ID   HEM3_STAA8              Reviewed;         308 AA.
AC   O34090; Q2FXR1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 132.
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=SAOUHSC_01774;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9358061; DOI=10.1016/s0378-1119(97)00372-7;
RA   Kafala B., Sasarman A.;
RT   "Isolation of the Staphylococcus aureus hemCDBL gene cluster coding for
RT   early steps in heme biosynthesis.";
RL   Gene 199:231-239(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U89396; AAC45833.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD30843.1; -; Genomic_DNA.
DR   RefSeq; WP_001230228.1; NZ_LS483365.1.
DR   RefSeq; YP_500279.1; NC_007795.1.
DR   AlphaFoldDB; O34090; -.
DR   SMR; O34090; -.
DR   STRING; 1280.SAXN108_1697; -.
DR   EnsemblBacteria; ABD30843; ABD30843; SAOUHSC_01774.
DR   GeneID; 3919692; -.
DR   KEGG; sao:SAOUHSC_01774; -.
DR   PATRIC; fig|93061.5.peg.1618; -.
DR   eggNOG; COG0181; Bacteria.
DR   HOGENOM; CLU_019704_0_2_9; -.
DR   OMA; LWQANHI; -.
DR   UniPathway; UPA00251; UER00319.
DR   PRO; PR:O34090; -.
DR   Proteomes; UP000008816; 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..308
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_0000142993"
FT   MOD_RES         241
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  34354 MW;  9A109574E1A44F13 CRC64;
     MRKLVVGSRR SKLALTQSQQ FIDKLKAVEP NLEIEIKEIV TKGDRIVDKQ LSKVGGKGLF
     VKEIQHELFE KNIDMAIHSL KDVPSVIPEG LTLGCIPDRE LPFDAYISKT HTPLSQLPEG
     SIIGTSSLRR GAQILSKYPN LEIKWIRGNI DTRLEKLQTE DYDAIILAAA GLRRMGWSDD
     IVTSYLDRDT LLPAIGQGAL GIECRSDDEE LLTLLSKVHN DEVAKCVTAE RTFLAEMDGS
     CQVPIAGYAT ISDQNEIEFT GLIMTPDGKE RFEYTMNGTD PVELGKTVSN KLKEQGAYEI
     IKRLNEQH