DCUP_CHESB
ID DCUP_CHESB Reviewed; 342 AA.
AC Q11CM8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Meso_3476;
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX NCBI_TaxID=266779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BNC1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000390; ABG64847.1; -; Genomic_DNA.
DR RefSeq; WP_011582788.1; NC_008254.1.
DR AlphaFoldDB; Q11CM8; -.
DR SMR; Q11CM8; -.
DR STRING; 266779.Meso_3476; -.
DR EnsemblBacteria; ABG64847; ABG64847; Meso_3476.
DR KEGG; mes:Meso_3476; -.
DR eggNOG; COG0407; Bacteria.
DR HOGENOM; CLU_040933_0_0_5; -.
DR OMA; LWLMRQA; -.
DR OrthoDB; 1104410at2; -.
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..342
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_1000023919"
FT BINDING 24..28
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT SITE 74
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ SEQUENCE 342 AA; 37964 MW; 7093FB487D1DE419 CRC64;
MAERKLLEAL NGRTVFPPPI WLMRQAGRYL PEYRETRKKA GSFLDLCYNP ELAVEVTLQP
IRRFGFDAAI LFSDILVIPH ALGRDLRFEE GAGPLMSPIQ ANEIPGLDPN LIHNRLQPVY
ETVRRLRSEL SEETALIGFC GAPWTVATYM IAGRGTPDQA PARLFGYRHP KEFSELLDTI
SAASADYLIR QIDEGADAVQ IFDSWAGILD ETSFDQWCLR PVAEIVRRVR ERHPNVPIIG
FPKGAGWLYS RYRQQTGVTA LGLDWTVPLS EASRLQAEGP VQGNLDPMRL VAGGQALSKG
VEDILSALGG APFIFNLGHG ITPETPIGHV EAMIQQVREG RL
