HEM2_PHYPA
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 03-AUG-2022, entry version 108.
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 STRING; 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 OrthoDB; 918089at2759; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000006727; Chromosome 4.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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-KW.
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..?
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
