DABC_PSEMU
ID DABC_PSEMU Reviewed; 373 AA.
AC A0A386KZ95;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Alpha-ketoglutarate dependent kainoid synthase {ECO:0000303|PubMed:30262498};
DE Short=Alpha-KG dependent kainoid synthase {ECO:0000303|PubMed:30262498};
DE EC=1.14.11.- {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:30262498};
DE AltName: Full=Domoic acid biosynthesis cluster protein C {ECO:0000303|PubMed:30262498};
DE Short=PmDabC {ECO:0000303|PubMed:30262498};
GN Name=dabC {ECO:0000303|PubMed:30262498};
OS Pseudo-nitzschia multiseries (Marine planktonic diatom) (Nitzschia pungens
OS f. multiseries).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC Pseudo-nitzschia.
OX NCBI_TaxID=37319;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND INDUCTION BY PHOSPHATE LIMITATION AND CO(2).
RC STRAIN=15091C3;
RX PubMed=30262498; DOI=10.1126/science.aau0382;
RA Brunson J.K., McKinnie S.M.K., Chekan J.R., McCrow J.P., Miles Z.D.,
RA Bertrand E.M., Bielinski V.A., Luhavaya H., Obornik M., Smith G.J.,
RA Hutchins D.A., Allen A.E., Moore B.S.;
RT "Biosynthesis of the neurotoxin domoic acid in a bloom-forming diatom.";
RL Science 361:1356-1358(2018).
RN [2]
RP REVIEW ON NEUROTOXIC ACTIVITY.
RX PubMed=10223631;
RX DOI=10.1002/(sici)1522-7189(199805/08)6:3/4<153::aid-nt16>3.0.co;2-1;
RA Hampson D.R., Manalo J.L.;
RT "The activation of glutamate receptors by kainic acid and domoic acid.";
RL Nat. Toxins 6:153-158(1998).
CC -!- FUNCTION: Iron/ascorbate-dependent oxidoreductase: part of the gene
CC cluster that mediates the biosynthesis of domoic acid (DA) and
CC derivatives, natural products with neurochemical activity acting as
CC ionotropic glutamate receptor (iGluR) agonists, thus being neurotoxins
CC causing amnesic shellfish poisoning (ASP) (PubMed:30262498). Catalyzes
CC the conversion of 7'-N-carboxy-L-geranyl-L-glutamic acid (cNGG) to
CC isodomoic acid-A (PubMed:30262498). Mediates also the conversion of N-
CC geranyl-L-glutamic acid (L-NGG) to dainic acid A (PubMed:30262498).
CC {ECO:0000269|PubMed:30262498}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N-(7'-carboxy-7'-demethylgeranyl)-L-glutamate
CC + O2 = CO2 + H2O + isodomoate A + succinate; Xref=Rhea:RHEA:68172,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:172366,
CC ChEBI:CHEBI:172367; Evidence={ECO:0000269|PubMed:30262498};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68173;
CC Evidence={ECO:0000269|PubMed:30262498};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N-geranyl-L-glutamate + O2 = CO2 + dainate A
CC + H2O + succinate; Xref=Rhea:RHEA:68176, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:172365, ChEBI:CHEBI:176974;
CC Evidence={ECO:0000269|PubMed:30262498};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68177;
CC Evidence={ECO:0000269|PubMed:30262498};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:30262498}.
CC -!- INDUCTION: Up-regulated under phosphate limitation and by increasing
CC partial pressure of CO(2). {ECO:0000269|PubMed:30262498}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; MH202990; AYD91075.1; -; Genomic_DNA.
DR SMR; A0A386KZ95; -.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IEP:UniProtKB.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:UniProtKB.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..373
FT /note="Alpha-ketoglutarate dependent kainoid synthase"
FT /id="PRO_0000454274"
FT DOMAIN 204..320
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 235
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 296
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 311
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 373 AA; 42448 MW; BCE01BEE7CB987FB CRC64;
MTVAINNETV VLTPNEDDVQ VNKGKTLETS FPPLKGDDLK WFPRSSLPAE IPAIDIGKVS
TKEELEQFLV DIRKSGLFYI VNHGVPEEVS INVYNAFREF ISTTTEEERM KYYTDTHFQN
GGYVPFQGSS IRGGNLGKPQ KDHVVKYFWR GPEVINRTPN EKFTEAHNMH HTETFKVAEK
VIRTIFKALK LRFPDFDPME FENTINSKKM FFTNRIYPQA EPSDEEEITH RLVPHLDTSF
ITLANQVPAD NGFQGLFVET GDGKKVKVPG IRNSYLVFIG QSLSYLTKNY LPSALHGVDK
PPSDLFEGSE RSSLITFYEP AEIIIPSKNI NPNPEETSES CPFFYDIGLT VNDPEGTTWD
FVKNKFITGY YAD
