ID   HEM2_PHYPA              Reviewed;         432 AA.
AC   Q43058; A9TFG3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   03-SEP-2014, sequence version 2.
DT   24-JAN-2024, entry version 114.
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; ORFNames=PHYPADRAFT_221821;
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gwarek M.A.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004;
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
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   -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
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DR   EMBL; X89886; CAA61978.1; -; mRNA.
DR   EMBL; DS545108; EDQ57858.1; -; Genomic_DNA.
DR   PIR; S58169; S58169.
DR   RefSeq; XP_001777328.1; XM_001777276.1.
DR   AlphaFoldDB; Q43058; -.
DR   SMR; Q43058; -.
DR   PaxDb; 3218-PP1S219_94V6-1; -.
DR   EnsemblPlants; Pp3c4_13690V3.1; Pp3c4_13690V3.1; Pp3c4_13690.
DR   EnsemblPlants; Pp3c4_13690V3.3; Pp3c4_13690V3.3; Pp3c4_13690.
DR   EnsemblPlants; Pp3c4_13690V3.4; Pp3c4_13690V3.4; Pp3c4_13690.
DR   EnsemblPlants; Pp3c4_13690V3.5; Pp3c4_13690V3.5; Pp3c4_13690.
DR   Gramene; Pp3c4_13690V3.1; Pp3c4_13690V3.1; Pp3c4_13690.
DR   Gramene; Pp3c4_13690V3.3; Pp3c4_13690V3.3; Pp3c4_13690.
DR   Gramene; Pp3c4_13690V3.4; Pp3c4_13690V3.4; Pp3c4_13690.
DR   Gramene; Pp3c4_13690V3.5; Pp3c4_13690V3.5; Pp3c4_13690.
DR   eggNOG; KOG2794; Eukaryota.
DR   HOGENOM; CLU_035731_1_2_1; -.
DR   InParanoid; Q43058; -.
DR   OrthoDB; 2782182at2759; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000006727; Chromosome 4.
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   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.
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..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..432
FT                   /note="Delta-aminolevulinic acid dehydratase,
FT                   chloroplastic"
FT                   /id="PRO_0000013318"
FT   REGION          84..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        300
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        353
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         310
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         322
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         338
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         379
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         418
FT                   /ligand="5-aminolevulinate"
FT                   /ligand_id="ChEBI:CHEBI:356416"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        15
FT                   /note="G -> R (in Ref. 1; CAA61978)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        24
FT                   /note="G -> S (in Ref. 1; CAA61978)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212..214
FT                   /note="DKF -> AI (in Ref. 1; CAA61978)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="M -> I (in Ref. 1; CAA61978)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        309
FT                   /note="F -> S (in Ref. 1; CAA61978)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        388..391
FT                   /note="AAAA -> GCR (in Ref. 1; CAA61978)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   432 AA;  46263 MW;  E90018ADAAAA12FD CRC64;
     MVGVMMAAAA TPGCGVSQAL TACGSHEGLR RVAPVFGPGV VSVSAPCKLP RKLNVQAVAE
     PIAKSSPRTI EECEANVVAG NAPAAPPVPA KPSAPEGTPA ISPLVMPARP RRNRRSPALR
     AAFQETTISP ANFILPLFVH EGEQNAPIGA MPGCQRLGWR HGLIDEVYKA RDVGVNSVVL
     FPKVPDALKS STGDEAYNPD GLVPRCIRLL KDKFPDLVIY TDVALDPYSS DGHDGIVRED
     GLIMNDETVH QLCKQAVAQA QAGADVVSPS DMMDGRVGAI RKALDLAGHQ DVSIMAYTAK
     YASAFYGPFR EALDSNPRFG DKKTYQMNPA NYREALIETR MDEAEGADIL MVKPAMPYLD
     VIRLLRDNTA LPISAYQVSG EYSMIRAAAA AGMLDEKKAV LESLLSIRRA GADVILTYFA
     IQAAQWLCAE RV
//