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Delta-aminolevulinic acid dehydratase, chloroplastic (ALADH) (EC 4.2.1.24) (Porphobilinogen synthase) (Fragment)

 HEM2_PEA                Reviewed;         398 AA.
P30124;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
15-MAR-2017, entry version 89.
RecName: Full=Delta-aminolevulinic acid dehydratase, chloroplastic;
Short=ALADH;
EC=4.2.1.24;
AltName: Full=Porphobilinogen synthase;
Flags: Precursor; Fragment;
Name=HEMB; Synonyms=ALAD;
Pisum sativum (Garden pea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Pisum.
NCBI_TaxID=3888;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1894602;
Boese Q.F., Spano A.J., Li J., Timko M.P.;
"Aminolevulinic acid dehydratase in pea (Pisum sativum L.).
Identification of an unusual metal-binding domain in the plant
enzyme.";
J. Biol. Chem. 266:17060-17066(1991).
[2]
PROTEIN SEQUENCE OF 70-75, CATALYTIC ACTIVITY, FUNCTION, COFACTOR,
ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
PubMed=10913315; DOI=10.1021/bi000620c;
Kervinen J., Dunbrack R.L. Jr., Litwin S., Martins J., Scarrow R.C.,
Volin M., Yeung A.T., Yoon E., Jaffe E.K.;
"Porphobilinogen synthase from pea: expression from an artificial
gene, kinetic characterization, and novel implications for subunit
interactions.";
Biochemistry 39:9018-9029(2000).
-!- FUNCTION: Catalyzes an early step in the biosynthesis of
tetrapyrroles. Binds two molecules of 5-aminolevulinate per
subunit, each at a distinct site, and catalyzes their condensation
to form porphobilinogen. {ECO:0000269|PubMed:10913315}.
-!- CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2
H(2)O. {ECO:0000269|PubMed:10913315}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10913315};
Note=Binds 2 magnesium ions per monomer. The first magnesium ion
is required for catalysis. The second functions as allosteric
activator. {ECO:0000269|PubMed:10913315};
-!- ENZYME REGULATION: Activated by magnesium. Inhibited by succinyl
acetone. Enzyme activity may depend on the oligomerization state,
where the fully active octamer may dissociate and reassemble into
less active lower oligomers. {ECO:0000269|PubMed:10913315}.
-!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate:
step 1/4.
-!- SUBUNIT: Homooctamer; formed by oligomerization of dimers.
Probably forms also lower oligomers.
{ECO:0000269|PubMed:10913315}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast.
-!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
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EMBL; M71235; AAA33640.1; -; mRNA.
PIR; A40966; A40966.
ProteinModelPortal; P30124; -.
SMR; P30124; -.
BindingDB; P30124; -.
ChEMBL; CHEMBL3286082; -.
PRIDE; P30124; -.
UniPathway; UPA00251; UER00318.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC.
GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR001731; ALAD.
InterPro; IPR030656; ALAD_AS.
InterPro; IPR013785; Aldolase_TIM.
PANTHER; PTHR11458; PTHR11458; 1.
Pfam; PF00490; ALAD; 1.
PRINTS; PR00144; DALDHYDRTASE.
SMART; SM01004; ALAD; 1.
PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
1: Evidence at protein level;
Allosteric enzyme; Chlorophyll biosynthesis; Chloroplast;
Direct protein sequencing; Heme biosynthesis; Lyase; Magnesium;
Metal-binding; Plastid; Porphyrin biosynthesis; Transit peptide.
TRANSIT <1 ? Chloroplast.
CHAIN ? 398 Delta-aminolevulinic acid dehydratase,
chloroplastic.
/FTId=PRO_0000013317.
ACT_SITE 266 266 Schiff-base intermediate with substrate.
{ECO:0000250}.
ACT_SITE 319 319 Schiff-base intermediate with substrate.
{ECO:0000250}.
METAL 304 304 Magnesium. {ECO:0000250}.
BINDING 276 276 Substrate 1. {ECO:0000250}.
BINDING 288 288 Substrate 1. {ECO:0000250}.
BINDING 345 345 Substrate 2. {ECO:0000250}.
BINDING 384 384 Substrate 2. {ECO:0000250}.
NON_TER 1 1
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


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