ID   HEM3_ASHGO              Reviewed;         326 AA.
AC   Q75DY0;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-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=ABL107C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016815; AAS50664.1; -; Genomic_DNA.
DR   RefSeq; NP_982840.1; NM_208193.1.
DR   AlphaFoldDB; Q75DY0; -.
DR   SMR; Q75DY0; -.
DR   STRING; 33169.AAS50664; -.
DR   EnsemblFungi; AAS50664; AAS50664; AGOS_ABL107C.
DR   GeneID; 4618920; -.
DR   KEGG; ago:AGOS_ABL107C; -.
DR   eggNOG; KOG2892; Eukaryota.
DR   HOGENOM; CLU_019704_0_2_1; -.
DR   InParanoid; Q75DY0; -.
DR   OMA; NAHEWAG; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000000591; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IBA:GO_Central.
DR   GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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..326
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_0000143037"
FT   MOD_RES         251
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   326 AA;  35526 MW;  CA40F3088A161B5A CRC64;
     MGEETLRIAG RRSKLAVIQS ESVKEIVQRE FPNYTCTVLA KQTLGDQVQS KPLYAFGGKA
     LWTKELEDLL YEEDLDQRID MIVHSLKDMP TQLPEGFELG AITKRVDPSD CLVMAAGSPY
     KTLGDLPNGS VVGTSSIRRS AQLRRRYPHL VFASVRGNIQ TRLKKLDDPE NECKCIILAT
     AGLVRLGLES RITQRFDSTI MLHAVGQGAL GIETRTGDER LQAILAKVAD RNSTICCLAE
     RSLMRTLEGG CSVPIGVYST FDEETSMLTL DGLVVSVDGA DAAEATVSYK IKSDKEDAIA
     CGQLLAAKLL EAGAKKILDA IHLPEA