ID   HEM2_CHLTE              Reviewed;         328 AA.
AC   Q8KCJ0;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=CT1431;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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   -!- ACTIVITY REGULATION: Stimulated by magnesium, inhibited by zinc.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Does not seem to have a metal requirement for activity.
CC   -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
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DR   EMBL; AE006470; AAM72659.1; -; Genomic_DNA.
DR   RefSeq; NP_662317.1; NC_002932.3.
DR   RefSeq; WP_010933098.1; NC_002932.3.
DR   AlphaFoldDB; Q8KCJ0; -.
DR   SMR; Q8KCJ0; -.
DR   STRING; 194439.CT1431; -.
DR   EnsemblBacteria; AAM72659; AAM72659; CT1431.
DR   KEGG; cte:CT1431; -.
DR   PATRIC; fig|194439.7.peg.1299; -.
DR   eggNOG; COG0113; Bacteria.
DR   HOGENOM; CLU_035731_0_0_10; -.
DR   OMA; YQMDYAN; -.
DR   OrthoDB; 677575at2; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000001007; 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;
KW   Reference proteome.
FT   CHAIN           1..328
FT                   /note="Delta-aminolevulinic acid dehydratase"
FT                   /id="PRO_0000140497"
FT   ACT_SITE        200
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        253
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   328 AA;  36433 MW;  55556CA0D0632148 CRC64;
     MSQLDLLNIV HRPRRLRRTA ALRNLVQENT LTVNDLVFPL FVMPGTNAVE EVPSMPGSFR
     FTIDRAVEEC KELYDLGIQA IDLFGIPEKK TEDGSEAYND NGILQQAIRA IKKAVPELCI
     MTDVALDPFT PFGHDGLVRD GIILNDETVE VLQKMAVSHA EAGADFVSPS DMMDGRIGAI
     REALDESDHS DVGILSYAAK YASSFYGPFR DALHSAPQFG DKSTYQMNPA NTDEAMKEVE
     LDIIEGADIV MVKPGLAYLD IVWRTKERFD VPVAIYHVSG EYAMVKAAAA NGWIDEERVM
     MESLLCMKRA GADIIFTYYA KEAAKKLR