ID   HEM2_SELMA              Reviewed;         417 AA.
AC   P45623;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase, chloroplastic;
DE            Short=ALAD;
DE            Short=ALADH;
DE            EC=4.2.1.24;
DE   AltName: Full=Porphobilinogen synthase;
DE   Flags: Precursor;
GN   Name=HEMB; Synonyms=ALA2;
OS   Selaginella martensii (Martens's spike moss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=3247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sollbach M., Schneider-Poetsch H.A.W.;
RL   Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per monomer. The first magnesium ion is
CC       required for catalysis. The second functions as allosteric activator.
CC       {ECO:0000250};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
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DR   EMBL; X75043; CAA52955.1; -; Genomic_DNA.
DR   AlphaFoldDB; P45623; -.
DR   SMR; P45623; -.
DR   PRIDE; P45623; -.
DR   UniPathway; UPA00251; UER00318.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
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   PRINTS; PR00144; DALDHYDRTASE.
DR   SMART; SM01004; ALAD; 1.
DR   PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Chlorophyll biosynthesis; Chloroplast;
KW   Heme biosynthesis; Lyase; Magnesium; Metal-binding; Plastid;
KW   Porphyrin biosynthesis; Transit peptide.
FT   TRANSIT         1..40
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..417
FT                   /note="Delta-aminolevulinic acid dehydratase,
FT                   chloroplastic"
FT                   /id="PRO_0000013319"
FT   REGION          63..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        286
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        339
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         365
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         404
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   417 AA;  45182 MW;  036E57A607886759 CRC64;
     MAALLVPGGG AAPGLVWRRR RAAVQCAAAS PSSPDPSWRT NVVSDRVSVE PSPRTIHECE
     ADVVSGNPPA APAAPAKAKA PPGTPVVKPL RLTSRPRRNR KSAALRDAFQ ETTLTPANFI
     LPLFIHEGEE DSPIGAMPGC SRLGWRHGLI DEVYKARDVG VNSVVLFPKI PDALKSSTGD
     EAYNPDGLVP RAIRTLKDKF PDLVIYTDVA LDPYSSDGHD GIVREDGVIM NDETVHQLCK
     QAVAQAEAGA DVVSPSDMMD GRVGAIRTAL DEAGYYHVSI MAYTAKYASA FYEPFREELD
     SNPRFGDKKT YQMNPENYRE ALLEVHADES EGADILMVKP AMPYLHVIRL LRDTSALPIS
     AYQVSGEYSM IKAAASQGML DEKKAILESL LCIKRAGADV ILTYAALQAA RWLCGEK