ID   HEM3_CAMJE              Reviewed;         307 AA.
AC   Q9PHW9; O32364; Q0PAX1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
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; OrderedLocusNames=Cj0545;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-286.
RC   STRAIN=ATCC 700819 / NCTC 11168;
RA   Karlyshev A.V., Wren B.W.;
RT   "Cloning and characterisation of C. jejuni hemC gene.";
RL   Submitted (SEP-1997) 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: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}.
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DR   EMBL; AL111168; CAL34691.1; -; Genomic_DNA.
DR   EMBL; AJ000752; CAA04300.1; -; Genomic_DNA.
DR   PIR; A81401; A81401.
DR   RefSeq; WP_002856753.1; NC_002163.1.
DR   RefSeq; YP_002343976.1; NC_002163.1.
DR   AlphaFoldDB; Q9PHW9; -.
DR   SMR; Q9PHW9; -.
DR   IntAct; Q9PHW9; 2.
DR   STRING; 192222.Cj0545; -.
DR   PaxDb; Q9PHW9; -.
DR   PRIDE; Q9PHW9; -.
DR   EnsemblBacteria; CAL34691; CAL34691; Cj0545.
DR   GeneID; 904871; -.
DR   KEGG; cje:Cj0545; -.
DR   PATRIC; fig|192222.6.peg.537; -.
DR   eggNOG; COG0181; Bacteria.
DR   HOGENOM; CLU_019704_1_0_7; -.
DR   OMA; LWQANHI; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000000799; 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; Reference proteome; Transferase.
FT   CHAIN           1..307
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_0000142919"
FT   MOD_RES         239
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        205
FT                   /note="N -> H (in Ref. 2; CAA04300)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   307 AA;  34051 MW;  2518F72360BDB45F CRC64;
     MKLIIATRKS QLALWQSEHV AQILKNTHQI EVLLEGFKTK GDVLLDSPLA KIGGKGLFTK
     ELEESMLRKE AHLAVHSLKD VPSFFPQGLV LAAVSKREQS NDAMLSQNYK DFLSLPKGAK
     IGTTSLRRKM QLLLLRPDLE IISLRGNVNS RIEKLKNNDF DAIILAMAGI KRLNLDKQVN
     FVYEFSKDEL IPAASQGALG IESINDEKIL ELLKCLNDEN ALIETSIERE FIATLEGGCQ
     VPIGINAELL GDEICVRAVL GLPDGSEILK DKRMIKKNDF KGFGESLAKE FIAKGAKELL
     KKAESMI