ID   HEM3_CHLTR              Reviewed;         241 AA.
AC   O84301;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Probable 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=CT_299;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC   -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000305}.
CC   -!- CAUTION: This sequence may not function as a hydroxymethylbilane
CC       synthase because it lacks the cysteine residue necessary for attachment
CC       of the dipyrromethane cofactor. {ECO:0000305}.
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DR   EMBL; AE001273; AAC67892.1; -; Genomic_DNA.
DR   PIR; E71532; E71532.
DR   RefSeq; NP_219804.1; NC_000117.1.
DR   RefSeq; WP_009871647.1; NC_000117.1.
DR   AlphaFoldDB; O84301; -.
DR   SMR; O84301; -.
DR   STRING; 813.O172_01610; -.
DR   EnsemblBacteria; AAC67892; AAC67892; CT_299.
DR   GeneID; 884823; -.
DR   KEGG; ctr:CT_299; -.
DR   PATRIC; fig|272561.5.peg.321; -.
DR   HOGENOM; CLU_019704_2_0_0; -.
DR   InParanoid; O84301; -.
DR   OMA; CDLAIHS; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000000431; 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:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR000860; HemC.
DR   InterPro; IPR022417; Porphobilin_deaminase_N.
DR   PANTHER; PTHR11557; PTHR11557; 1.
DR   Pfam; PF01379; Porphobil_deam; 1.
DR   PRINTS; PR00151; PORPHBDMNASE.
PE   3: Inferred from homology;
KW   Porphyrin biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..241
FT                   /note="Probable porphobilinogen deaminase"
FT                   /id="PRO_0000143019"
SQ   SEQUENCE   241 AA;  26996 MW;  F89FE00C20BF7044 CRC64;
     MLSAYYNDPF LADFCLGNIP LRLASRQSSL AVLQAHECLR KLQIFFPRLW GQIITTTTQG
     DLDQETPLCA VENTGFFTDD VDFLVQSGQC DLGIHSAKDL PENPKATVVS ITASIDPRDI
     LVFHEKYLSI PLPRRLRIGS SSVRRKELLS LLYPSAIITD IRGTIQTRLK LLEEKNFDAI
     VMANAAVSRL GLRLPCTKIL PPPYHPLQGR LAITASRHIR SWRGLFLTCG ITEDVEIMCF
     S