ID   Q8IL68_PLAF7            Unreviewed;       451 AA.
AC   Q8IL68;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   02-SEP-2026, entry version 134.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE            EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN   ORFNames=PF3D7_1440300 {ECO:0000313|EMBL:CZU00098.1};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Laverania.
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:CZU00098.1, ECO:0000313|Proteomes:UP000001450};
RN   [1] {ECO:0000313|EMBL:CZU00098.1, ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA   Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., Chan M.S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
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
CC       porphobilinogen. {ECO:0000256|ARBA:ARBA00025628}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 5-aminolevulinate = porphobilinogen + 2 H2O + H(+);
CC         Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24;
CC         Evidence={ECO:0000256|ARBA:ARBA00047651,
CC         ECO:0000256|RuleBase:RU000515};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004694}.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|RuleBase:RU000515}.
CC   -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000256|ARBA:ARBA00008055,
CC       ECO:0000256|RuleBase:RU004161}.
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DR   EMBL; LN999946; CZU00098.1; -; Genomic_DNA.
DR   RefSeq; XP_001348555.1; XM_001348519.1.
DR   AlphaFoldDB; Q8IL68; -.
DR   SMR; Q8IL68; -.
DR   FunCoup; Q8IL68; 265.
DR   STRING; 36329.Q8IL68; -.
DR   PaxDb; 36329-Q8IL68; -.
DR   GeneID; 811964; -.
DR   KEGG; pfa:PF3D7_1440200; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1440300; -.
DR   HOGENOM; CLU_035731_0_0_1; -.
DR   InParanoid; Q8IL68; -.
DR   OMA; YMDIIWR; -.
DR   OrthoDB; 1530at2759; -.
DR   PhylomeDB; Q8IL68; -.
DR   Reactome; R-PFA-189451; Heme biosynthesis.
DR   Reactome; R-PFA-6798695; Neutrophil degranulation.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000001450; Chromosome 14.
DR   GO; GO:0020011; C:apicoplast; IDA:GeneDB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004655; F:porphobilinogen synthase activity; IDA:GeneDB.
DR   GO; GO:0006783; P:heme biosynthetic process; IDA:GeneDB.
DR   FunFam; 3.20.20.70:FF:000298; Delta-aminolevulinic acid dehydratase; 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   NCBIfam; NF006762; PRK09283.1; 1.
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   3: Inferred from homology;
KW   Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000515};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW   ECO:0000256|RuleBase:RU000515};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..451
FT                   /note="Delta-aminolevulinic acid dehydratase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030176283"
SQ   SEQUENCE   451 AA;  53188 MW;  B9D3001C167590D3 CRC64;
     MLKSDVVLLL YILIINLICC LNGNSKKRAY ILNTPKSSNC KRSSFRRWNN PVNNNNSQIL
     SKNEGSIEDV YNKKISGRCN IKNFSKDINN NIYIETNRRE RRIKRNKYLL SLYNNTNIKT
     SNFIYPLFIH EEDVEKKHTQ LEGIYTYNVD GIIKEIEECI KLNIHHFMFF PVIREENKTV
     YCEESYNENS YFCKTISRIK EKFSDDIIVY TDVALDPYNI YGHDGIYDDN KKEILNDITV
     HTLVKQSLCL AKSGADVVCP SDSMDKRIEL IRKNLDFHNF RDILILSYTC KYSSSMYKPF
     RSILNSNILK NFVKNKQSYQ HDFNSYMDLN NVDKHIIEGA DIIMVKPSMF YLDIIHKIKN
     RIKDDVQIPI AVYNVSGEYM MIKNYVKYLN EDINYENEII TELFKSYLRA GANIIITYFA
     KQYGLYMKKL YDKNIIIDDN SNNNFNIELT L
//