ID   HEM3_CORGB              Reviewed;         302 AA.
AC   A4QB59;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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}; OrderedLocusNames=cgR_0489;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(2007).
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; AP009044; BAF53456.1; -; Genomic_DNA.
DR   RefSeq; WP_003855548.1; NC_009342.1.
DR   AlphaFoldDB; A4QB59; -.
DR   SMR; A4QB59; -.
DR   EnsemblBacteria; BAF53456; BAF53456; cgR_0489.
DR   GeneID; 58311359; -.
DR   KEGG; cgt:cgR_0489; -.
DR   HOGENOM; CLU_019704_1_0_11; -.
DR   OMA; LWQANHI; -.
DR   PhylomeDB; A4QB59; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000006698; 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..302
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_0000304230"
FT   MOD_RES         234
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00260"
SQ   SEQUENCE   302 AA;  31973 MW;  E0D7F28363D94801 CRC64;
     MTLKIGTRGS KLATTQAGTI RDQLKYFGRD AELHIVTTPG DVNMSPVERI GVGVFTQALR
     DVLHAGECDV AVHSMKDLPT AADPRFHLVV PTRADSREAL IARDGLTLAE LPEGAKVGTS
     APRRISQLKA IRPDLEILPL RGNIDTRMGK VTSGELDAVM LAYAGLTRVG MQDRATEVFD
     ADIIMPAPAQ GALAIECRAD DTETVRALNM LMHADTFVSA VAERTVLNRL EAGCTAPVAA
     HATLDGYSGD TMTLTAGVYA LDGSDQLVFS AEGDGARPEE LGELVAQQLI DAGAANLLGD
     RS