ID   HEM21_ARATH             Reviewed;         430 AA.
AC   Q9SFH9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase 1, chloroplastic;
DE            Short=ALADH1;
DE            EC=4.2.1.24;
DE   AltName: Full=Porphobilinogen synthase;
DE   Flags: Precursor;
GN   Name=HEMB1; OrderedLocusNames=At1g69740; ORFNames=T6C23.6;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   INDUCTION BY FHY3 AND FAR1, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=22634759; DOI=10.1105/tpc.112.097022;
RA   Tang W., Wang W., Chen D., Ji Q., Jing Y., Wang H., Lin R.;
RT   "Transposase-derived proteins FHY3/FAR1 interact with PHYTOCHROME-
RT   INTERACTING FACTOR1 to regulate chlorophyll biosynthesis by modulating
RT   HEMB1 during deetiolation in Arabidopsis.";
RL   Plant Cell 24:1984-2000(2012).
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   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in cotyledons during dark-to-light
CC       transition. {ECO:0000269|PubMed:22634759}.
CC   -!- INDUCTION: Up-regulated by the transcription factors FAR1 and FHY3.
CC       {ECO:0000269|PubMed:22634759}.
CC   -!- DISRUPTION PHENOTYPE: Embryo lethal when homozygous. Impaired plant
CC       growth and development. {ECO:0000269|PubMed:22634759}.
CC   -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
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DR   EMBL; AC013289; AAG52549.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34969.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34970.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM58523.1; -; Genomic_DNA.
DR   EMBL; AF327428; AAG42018.1; -; mRNA.
DR   EMBL; AF361803; AAK32816.1; -; mRNA.
DR   EMBL; AY059154; AAL15379.1; -; mRNA.
DR   EMBL; AY081254; AAL91143.1; -; mRNA.
DR   EMBL; AY113941; AAM44989.1; -; mRNA.
DR   EMBL; AY120705; AAM53263.1; -; mRNA.
DR   EMBL; AY128711; AAM91111.1; -; mRNA.
DR   PIR; D96719; D96719.
DR   RefSeq; NP_001077800.1; NM_001084331.3.
DR   RefSeq; NP_001320950.1; NM_001334421.1.
DR   RefSeq; NP_177132.1; NM_105642.4.
DR   AlphaFoldDB; Q9SFH9; -.
DR   SMR; Q9SFH9; -.
DR   BioGRID; 28531; 2.
DR   STRING; 3702.Q9SFH9; -.
DR   iPTMnet; Q9SFH9; -.
DR   PaxDb; 3702-AT1G69740-1; -.
DR   ProteomicsDB; 228741; -.
DR   EnsemblPlants; AT1G69740.1; AT1G69740.1; AT1G69740.
DR   EnsemblPlants; AT1G69740.2; AT1G69740.2; AT1G69740.
DR   EnsemblPlants; AT1G69740.3; AT1G69740.3; AT1G69740.
DR   GeneID; 843310; -.
DR   Gramene; AT1G69740.1; AT1G69740.1; AT1G69740.
DR   Gramene; AT1G69740.2; AT1G69740.2; AT1G69740.
DR   Gramene; AT1G69740.3; AT1G69740.3; AT1G69740.
DR   KEGG; ath:AT1G69740; -.
DR   Araport; AT1G69740; -.
DR   TAIR; AT1G69740; HEMB1.
DR   eggNOG; KOG2794; Eukaryota.
DR   HOGENOM; CLU_035731_1_0_1; -.
DR   InParanoid; Q9SFH9; -.
DR   OMA; YQMDYAN; -.
DR   OrthoDB; 2782182at2759; -.
DR   PhylomeDB; Q9SFH9; -.
DR   UniPathway; UPA00251; UER00318.
DR   UniPathway; UPA00668; -.
DR   PRO; PR:Q9SFH9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SFH9; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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-UniPathway.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; TAS:TAIR.
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.
DR   Genevisible; Q9SFH9; AT.
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..52
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           53..430
FT                   /note="Delta-aminolevulinic acid dehydratase 1,
FT                   chloroplastic"
FT                   /id="PRO_0000013314"
FT   REGION          82..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        298
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        351
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         336
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         377
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         416
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   430 AA;  46690 MW;  44B0984247FC6147 CRC64;
     MATTPIFNAS CSFPSTRGID CKSYIGLRSN VSKVSVASSR IATSQRRNLV VRASESGNGH
     AKKLGMSDAE CEAAVAAGNV PEAPPVPPKP AAPVGTPIIK PLNLSRRPRR NRASPVTRAA
     FQETDISPAN FVYPLFIHEG EEDTPIGAMP GCYRLGWRHG LVQEVAKARA VGVNSIVLFP
     KVPEALKNST GDEAYNDNGL VPRTIRLLKD KYPDLIIYTD VALDPYSSDG HDGIVREDGV
     IMNDETVHQL CKQAVSQARA GADVVSPSDM MDGRVGAIRS ALDAEGFQNV SIMSYTAKYA
     SSFYGPFREA LDSNPRFGDK KTYQMNPANY REALIEARED EAEGADILLV KPGLPYLDII
     RLLRDKSPLP IAAYQVSGEY SMIKAGGVLK MIDEEKVMME SLMCLRRAGA DIILTYFALQ
     AATCLCGEKR
//