HEM21_ARATH
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 03-AUG-2022, entry version 143.
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.AT1G69740.1; -.
DR PaxDb; Q9SFH9; -.
DR PRIDE; Q9SFH9; -.
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; locus:2205035; AT1G69740.
DR eggNOG; KOG2794; Eukaryota.
DR HOGENOM; CLU_035731_1_0_1; -.
DR InParanoid; Q9SFH9; -.
DR OMA; YQMDYAN; -.
DR OrthoDB; 918089at2759; -.
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 Genevisible; Q9SFH9; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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-UniPathway.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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 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..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
