HEM2_SOYBN
ID HEM2_SOYBN Reviewed; 412 AA.
AC P43210;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 111.
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;
GN Name=HEMB; Synonyms=ALAD;
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=8016269; DOI=10.1104/pp.104.4.1411;
RA Kaczor C.M., Smith M.W., Sangwan I., O'Brian M.R.;
RT "Plant delta-aminolevulinic acid dehydratase. Expression in soybean root
RT nodules and evidence for a bacterial lineage of the Alad gene.";
RL Plant Physiol. 104:1411-1417(1994).
CC -!- FUNCTION: Is committed to plant tetrapyrrole synthesis.
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 -!- TISSUE SPECIFICITY: Leaves and root nodules.
CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
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DR EMBL; U04525; AAA18342.1; -; mRNA.
DR PIR; T06351; T06351.
DR RefSeq; NP_001238737.1; NM_001251808.1.
DR AlphaFoldDB; P43210; -.
DR SMR; P43210; -.
DR STRING; 3847.GLYMA06G12110.1; -.
DR PRIDE; P43210; -.
DR ProMEX; P43210; -.
DR GeneID; 548095; -.
DR KEGG; gmx:548095; -.
DR eggNOG; KOG2794; Eukaryota.
DR InParanoid; P43210; -.
DR OrthoDB; 918089at2759; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004655; F:porphobilinogen synthase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Allosteric enzyme; Chlorophyll biosynthesis; Chloroplast;
KW Heme biosynthesis; Lyase; Magnesium; Metal-binding; Plastid;
KW Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..412
FT /note="Delta-aminolevulinic acid dehydratase,
FT chloroplastic"
FT /id="PRO_0000013320"
FT REGION 68..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 280
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT ACT_SITE 333
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 412 AA; 45068 MW; 0ECDF209A09572D8 CRC64;
MASSIPNAPS AFNSQSYVGL RAPLRTFNFS SPQAAKIPRS QRLFVVRASD SEFEAAVVAG
KVPPAPPVRP RPAAPVGTPV VPSLPLHRRP RRNRKSPALR SAFQETSISP ANFVYPLFIH
EGEEDTPIGA MPGCYRLGWR HGLVEEVAKA RDVGVNSVVL FPKIPDALKS PTGDEAYNEN
GLVPRTIRLL KDKYPDLVIY TDVALDPYSS DGHDGIVRED GVIMNDETVH QLCKQAVAQA
QAGADVVSPS DMMDGRVGAL RAALDAEGFQ HVSIMSYTAK YASSFYGPFR EALDSNPRFG
DKKTYQMNPA NYREALTEMR EDESEGADIL LVKPGLPYLD IIRLLRDNSP LPIAAYQVSG
EYAMIKAAGA LKMIDEEKVM MESLMCLRRA GADIILTYSA LQAARCLCGE KR
