ID   HEM3_DEBHA              Reviewed;         361 AA.
AC   Q6BM23;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Porphobilinogen deaminase;
DE            Short=PBG;
DE            EC=2.5.1.61;
DE   AltName: Full=Hydroxymethylbilane synthase;
DE            Short=HMBS;
DE   AltName: Full=Pre-uroporphyrinogen synthase;
GN   Name=HEM3; OrderedLocusNames=DEHA2F08888g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the
CC       hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=dipyrromethane; Xref=ChEBI:CHEBI:60342; Evidence={ECO:0000250};
CC       Note=Binds 1 dipyrromethane group covalently. {ECO:0000250};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC   -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC       dipyrromethan group.
CC   -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000305}.
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DR   EMBL; CR382138; CAG89089.1; -; Genomic_DNA.
DR   RefSeq; XP_460748.1; XM_460748.1.
DR   AlphaFoldDB; Q6BM23; -.
DR   SMR; Q6BM23; -.
DR   STRING; 4959.XP_460748.1; -.
DR   EnsemblFungi; CAG89089; CAG89089; DEHA2F08888g.
DR   GeneID; 2903764; -.
DR   KEGG; dha:DEHA2F08888g; -.
DR   VEuPathDB; FungiDB:DEHA2F08888g; -.
DR   eggNOG; KOG2892; Eukaryota.
DR   HOGENOM; CLU_019704_0_2_1; -.
DR   InParanoid; Q6BM23; -.
DR   OMA; NAHEWAG; -.
DR   OrthoDB; 1189095at2759; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018160; P:peptidyl-pyrromethane cofactor linkage; IEA:InterPro.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.160.40; -; 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   PANTHER; PTHR11557; PTHR11557; 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; SSF54782; SSF54782; 1.
DR   TIGRFAMs; TIGR00212; hemC; 1.
DR   PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
PE   3: Inferred from homology;
KW   Heme biosynthesis; Porphyrin biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..361
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_0000143040"
FT   REGION          341..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         265
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   361 AA;  39687 MW;  AE8DA10CCD86E621 CRC64;
     MPHNTKSMDN TLNIKDNHVQ IGGRKSKLAV VQSEIVKECI VEKFPELSCS VLALSTLGDK
     VQSKPLYSFG GKALWTKELE ILLLEQVEEY PRLDLIVHSL KDIPTNLPEE FELGCILNRE
     DARDALVMKS GSSYKSLADL PDGSLVGTSS VRRSSQLLKN HPKLRFDSVR GNLQTRLNKL
     DDENSPFECL LLASAGLIRI GLGDRITAHL DAPEMYYAVG QGALGIEIRK GDEKMLQLLK
     TIEDLPTTYC CLAERSLMRH LEGGCSVPIG VQSHYNESTN ELSLKAIIVS PDGIHFVEDE
     YKGVVNNKDD ADAIGIKVGD LLSAKGGREI LNSINFERIN LPPSSNTPTP QPITPITTNN
     S