ID   HEM3_CAMJJ              Reviewed;         307 AA.
AC   A1VYQ4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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};
GN   OrderedLocusNames=CJJ81176_0570;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000538; EAQ72963.1; -; Genomic_DNA.
DR   RefSeq; WP_002820769.1; NC_008787.1.
DR   AlphaFoldDB; A1VYQ4; -.
DR   SMR; A1VYQ4; -.
DR   STRING; 354242.CJJ81176_0570; -.
DR   EnsemblBacteria; EAQ72963; EAQ72963; CJJ81176_0570.
DR   KEGG; cjj:CJJ81176_0570; -.
DR   eggNOG; COG0181; Bacteria.
DR   HOGENOM; CLU_019704_1_0_7; -.
DR   OMA; LWQANHI; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000000646; Chromosome.
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..307
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_0000304224"
FT   MOD_RES         239
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00260"
SQ   SEQUENCE   307 AA;  34037 MW;  AEF7DF1675BCE51A CRC64;
     MKLIIATRKS QLALWQSEHV AQILKNTHQI EVLLEGFKTK GDVLLDSPLA KIGGKGLFTK
     ELEESMLRKE AHLAVHSLKD VPSFFPQGLV LAAVSKREQS NDAMLSQNYK DFLSLPKGAK
     IGTTSLRRKM QLLLLRPDLD IISLRGNVNS RIEKLKNNDF DAIILAMAGI KRLNLDKQVN
     FVYEFSKDEL IPAASQGALG IESINDEKIL ELLKCLNDEN ALIETSIERE FIATLEGGCQ
     VPIGINAELL GDEICVRAVL GLPDGSEILK DKRMIKKNDF KGFGESLAKE FIAKGAKELL
     KKAESMI