ID   HEM3_YEAST              Reviewed;         327 AA.
AC   P28789; D6VRE9; Q2VQW9;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Porphobilinogen deaminase;
DE            Short=PBG;
DE            EC=2.5.1.61 {ECO:0000305|PubMed:1508149};
DE   AltName: Full=Hydroxymethylbilane synthase;
DE            Short=HMBS;
DE   AltName: Full=Pre-uroporphyrinogen synthase;
GN   Name=HEM3; OrderedLocusNames=YDL205C; ORFNames=D1057;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=1508149; DOI=10.1007/bf00283844;
RA   Keng T., Richard C., Larocque R.;
RT   "Structure and regulation of yeast HEM3, the gene for porphobilinogen
RT   deaminase.";
RL   Mol. Gen. Genet. 234:233-243(1992).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-97.
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=15905473; DOI=10.1093/nar/gki583;
RA   Zhang Z., Dietrich F.S.;
RT   "Mapping of transcription start sites in Saccharomyces cerevisiae using 5'
RT   SAGE.";
RL   Nucleic Acids Res. 33:2838-2851(2005).
RN   [5]
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   [6]
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 tetrapolymerization of the monopyrrole
CC       porphobilinogen (PBG) into the hydroxymethylbilane pre-uroporphyrinogen
CC       in several discrete steps. {ECO:0000305|PubMed:1508149}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+);
CC         Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61;
CC         Evidence={ECO:0000305|PubMed:1508149};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13186;
CC         Evidence={ECO:0000305|PubMed:1508149};
CC   -!- COFACTOR:
CC       Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC       Note=Binds 1 dipyrromethane group covalently.
CC       {ECO:0000305|PubMed:1508149};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC       {ECO:0000305|PubMed:1508149}.
CC   -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC       dipyrromethane group. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 8480 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000305}.
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DR   EMBL; Z11745; CAA77804.1; -; Genomic_DNA.
DR   EMBL; X99000; CAA67486.1; -; Genomic_DNA.
DR   EMBL; Z74253; CAA98783.1; -; Genomic_DNA.
DR   EMBL; AY899249; AAX83934.1; -; mRNA.
DR   EMBL; BK006938; DAA11659.1; -; Genomic_DNA.
DR   PIR; S25071; S25071.
DR   RefSeq; NP_010076.1; NM_001180265.1.
DR   AlphaFoldDB; P28789; -.
DR   SMR; P28789; -.
DR   BioGRID; 31841; 21.
DR   STRING; 4932.YDL205C; -.
DR   iPTMnet; P28789; -.
DR   MaxQB; P28789; -.
DR   PaxDb; 4932-YDL205C; -.
DR   PeptideAtlas; P28789; -.
DR   EnsemblFungi; YDL205C_mRNA; YDL205C; YDL205C.
DR   GeneID; 851322; -.
DR   KEGG; sce:YDL205C; -.
DR   AGR; SGD:S000002364; -.
DR   SGD; S000002364; HEM3.
DR   VEuPathDB; FungiDB:YDL205C; -.
DR   eggNOG; KOG2892; Eukaryota.
DR   GeneTree; ENSGT00390000009083; -.
DR   HOGENOM; CLU_019704_0_2_1; -.
DR   InParanoid; P28789; -.
DR   OMA; NAHEWAG; -.
DR   OrthoDB; 788at2759; -.
DR   BioCyc; YEAST:YDL205C-MONOMER; -.
DR   Reactome; R-SCE-189451; Heme biosynthesis.
DR   UniPathway; UPA00251; UER00319.
DR   BioGRID-ORCS; 851322; 8 hits in 10 CRISPR screens.
DR   PRO; PR:P28789; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P28789; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IMP: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; cd13645; PBP2_HuPBGD_like; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   Gene3D; 3.30.160.40; Porphobilinogen deaminase, C-terminal domain; 1.
DR   InterPro; IPR000860; HemC.
DR   InterPro; IPR022419; Porphobilin_deaminase_cofac_BS.
DR   InterPro; IPR022417; Porphobilin_deaminase_N.
DR   InterPro; IPR022418; Porphobilinogen_deaminase_C.
DR   InterPro; IPR036803; Porphobilinogen_deaminase_C_sf.
DR   NCBIfam; TIGR00212; hemC; 1.
DR   PANTHER; PTHR11557; PORPHOBILINOGEN DEAMINASE; 1.
DR   PANTHER; PTHR11557:SF0; PORPHOBILINOGEN DEAMINASE; 1.
DR   Pfam; PF01379; Porphobil_deam; 1.
DR   Pfam; PF03900; Porphobil_deamC; 1.
DR   PIRSF; PIRSF001438; 4pyrrol_synth_OHMeBilane_synth; 1.
DR   PRINTS; PR00151; PORPHBDMNASE.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   SUPFAM; SSF54782; Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain; 1.
DR   PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
PE   1: Evidence at protein level;
KW   Heme biosynthesis; Porphyrin biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..327
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_0000143045"
FT   MOD_RES         251
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   327 AA;  36675 MW;  1D22FF3B131ECE73 CRC64;
     MGPETLHIGG RKSKLAVIQS NHVLKLIEEK YPDYDCKVFT LQTLGDQIQF KPLYSFGGKA
     LWTKELEDHL YHDDPSKKLD LIVHSLKDMP TLLPEGFELG GITKRVDPTD CLVMPFYSAY
     KSLDDLPDGG IVGTSSVRRS AQLKRKYPHL KFESVRGNIQ TRLQKLDDPK SPYQCIILAS
     AGLMRMGLEN RITQRFHSDT MYHAVGQGAL GIEIRKGDTK MMKILDEICD LNATICCLSE
     RALMRTLEGG CSVPIGVESK YNEETKKLLL KAIVVDVEGT EAVEDEIEML IENVKEDSMA
     CGKILAERMI ADGAKKILDE INLDRIK
//