ID A0A1X7SSR5_AMPQE Unreviewed; 594 AA.
AC A0A1X7SSR5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
OS Amphimedon queenslandica (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Haplosclerida; Niphatidae; Amphimedon.
OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.05199_001, ECO:0000313|Proteomes:UP000007879};
RN [1] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20686567; DOI=10.1038/nature09201;
RA Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The Amphimedon queenslandica genome and the evolution of animal
RT complexity.";
RL Nature 466:720-726(2010).
RN [2] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT evolution of animal complexity.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.05199_001}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2017) to UniProtKB.
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; active form. Homohexamer; low activity form.
CC {ECO:0000256|ARBA:ARBA00025861}.
CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000256|ARBA:ARBA00008055,
CC ECO:0000256|RuleBase:RU004161}.
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DR AlphaFoldDB; A0A1X7SSR5; -.
DR STRING; 400682.A0A1X7SSR5; -.
DR EnsemblMetazoa; Aqu2.1.05199_001; Aqu2.1.05199_001; Aqu2.1.05199.
DR eggNOG; KOG2794; Eukaryota.
DR InParanoid; A0A1X7SSR5; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000007879; Unassembled WGS sequence.
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 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:UP000007879}.
FT REGION 246..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 594 AA; 64242 MW; 67361D67E4EA9957 CRC64;
AISSIKAACP DLVIITDVCV CEYTDHGHCG LLSQGHPHLP DGYVLNDESV DILARVSLSH
ALAGADIVAP SAMLDGMVAG IRKALDGQSF HHLPIMSYAV KYASAFYGPF RDAAQGAPKF
GDRRSHQMDP ANAREALKEA AIDVEEGADF LMVKPALAYL DIIARVRERF PEMPMVAYNT
SGEYAMVKAA SERGWLDERA TVLEKLTAIK RAGADLIISY HALEAAAWQG CALALKEDSP
ISACRIGPEN TPPSPIRATV LRGSPRGSLR APERSRMPPK GKRRCRIAAD RLSVSDADAI
ALEKRRSREE SDWPMPIEGR SSTSAAPGSS PSPKYANPHR FGAIFQGQPQ KDGPRGISLL
RIGTGDAGGR KADIRPENLA HPDSHRLGRL FRNHRTARHT QEIEFDFTVV GDHRAFENIA
RPGDRRQPGS DEPAGQGLGH RQREPSLAQH IEGHRFHGLR IDPENRIPDN LPDAHFLGRD
QCIGGRGIGG LGGDPHFQPL DAAGLECEGG IAGGIEGTDA LFEQLRQARF AFAPGLEHPA
SNRGLHPGPT PKVGKDRALD HLAHLRGHPR HGVDHSGFEG ANETGSGPRH LRDE
//
