ID   HEM3_PROMI              Reviewed;         313 AA.
AC   Q59684;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=hemC;
OS   Proteus mirabilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=584;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8874804; DOI=10.1016/0300-9084(96)82192-4;
RA   Trotot P., Sismeiro O., Vivares C., Glaser P., Bresson-Roy A., Danchin A.;
RT   "Comparative analysis of the cya locus in enterobacteria and related Gram-
RT   negative facultative anaerobes.";
RL   Biochimie 78:277-287(1996).
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;
CC       Note=Binds 1 dipyrromethane group covalently.;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC       dipyrromethane group. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000305}.
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DR   EMBL; U22969; AAC44329.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59684; -.
DR   SMR; Q59684; -.
DR   STRING; 584.AOUC001_17905; -.
DR   UniPathway; UPA00251; UER00319.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00260; Porphobil_deam; 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   Porphyrin biosynthesis; Transferase.
FT   CHAIN           1..313
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_0000142971"
FT   MOD_RES         242
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   313 AA;  33912 MW;  9EA90FA04BD3CD65 CRC64;
     MPKSTIRIAT RQSPLAMWQA LYVKEQLQIA HPSLVVELVP MVTKGDIILD TPLAKVGGKG
     LFVKELELAL LSSRADIAVH SMKDVPIDFP EGLGLVTICE REDPRDAFVS NHYDSLEQLP
     AGSVVGTSSL RRQCQLKALR PDLIIRDLRG NVGTRLSKLD NGDYDAIILA VAGLKRLKLT
     ERIRSSLSAE QSLPAVGQGA VGIECRLDDH DTQALLAALN HADTATCVKA ERAMNTRLEG
     GCQVPIGSYA IWQNDKIWLR ALVGAPDGKT ILRGERLVSP EDAEQAGISL AEELLDKGAR
     EILTAVYQGN TAI