ID Q9ARD8_LINPO Unreviewed; 270 AA.
AC Q9ARD8;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 22-FEB-2023, entry version 66.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
DE Flags: Fragment;
GN Name=hemB {ECO:0000313|EMBL:CAC36151.1};
OS Lingulodinium polyedra (Dinoflagellate) (Gonyaulax polyedra).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Gonyaulacales; Lingulodiniaceae;
OC Lingulodinium.
OX NCBI_TaxID=160621 {ECO:0000313|EMBL:CAC36151.1};
RN [1] {ECO:0000313|EMBL:CAC36151.1}
RP NUCLEOTIDE SEQUENCE.
RA Evans C., Smith A.;
RT "Algal ALAD is unlikely to be derived from the plastid endosymbiont.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
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 = 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 Evidence={ECO:0000256|ARBA:ARBA00001227,
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; AJ310907; CAC36151.1; -; mRNA.
DR AlphaFoldDB; Q9ARD8; -.
DR UniPathway; UPA00251; UER00318.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
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 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}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAC36151.1"
SQ SEQUENCE 270 AA; 29586 MW; 06A03F1889D9D692 CRC64;
WHEVKSVVIF PKTPDELKTP TAEEAFNPDG LAQRAIRNVK RAFPDVVVYT DVALDPYNSL
GHDGIVRSDG VVLNDETIAY LCKQAVSQAE AGADYVSPSD MMDGRVGAIR DALDEAGFTD
VGIMAYSAKY ASAFYGPFRE ALDSNPRLPS PDWQVPDGKQ TYQQDPGNYR EALLEAKLDE
EEGADILMVK PGMPYLDVIK GLHENSNLPI AAYHVSGEYA MLKAAALNGW LDEKAVVLEA
LLSIKRAGAT VILTYYATQA ARWLKEDQEA
//
