ID   HEM2_PEA                Reviewed;         398 AA.
AC   P30124;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   24-JAN-2024, entry version 101.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase, chloroplastic;
DE            Short=ALADH;
DE            EC=4.2.1.24;
DE   AltName: Full=Porphobilinogen synthase;
DE   Flags: Precursor; Fragment;
GN   Name=HEMB; Synonyms=ALAD;
OS   Pisum sativum (Garden pea) (Lathyrus oleraceus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1894602; DOI=10.1016/s0021-9258(19)47339-0;
RA   Boese Q.F., Spano A.J., Li J., Timko M.P.;
RT   "Aminolevulinic acid dehydratase in pea (Pisum sativum L.). Identification
RT   of an unusual metal-binding domain in the plant enzyme.";
RL   J. Biol. Chem. 266:17060-17066(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 70-75, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ACTIVITY
RP   REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX   PubMed=10913315; DOI=10.1021/bi000620c;
RA   Kervinen J., Dunbrack R.L. Jr., Litwin S., Martins J., Scarrow R.C.,
RA   Volin M., Yeung A.T., Yoon E., Jaffe E.K.;
RT   "Porphobilinogen synthase from pea: expression from an artificial gene,
RT   kinetic characterization, and novel implications for subunit
RT   interactions.";
RL   Biochemistry 39:9018-9029(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
CC       porphobilinogen. {ECO:0000269|PubMed:10913315}.
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         Evidence={ECO:0000269|PubMed:10913315};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:10913315};
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:0000269|PubMed:10913315};
CC   -!- ACTIVITY REGULATION: Activated by magnesium. Inhibited by succinyl
CC       acetone. Enzyme activity may depend on the oligomerization state, where
CC       the fully active octamer may dissociate and reassemble into less active
CC       lower oligomers. {ECO:0000269|PubMed:10913315}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC   -!- SUBUNIT: Homooctamer; formed by oligomerization of dimers. Probably
CC       forms also lower oligomers. {ECO:0000269|PubMed:10913315}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
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DR   EMBL; M71235; AAA33640.1; -; mRNA.
DR   PIR; A40966; A40966.
DR   AlphaFoldDB; P30124; -.
DR   SMR; P30124; -.
DR   BindingDB; P30124; -.
DR   ChEMBL; CHEMBL3286082; -.
DR   EnsemblPlants; Psat5g087720.1; Psat5g087720.1.cds; Psat5g087720.
DR   EnsemblPlants; Psat5g087760.1; Psat5g087760.1.cds1; Psat5g087760.
DR   Gramene; Psat5g087720.1; Psat5g087720.1.cds; Psat5g087720.
DR   Gramene; Psat5g087760.1; Psat5g087760.1.cds1; Psat5g087760.
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   CDD; cd04823; ALAD_PBGS_aspartate_rich; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR001731; ALAD.
DR   InterPro; IPR030656; ALAD_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   PANTHER; PTHR11458; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR   PANTHER; PTHR11458:SF0; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR   Pfam; PF00490; ALAD; 1.
DR   PRINTS; PR00144; DALDHYDRTASE.
DR   SMART; SM01004; ALAD; 1.
DR   SUPFAM; SSF51569; Aldolase; 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..?
FT                   /note="Chloroplast"
FT   CHAIN           ?..398
FT                   /note="Delta-aminolevulinic acid dehydratase,
FT                   chloroplastic"
FT                   /id="PRO_0000013317"
FT   REGION          48..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..65
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        266
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        319
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         384
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   398 AA;  43815 MW;  75DDCB55CE3C6BD1 CRC64;
     HTFVDLKSPF TLSNYLSFSS SKRRQPPSLF TVRASDSDFE AAVVAGKVPE APPVPPTPAS
     PAGTPVVPSL PIQRRPRRNR RSPALRSAFQ ETTLSPANFV YPLFIHEGEE DTPIGAMPGC
     YRLGWRHGLL EEVAKARDVG VNSVVLFPKI PDALKTPTGD EAYNEDGLVP RSIRLLKDKY
     PDLIIYTDVA LDPYSSDGHD GIVREDGVIM NDETVHQLCK QAVAQARAGA DVVSPSDMMD
     GRVGAMRVAL DAEGFQHVSI MSYTAKYASS FYGPFREALD SNPRFGDKKT YQMNPANYRE
     ALTEMREDES EGADILLVKP GLPYLDIIRL LRDNSPLPIA AYQVSGEYSM IKAGGALKMI
     DEEKVMMESL LCLRRAGADI ILTYFALQAA RTLCGEKR
//