ID   HEM3_CLOBK              Reviewed;         290 AA.
AC   B1IHD1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Porphobilinogen deaminase {ECO:0000255|HAMAP-Rule:MF_00260};
DE            Short=PBG {ECO:0000255|HAMAP-Rule:MF_00260};
DE            EC=2.5.1.61 {ECO:0000255|HAMAP-Rule:MF_00260};
DE   AltName: Full=Hydroxymethylbilane synthase {ECO:0000255|HAMAP-Rule:MF_00260};
DE            Short=HMBS {ECO:0000255|HAMAP-Rule:MF_00260};
DE   AltName: Full=Pre-uroporphyrinogen synthase {ECO:0000255|HAMAP-Rule:MF_00260};
GN   Name=hemC {ECO:0000255|HAMAP-Rule:MF_00260}; OrderedLocusNames=CLD_3639;
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the
CC       hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
CC       {ECO:0000255|HAMAP-Rule:MF_00260}.
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:0000255|HAMAP-Rule:MF_00260};
CC   -!- COFACTOR:
CC       Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00260};
CC       Note=Binds 1 dipyrromethane group covalently. {ECO:0000255|HAMAP-
CC       Rule:MF_00260};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC       {ECO:0000255|HAMAP-Rule:MF_00260}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00260}.
CC   -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC       dipyrromethane group. {ECO:0000255|HAMAP-Rule:MF_00260}.
CC   -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00260}.
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DR   EMBL; CP000939; ACA46545.1; -; Genomic_DNA.
DR   RefSeq; WP_003404066.1; NC_010516.1.
DR   AlphaFoldDB; B1IHD1; -.
DR   SMR; B1IHD1; -.
DR   EnsemblBacteria; ACA46545; ACA46545; CLD_3639.
DR   KEGG; cbb:CLD_3639; -.
DR   HOGENOM; CLU_019704_0_2_9; -.
DR   OMA; LWQANHI; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000008541; Chromosome.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
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; 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.
PE   3: Inferred from homology;
KW   Porphyrin biosynthesis; Transferase.
FT   CHAIN           1..290
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_1000114144"
FT   MOD_RES         237
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00260"
SQ   SEQUENCE   290 AA;  32822 MW;  C3896627EA0FC967 CRC64;
     MNFVIATRRS KLAQVQTEII IDLLNKKHDI ECEKLLIETV GDKILEVSLD KIGGKGLFVK
     DIEVAMLEQR ADAAVHSMKD VPYEMPKGFE IIAIPEREDV RDAFISLDNI KFKDLRKGAK
     IGTSSRRRAA QLKLLRPDLD IVPIRGNVQT RIEKIKKENL DGIILAVAGL KRVNLDHLIT
     DYFDTKEMVP AIGQGALGIE VMEEHPKKEL FKDLDHYNSK ICVLAERAFM RELDGDCHST
     IGAYASIKDN IMHIIGIFER KNKIIKKEIT GTKDQYEKLG IALAEHILKD