ID   HEM2_CHLMU              Reviewed;         333 AA.
AC   Q9PLU4;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase;
DE            Short=ALAD;
DE            Short=ALADH;
DE            EC=4.2.1.24;
DE   AltName: Full=Porphobilinogen synthase;
GN   Name=hemB; OrderedLocusNames=TC_0001;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
CC   -!- FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles.
CC       Binds two molecules of 5-aminolevulinate per subunit, each at a
CC       distinct site, and catalyzes their condensation to form porphobilinogen
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen;
CC         Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
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DR   EMBL; AE002160; AAF38895.1; -; Genomic_DNA.
DR   PIR; B81751; B81751.
DR   RefSeq; WP_010229069.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PLU4; -.
DR   SMR; Q9PLU4; -.
DR   STRING; 243161.TC_0001; -.
DR   EnsemblBacteria; AAF38895; AAF38895; TC_0001.
DR   GeneID; 1245524; -.
DR   KEGG; cmu:TC_0001; -.
DR   eggNOG; COG0113; Bacteria.
DR   HOGENOM; CLU_035731_0_0_0; -.
DR   OMA; YQMDYAN; -.
DR   OrthoDB; 677575at2; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR001731; ALAD.
DR   InterPro; IPR030656; ALAD_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   PANTHER; PTHR11458; PTHR11458; 1.
DR   Pfam; PF00490; ALAD; 1.
DR   PIRSF; PIRSF001415; Porphbilin_synth; 1.
DR   PRINTS; PR00144; DALDHYDRTASE.
DR   SMART; SM01004; ALAD; 1.
DR   PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE   3: Inferred from homology;
KW   Heme biosynthesis; Lyase; Magnesium; Metal-binding; Porphyrin biosynthesis.
FT   CHAIN           1..333
FT                   /note="Delta-aminolevulinic acid dehydratase"
FT                   /id="PRO_0000140495"
FT   ACT_SITE        199
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        252
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  37450 MW;  905DC8BCE50B87B5 CRC64;
     MTRLPLLKRP RRNRKSAAIR SMIRETNMVS SDLIWPIFLK EGSGIREEIP SMPGVYRWSL
     DTISRELERL CLIGLKAVIL FPVIEDQKKD QFGAYASHPY NIVCRGIQEI KKSFPQLCVI
     SDIALDPFTT SGHDGIFYNN EVLNDESVRV YGDIATLHAE MGADIVAPSD MMDGRVRHIR
     EKMDQMGFVN TGILSYSAKY ASYLYGPFRD ALSSHPQSGD KRQYQMDPAN VREALLECRL
     DEEEGADMVM IKPAGFYLDV IMKAQECTHL PVVAYQVSGE YSMIMAASLH GWLSKEGAIS
     ESLLAIKRAG ATAIISYATP WVLEWLARDA LPF