ID DCUP_CAUVN Reviewed; 351 AA.
AC B8GW41; Q59269;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Uroporphyrinogen decarboxylase;
DE Short=UPD;
DE Short=URO-D;
DE EC=4.1.1.37;
GN Name=hemE; OrderedLocusNames=CCNA_03879;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-294.
RA Marczynski G.T.;
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of
CC uroporphyrinogen III to yield coproporphyrinogen III. {ECO:0000250}.
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 -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; CP001340; ACL97344.2; -; Genomic_DNA.
DR EMBL; U13664; AAA64267.1; -; Genomic_DNA.
DR PIR; I40672; I40672.
DR RefSeq; WP_010921590.1; NC_011916.1.
DR RefSeq; YP_002519252.2; NC_011916.1.
DR AlphaFoldDB; B8GW41; -.
DR SMR; B8GW41; -.
DR GeneID; 7332727; -.
DR KEGG; ccs:CCNA_03879; -.
DR PATRIC; fig|565050.3.peg.3784; -.
DR HOGENOM; CLU_040933_0_0_5; -.
DR OrthoDB; 9806656at2; -.
DR PhylomeDB; B8GW41; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000001364; 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..351
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000378316"
FT BINDING 32..36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 82
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 222..223
FT /note="DR -> EP (in Ref. 2; AAA64267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 37944 MW; E33D7A2C98765EE8 CRC64;
MTSSSPILKQ TPKFLSALEG QSHANPPVWF MRQAGRYLPE YRAVRATAPD FISFCFDPEK
AAEVTLQPMR RFPFDASIVF ADILLIPGAL GQKVWFEAGE GPKLGDMPSV ESMAEKAGEA
GKALSLVGET LTRVRSALDP DKALIGFAGA PWTVATYMIE KGSSDRSGAR TFAYQNPETL
DALIQVLVDA TIDYLAMQVD AGAQALKLFE SWAEGLSEPL FDRLVTQPHI RIIEGLRARG
VTVPIIGFPR GAGTLVEDYA ARTPVQGVAL DTSASAKLGQ TIQKTKTIQG ALDPLLLRAG
GDALLKRVDE MLEQWNQGPY IFNLGHGILP DTPIAHVEAV LERVTGQKVG Q
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