HEM22_ARATH
ID HEM22_ARATH Reviewed; 406 AA.
AC Q94LA4;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable delta-aminolevulinic acid dehydratase 2, chloroplastic;
DE Short=ALADH2;
DE EC=4.2.1.24;
DE AltName: Full=Porphobilinogen synthase;
DE Flags: Precursor;
GN Name=HEMB2; OrderedLocusNames=At1g44318; ORFNames=T18F15.10;
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).
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 an allosteric
CC activator. {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 -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC084807; AAK43479.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32031.1; -; Genomic_DNA.
DR RefSeq; NP_175085.1; NM_103545.2.
DR AlphaFoldDB; Q94LA4; -.
DR SMR; Q94LA4; -.
DR STRING; 3702.AT1G44318.1; -.
DR PaxDb; Q94LA4; -.
DR PRIDE; Q94LA4; -.
DR ProMEX; Q94LA4; -.
DR ProteomicsDB; 232213; -.
DR EnsemblPlants; AT1G44318.1; AT1G44318.1; AT1G44318.
DR GeneID; 841025; -.
DR Gramene; AT1G44318.1; AT1G44318.1; AT1G44318.
DR KEGG; ath:AT1G44318; -.
DR Araport; AT1G44318; -.
DR TAIR; locus:2823624; AT1G44318.
DR eggNOG; KOG2794; Eukaryota.
DR HOGENOM; CLU_035731_1_0_1; -.
DR InParanoid; Q94LA4; -.
DR OMA; GFEQKSY; -.
DR OrthoDB; 918089at2759; -.
DR PhylomeDB; Q94LA4; -.
DR BioCyc; ARA:AT1G44318-MON; -.
DR UniPathway; UPA00251; UER00318.
DR UniPathway; UPA00668; -.
DR PRO; PR:Q94LA4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94LA4; baseline and differential.
DR Genevisible; Q94LA4; AT.
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-UniPathway.
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; IPR013785; Aldolase_TIM.
DR PANTHER; PTHR11458; PTHR11458; 1.
DR Pfam; PF00490; ALAD; 1.
DR PRINTS; PR00144; DALDHYDRTASE.
DR SMART; SM01004; ALAD; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Chlorophyll biosynthesis; Chloroplast;
KW Heme biosynthesis; Lyase; Magnesium; Metal-binding; Plastid;
KW Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 35..406
FT /note="Probable delta-aminolevulinic acid dehydratase 2,
FT chloroplastic"
FT /id="PRO_0000422672"
FT ACT_SITE 275
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT ACT_SITE 322
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 406 AA; 44878 MW; 47ED3AD6F1ED0A91 CRC64;
MTSSMFRSPC KIPSVKGFEQ KSYVGLKAAS YNVRVNSFKS SEVASQLQKI DSTLIWPVNA
LEAPPVPSKP ATPLIDQPLQ LSRRARRNRK CPTQRAAFQE TNISPANFIY PLFIHEGEVD
IPITSMPGRY MLGWRHGLIE EVARALDVGV NSVKLYPKVP EALKSPTGEE AFNDNGLIPR
TVRLLKDRFP DLVIYTDVNF DEYSTTGHGG IVGEDGVILN DETIHQLRKQ AVSQARAGAD
VVCTSEMLDG RVGAVRAALD AEGFQDVSIM SYSVKYTSSL YGRFRKVQLD KKTYQINPAN
SREALLEARE DEAEGADILM VKPALPSLDI IRLLKNQTLL PIGACQVSGE YSMIKAAGLL
KMIDEEKVMM ESLLCIRRAG ADLILTYFAL QAATKLCGEN KRFSSN
