ID   HEM3_RUMJO              Reviewed;         291 AA.
AC   Q59293;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2002, sequence version 2.
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   Ruminiclostridium josui (Clostridium josui).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=1499;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 25723 / FERM P-9684 / JCM 17888 / KCTC 15379 / III;
RX   PubMed=7665501; DOI=10.1128/jb.177.17.5169-5175.1995;
RA   Fujino E., Fujino T., Karita S., Sakka K., Ohmiya K.;
RT   "Cloning and sequencing of some genes responsible for porphyrin
RT   biosynthesis from the anaerobic bacterium Clostridium josui.";
RL   J. Bacteriol. 177:5169-5175(1995).
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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA05861.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D28503; BAA05861.1; ALT_INIT; Genomic_DNA.
DR   PIR; I40810; I40810.
DR   AlphaFoldDB; Q59293; -.
DR   SMR; Q59293; -.
DR   PRIDE; Q59293; -.
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..291
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_0000142926"
FT   MOD_RES         233
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   291 AA;  32252 MW;  7DEF972A4275D962 CRC64;
     MKKIRIGSRD SKLAIIQSEL IMSAIRKYDP DIELELITMK TTGDKILDKT LDKIEGKGLF
     VKELDNALYN NEVDITVHSY KDMPLEENPE LPVVALSKRE DPRDAFILPQ NGENGEPIGS
     SSLRRQLQLK ELFPGCKTAP IRGNVQTRLK KLDSGEFSAI VLAAAGIKRL GLESRIGRYF
     SVDEILPAAS QGIIAVQGRV GENFDFLKLF HSEESLCISL AERTFVREMN GGCSTPIAAY
     ATIQGSEIIL KGLYCNETTG ELRKECVSGN RNNPVELGYE LVKKMKSSKS I