ID   HEM3_MYCLE              Reviewed;         315 AA.
AC   Q49808; Q49818; Q9CB59;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 126.
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=ML2421; ORFNames=B2168_C1_179, B2168_C3_262;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17244.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAC31937.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U00018; AAA17223.1; -; Genomic_DNA.
DR   EMBL; U00018; AAA17244.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL583925; CAC31937.1; ALT_INIT; Genomic_DNA.
DR   PIR; A87212; A87212.
DR   PIR; S72887; S72887.
DR   PIR; S72908; S72908.
DR   RefSeq; WP_041323398.1; NC_002677.1.
DR   AlphaFoldDB; Q49808; -.
DR   SMR; Q49808; -.
DR   STRING; 272631.ML2421; -.
DR   EnsemblBacteria; CAC31937; CAC31937; CAC31937.
DR   KEGG; mle:ML2421; -.
DR   Leproma; ML2421; -.
DR   eggNOG; COG0181; Bacteria.
DR   HOGENOM; CLU_019704_1_0_11; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000000806; 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..315
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_0000142958"
FT   MOD_RES         234
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        169
FT                   /note="L -> P (in Ref. 1; AAA17223)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   315 AA;  32523 MW;  64685F2D970D3882 CRC64;
     MIRIGTRGSL LATTQAALVR DALIANGHPA ELVIVNTAGD QSSASIDSLG VGVFTTALRA
     AIEEGCVDAA VHSYKDLPTA DDPRFTVAAI PPRNDPRDAV VTRDELVLAE LPAGSLVGTS
     SPRRAAQLRA LGLGLEIRPL RGNLDTRLNR VSSGDLDAIV VARAGLARLG RLDEVTETLD
     PVQMVPAPAQ GAIAVECRAG DSRLVAVLAA LDDADTRAAV TAERVLLAEL EAGCSAPVGA
     IAQVVESIDG EGRVFEELSL RGCVAALDGS DVIRASGIST SGRASELGLA VAVELFELGA
     RELMWGARSD RARGS