HEM2_PEA
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 03-AUG-2022, entry version 98.
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).
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 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..?
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
