DCUP_DROVI
ID DCUP_DROVI Reviewed; 386 AA.
AC O18601;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Uroporphyrinogen decarboxylase;
DE Short=UPD;
DE Short=URO-D;
DE EC=4.1.1.37;
GN Name=Urod {ECO:0000250|UniProtKB:Q9V595};
GN Synonyms=Updo {ECO:0000250|UniProtKB:Q9V595};
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Gao L., Wang S., Hickey D.A.;
RL Submitted (MAR-1997) 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.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; U93213; AAB66372.1; -; Genomic_DNA.
DR AlphaFoldDB; O18601; -.
DR SMR; O18601; -.
DR STRING; 7244.FBpp0235919; -.
DR PRIDE; O18601; -.
DR eggNOG; KOG2872; Eukaryota.
DR UniPathway; UPA00251; UER00321.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-EC.
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; Heme biosynthesis; Lyase; Porphyrin biosynthesis.
FT CHAIN 1..386
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187574"
FT BINDING 44..48
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 93
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 386 AA; 43023 MW; A119F8CC5F17DF6D CRC64;
MTIKNNNNNN TLKHLQAFPP LKNDNLLRAA RGEVVDRVPV WVMRQAGRYL PEFQELRKQH
DFFTVCRTPE LACEVTMQPL RRFDLDASII FSDILVIPQA LGLTVEMHAG VGPVLPQPIC
TPEDLKRLTP DGALSRLTYV GDAITMMRHK LDGRVPLIGF TGAPWTLMGY MIEGGGSKTM
SKAKAWLTNY PEDTKLFLIL LTDVIVDYLE MQVIAGAQML QVFESSAEHL SKEEFLLGSE
PYLRRIRDDL VDRLTKKVIP AVPLVSSYPN NIFTLLTYLI SLLIIFAKGA GHSLKEQSEL
GYDVIGLDWT VDPVEARAVV GPNITLQGNL DPQSMYCEPN ELRSLATEMV HKCGKSRYIA
NVGHGITPQT PITSMEVLVE AAHNAL