RefSeq; WP_012081443.1; NC_009659.1.
DR   AlphaFoldDB; A6T450; -.
DR   SMR; A6T450; -.
DR   STRING; 375286.mma_3607; -.
DR   KEGG; mms:mma_3607; -.
DR   eggNOG; COG0407; Bacteria.
DR   HOGENOM; CLU_040933_0_0_4; -.
DR   OrthoDB; 9806656at2; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000006388; 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   NCBIfam; TIGR01464; hemE; 1.
DR   PANTHER; PTHR21091; METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED; 1.
DR   PANTHER; PTHR21091:SF169; UROPORPHYRINOGEN DECARBOXYLASE; 1.
DR   Pfam; PF01208; URO-D; 1.
DR   SUPFAM; SSF51726; UROD/MetE-like; 1.
DR   PROSITE; PS00906; UROD_1; 1.
DR   PROSITE; PS00907; UROD_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Decarboxylase; Lyase; Porphyrin biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..360
FT                   /note="Uroporphyrinogen decarboxylase"
FT                   /id="PRO_0000325658"
FT   BINDING         31..35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   SITE            81
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ   SEQUENCE   360 AA;  39554 MW;  0AA3084E30AF5AA4 CRC64;
     MPTQFAPLQN DTFLRALLRQ PTEYTPLWLM RQAGRYLPEY RATRARAGSF LGLAKNPDFA
     TEVTLQPLDR YKLDAAILFS DILTVPDAMG LGLYFIEGEG PKFERPLRDE KAVQALKVPE
     LGSLQYVFDA VTQIRTELKG RVPLIGFTGS PWTLACYMVE GGGSDDFRTV KAMLYNRPDL
     MHHILQTNAL TVAAYLNAQI DAGAQAVMMF DTWGGALADG AYQQFSLHYM REVMKHVKTE
     KDGVRIPSIV FTKGGGLWLK EIAAVGADAV GLDWTVNLGA ARAKVGERVA LQGNLDPSIL
     FAQPDQIRAE VAKVLESFGK HSAGSGHVFN LGHGISQFTP PEAVTVLVDA VHELSRPLHK
//
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