ID   HEM3_HELPY              Reviewed;         306 AA.
AC   P56140;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 124.
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=HP_0237;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; AE000511; AAD07304.1; -; Genomic_DNA.
DR   PIR; E64549; E64549.
DR   RefSeq; NP_207035.1; NC_000915.1.
DR   RefSeq; WP_000527585.1; NC_018939.1.
DR   AlphaFoldDB; P56140; -.
DR   SMR; P56140; -.
DR   STRING; 85962.C694_01195; -.
DR   PaxDb; P56140; -.
DR   EnsemblBacteria; AAD07304; AAD07304; HP_0237.
DR   KEGG; hpy:HP_0237; -.
DR   PATRIC; fig|85962.47.peg.256; -.
DR   eggNOG; COG0181; Bacteria.
DR   OMA; LWQANHI; -.
DR   PhylomeDB; P56140; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IBA:GO_Central.
DR   GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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..306
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_0000142945"
FT   MOD_RES         239
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   306 AA;  33940 MW;  583F9944464A8B46 CRC64;
     MGNLVIGSRG SELALWQANH IKERLKKECL IESEIQIVKT KGDKILDTPL NKIGGKGLFT
     KELEELLLKG AIDLAVHSLK DVPVVFEKGL DLACITKRAD VRDTFLSVKF PDLMSLPKGA
     KVGTTSLRRS MQIKLKRQDL DTESLRGNVQ TRLKKLECGE FDAIILAEAG LCRLEIQGAK
     YRKAFSVEEM IPSMGQGALG VEMLKNHKHF ATLQKLNDEK SAFCCRLERE FIKGLNGGCQ
     IPIGVHASLM GDRVKIQAVL GLPNGKEVIT KEKQGDKTKA FDLVQELLEE FLQSGAKEIL
     EKAQLF