ID   HEM2_SPIOL              Reviewed;         433 AA.
AC   P24493;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 103.
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=ALA1;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 57-70.
RC   STRAIN=cv. Aestivato;
RX   PubMed=1351729; DOI=10.1515/znc-1992-1-214;
RA   Schaumburg A., Schneider-Poetsch H.A.W., Eckerskorn C.;
RT   "Characterization of plastid 5-aminolevulinate dehydratase (ALAD; EC
RT   4.2.1.24) from spinach (Spinacia oleracea L.) by sequencing and comparison
RT   with non-plant ALAD enzymes.";
RL   Z. Naturforsch. C 47:77-84(1992).
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; X57842; CAA40974.1; -; mRNA.
DR   PIR; A50000; A50000.
DR   AlphaFoldDB; P24493; -.
DR   SMR; P24493; -.
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   1: Evidence at protein level;
KW   Allosteric enzyme; Chlorophyll biosynthesis; Chloroplast;
KW   Direct protein sequencing; Heme biosynthesis; Lyase; Magnesium;
KW   Metal-binding; Plastid; Porphyrin biosynthesis; Transit peptide.
FT   TRANSIT         1..56
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:1351729"
FT   CHAIN           57..433
FT                   /note="Delta-aminolevulinic acid dehydratase,
FT                   chloroplastic"
FT                   /id="PRO_0000013321"
FT   REGION          83..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..99
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        301
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        354
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         323
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         380
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         419
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   433 AA;  47322 MW;  4B02E3EFC4BBE131 CRC64;
     MASTFNIPCN AGTIKNFNNS QRNLGFSSNL GINFAKTRFS NCGDSGRIPS QLVVRASERR
     DNLTQQKTGL SIEECEAAVV AGNAPSAPPV PPTPKAPSGT PSVSPLSLGR RPRRNRTSPV
     FRAAFQETTL SPANVVYPLF IHEGEEDTPI GAMPGCYRLG WRHGLVEEVA KARDVVVNSI
     VVFPKPDALK SPTGDEAYNE NGLVPRTIRM LKDKFPDLII YTDVALDPYY YDGHDGIVTQ
     HGVIMNDETV HQLCKQAVAQ ARAGADVVSP SDMMDGRVGA IRAALDAEGY SNVSIMSYTA
     KYASSFYGPF REALDSNPRF GDKKTYQMNP ANYREALIET QEDESEGADI LLVKPGLPYL
     DIIRLLRDNS DLPIAAYQVS GEYSMIKAGG VLKMIDEEKV MLESLLCLRR AGADIILTYF
     ALQAARCLCG EKR