DCUP_DROME
ID DCUP_DROME Reviewed; 356 AA.
AC Q9V595;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Uroporphyrinogen decarboxylase;
DE Short=UPD;
DE Short=URO-D;
DE EC=4.1.1.37;
GN Name=Urod {ECO:0000312|FlyBase:FBgn0033428};
GN Synonyms=Updo {ECO:0000312|FlyBase:FBgn0033428};
GN ORFNames=CG1818 {ECO:0000312|FlyBase:FBgn0033428};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
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; AE013599; AAF58922.1; -; Genomic_DNA.
DR RefSeq; NP_610501.1; NM_136657.3.
DR AlphaFoldDB; Q9V595; -.
DR SMR; Q9V595; -.
DR BioGRID; 61817; 2.
DR DIP; DIP-21696N; -.
DR IntAct; Q9V595; 1.
DR STRING; 7227.FBpp0113059; -.
DR PaxDb; Q9V595; -.
DR PRIDE; Q9V595; -.
DR DNASU; 35986; -.
DR EnsemblMetazoa; FBtr0088524; FBpp0087607; FBgn0033428.
DR GeneID; 35986; -.
DR KEGG; dme:Dmel_CG1818; -.
DR UCSC; CG1818-RA; d. melanogaster.
DR CTD; 7389; -.
DR FlyBase; FBgn0033428; Urod.
DR VEuPathDB; VectorBase:FBgn0033428; -.
DR eggNOG; KOG2872; Eukaryota.
DR GeneTree; ENSGT00390000018302; -.
DR HOGENOM; CLU_040933_0_0_1; -.
DR InParanoid; Q9V595; -.
DR OMA; LWLMRQA; -.
DR OrthoDB; 1114675at2759; -.
DR PhylomeDB; Q9V595; -.
DR Reactome; R-DME-189451; Heme biosynthesis.
DR SignaLink; Q9V595; -.
DR UniPathway; UPA00251; UER00321.
DR BioGRID-ORCS; 35986; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35986; -.
DR PRO; PR:Q9V595; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033428; Expressed in eye disc (Drosophila) and 33 other tissues.
DR ExpressionAtlas; Q9V595; baseline and differential.
DR Genevisible; Q9V595; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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;
KW Reference proteome.
FT CHAIN 1..356
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187573"
FT BINDING 33..37
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 82
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 356 AA; 39988 MW; 75E2B3AEFD59DBFD CRC64;
MKDAKPFPVL KNDNLLRAAR GEVVDRVPVW VMRQAGRYLP EFQELRKHHD FFTVCRTPEL
ACEVTMQPLR RFDLDASIIF SDILVIPQAL GLTVEMHAGV GPVLPQPIVV PEDLKRLTPD
GALSRLSYVG DAITMMRHKL EGRVPLIGFT GAPWTLMGYM IEGGGSKTMS KAKAWLNEHP
EDSKLFLNLL TDAIVDYLEM QVKAGAQMLQ VFESSAEHLS KEQFLQWCVP YLKRIRDELV
DRLTKKAIPV VPMTLFAKGA GHSLKEQSEL GYDVIGLDWT VDPLEARNLV GPNITLQGNL
DPQDMYRDPD ELRNLTTEMV HKFGKSRYIA NLGHGITPQT PITSMEVLVE AVHKAL
