DCUP_CERS4
ID DCUP_CERS4 Reviewed; 343 AA.
AC P32920; Q3J028;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Uroporphyrinogen decarboxylase;
DE Short=UPD;
DE Short=URO-D;
DE EC=4.1.1.37;
GN Name=hemE; OrderedLocusNames=RHOS4_22880; ORFNames=RSP_0680;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 4-30, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ACTIVITY REGULATION.
RX PubMed=8352737; DOI=10.1042/bj2930703;
RA Jones R.M., Jordan P.M.;
RT "Purification and properties of the uroporphyrinogen decarboxylase from
RT Rhodobacter sphaeroides.";
RL Biochem. J. 293:703-712(1993).
CC -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of
CC uroporphyrinogen-III to yield coproporphyrinogen-III.
CC {ECO:0000269|PubMed:8352737}.
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 -!- ACTIVITY REGULATION: Inhibited by N-ethyl-maleimide and phenylglyoxal.
CC {ECO:0000269|PubMed:8352737}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 uM for uroporphyrinogen I {ECO:0000269|PubMed:8352737};
CC KM=6.0 uM for uroporphyrinogen III {ECO:0000269|PubMed:8352737};
CC pH dependence:
CC Optimum pH is 6.7-6.9. {ECO:0000269|PubMed:8352737};
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; CP000143; ABA79856.1; -; Genomic_DNA.
DR PIR; S35595; S35595.
DR RefSeq; WP_011338412.1; NZ_CP030271.1.
DR RefSeq; YP_353757.1; NC_007493.2.
DR AlphaFoldDB; P32920; -.
DR SMR; P32920; -.
DR STRING; 272943.RSP_0680; -.
DR EnsemblBacteria; ABA79856; ABA79856; RSP_0680.
DR KEGG; rsp:RSP_0680; -.
DR PATRIC; fig|272943.9.peg.2632; -.
DR eggNOG; COG0407; Bacteria.
DR OMA; LWLMRQA; -.
DR PhylomeDB; P32920; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000002703; Chromosome 1.
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 1: Evidence at protein level;
KW Cytoplasm; Decarboxylase; Direct protein sequencing; Lyase;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..343
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187632"
FT BINDING 23..27
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 73
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 18
FT /note="P -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="R -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 37575 MW; 85E196904EB46BEF CRC64;
MTKTMLRALK GETLPTPPIW LMRQAGRYLP EYRATRAQAG DFLSLCYTPD LAAEVTLQPI
RRYGFDAAIL FADILLLPQA LGADLWFETG EGPRMSTITD MAGVTALKGR DDIHETLAPV
YETCRILARE LPKETTFIGF AGMPWTVATY MIAGRGSKDQ AAAHKLKDTD RPAFEALMDR
VTEATIEYLA KQVEAGCEVV KLFDSWAGSL KGQDFEDFAV APAKRIVSEL KARFQGLPVI
AFPREAGEGY IGFAEKTGAD CVAIDNSVSP EWAAEKVQAG RTCVQGNLDP KYMVTGGEEL
VQATKRVVEA FRNGPHIFNL GHGITPEADP ENVTLLVETI RGK
