DCUP_YEAST
ID DCUP_YEAST Reviewed; 362 AA.
AC P32347; D6VS35;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Uroporphyrinogen decarboxylase;
DE Short=UPD;
DE Short=URO-D;
DE EC=4.1.1.37;
GN Name=HEM12; Synonyms=HEM6, POP3; OrderedLocusNames=YDR047W;
GN ORFNames=YD9609.03;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1576986; DOI=10.1111/j.1432-1033.1992.tb16868.x;
RA Garey J.R., Labbe-Bois R., Chelstowska A., Rytka J., Harrison L.,
RA Kushner J., Labbe P.;
RT "Uroporphyrinogen decarboxylase in Saccharomyces cerevisiae. HEM12 gene
RT sequence and evidence for two conserved glycines essential for enzymatic
RT activity.";
RL Eur. J. Biochem. 205:1011-1016(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8346678; DOI=10.1002/yea.320090608;
RA Diflumeri C., Larocque R., Keng T.;
RT "Molecular analysis of HEM6 (HEM12) in Saccharomyces cerevisiae, the gene
RT for uroporphyrinogen decarboxylase.";
RL Yeast 9:613-623(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP MUTANTS.
RX PubMed=1471989; DOI=10.1042/bj2880753;
RA Chelstowska A., Zoadek T., Garey J.R., Kushner J., Rytka J., Labbe-Bois R.;
RT "Identification of amino acid changes affecting yeast uroporphyrinogen
RT decarboxylase activity by sequence analysis of hem12 mutant alleles.";
RL Biochem. J. 288:753-757(1992).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 -!- INTERACTION:
CC P32347; P39940: RSP5; NbExp=2; IntAct=EBI-5711, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 9220 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; X63721; CAA45253.1; -; Genomic_DNA.
DR EMBL; Z19089; CAA79514.1; -; Genomic_DNA.
DR EMBL; Z49209; CAA89078.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11895.1; -; Genomic_DNA.
DR PIR; S23471; S23471.
DR RefSeq; NP_010332.3; NM_001180355.3.
DR AlphaFoldDB; P32347; -.
DR SMR; P32347; -.
DR BioGRID; 32102; 152.
DR IntAct; P32347; 3.
DR MINT; P32347; -.
DR STRING; 4932.YDR047W; -.
DR MaxQB; P32347; -.
DR PaxDb; P32347; -.
DR PRIDE; P32347; -.
DR EnsemblFungi; YDR047W_mRNA; YDR047W; YDR047W.
DR GeneID; 851617; -.
DR KEGG; sce:YDR047W; -.
DR SGD; S000002454; HEM12.
DR VEuPathDB; FungiDB:YDR047W; -.
DR eggNOG; KOG2872; Eukaryota.
DR GeneTree; ENSGT00390000018302; -.
DR HOGENOM; CLU_040933_0_0_1; -.
DR InParanoid; P32347; -.
DR OMA; LWLMRQA; -.
DR BioCyc; YEAST:YDR047W-MON; -.
DR BRENDA; 4.1.1.37; 984.
DR Reactome; R-SCE-189451; Heme biosynthesis.
DR UniPathway; UPA00251; UER00321.
DR PRO; PR:P32347; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32347; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IDA:SGD.
DR GO; GO:0006783; P:heme biosynthetic process; IMP:SGD.
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; Heme biosynthesis; Lyase; Nucleus;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..362
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187577"
FT BINDING 30..34
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 81
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT VARIANT 59
FT /note="S -> F (in HEM12-6 and HEM12-12)"
FT VARIANT 62
FT /note="T -> I (in HEM12-14)"
FT VARIANT 107
FT /note="L -> S (in HEM12-3 and HEM12-13)"
FT VARIANT 215
FT /note="S -> N (in HEM12-2 and HEM12-11)"
FT MUTAGEN 33
FT /note="G->D: Inactivation."
FT MUTAGEN 300
FT /note="G->D: Inactivation."
SQ SEQUENCE 362 AA; 41349 MW; E9CB3A48E62BC277 CRC64;
MGNFPAPKND LILRAAKGEK VERPPCWIMR QAGRYLPEYH EVKNNRDFFQ TCRDAEIASE
ITIQPVRRYR GLIDAAIIFS DILVIPQAMG MRVEMLEGKG PHFPEPLRNP EDLQTVLDYK
VDVLKELDWA FKAITMTRIK LDGEVPLFGF CGGPWTLMVY MTEGGGSRLF RFAKQWINMY
PELSHKLLQK ITDVAVEFLS QQVVAGAQIL QVFESWGGEL SSVDFDEFSL PYLRQIAERV
PKRLQELGIM EQIPMIVFAK GSWYALDKLC CSGFDVVSLD WSWDPREAVK INKNRVTLQG
NLDPGVMYGS KEVITKKVKQ MIEAFGGGKS RYIVNFGHGT HPFMDPDVIK FFLEECHRIG
SK
