DABD_PSEMU
ID DABD_PSEMU Reviewed; 559 AA.
AC A0A386KZI3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=N-geranyl-L-glutamate oxidase {ECO:0000303|PubMed:30262498};
DE EC=1.14.14.- {ECO:0000269|PubMed:30262498};
DE AltName: Full=Domoic acid biosynthesis cluster protein D {ECO:0000303|PubMed:30262498};
DE Short=PmDabD {ECO:0000303|PubMed:30262498};
GN Name=dabD {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: Cytochrome P450 monooxygenase: part of the gene cluster that
CC mediates the biosynthesis of domoic acid (DA) and derivatives, natural
CC products with neurochemical activity acting as ionotropic glutamate
CC receptor (iGluR) agonists, thus being neurotoxins causing amnesic
CC shellfish poisoning (ASP) (PubMed:30262498). Catalyzes the conversion
CC of N-geranyl-L-glutamic acid (L-NGG) to N-(7'-carboxy-7'-
CC demethylgeranyl)-L-glutamic acid (cNGG) via three successive steps
CC involving N-(8'-hydroxygeranyl)-L-glutamic acid and N-(8'-oxogeranyl)-
CC L-glutamic acid as intermediates (PubMed:30262498).
CC {ECO:0000269|PubMed:30262498}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-geranyl-L-glutamate + O2 + reduced [NADPH--hemoprotein
CC reductase] = H(+) + H2O + N-(8'-hydroxygeranyl)-L-glutamate +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68160,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:172365, ChEBI:CHEBI:176971;
CC Evidence={ECO:0000269|PubMed:30262498};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68161;
CC Evidence={ECO:0000269|PubMed:30262498};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(8'-hydroxygeranyl)-L-glutamate + O2 + reduced [NADPH--
CC hemoprotein reductase] = H(+) + 2 H2O + N-(8'-oxogeranyl)-L-glutamate
CC + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68164,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:176971, ChEBI:CHEBI:176972;
CC Evidence={ECO:0000269|PubMed:30262498};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68165;
CC Evidence={ECO:0000269|PubMed:30262498};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(8'-oxogeranyl)-L-glutamate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 2 H(+) + H2O + N-(7'-carboxy-7'-
CC demethylgeranyl)-L-glutamate + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:68168, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:172366,
CC ChEBI:CHEBI:176972; Evidence={ECO:0000269|PubMed:30262498};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68169;
CC Evidence={ECO:0000269|PubMed:30262498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:30262498}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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 cytochrome P450 family. {ECO:0000305}.
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DR EMBL; MH202990; AYD91074.1; -; Genomic_DNA.
DR SMR; A0A386KZI3; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..559
FT /note="N-geranyl-L-glutamate oxidase"
FT /id="PRO_0000454275"
FT TRANSMEM 49..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 503
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q94IP1"
SQ SEQUENCE 559 AA; 63266 MW; EAB402B04A884DA2 CRC64;
MNIATASLCA GLAVSGKFLS KYYQFLSTSQ SDEVGFIEIM NMGMTGNDAV ACASLGFVMY
CVLSFARSYY RFRFSPLRNA PGFGPKSFVY GMFYEFLEAP FMEPPIEALK KLRKGGNDIP
FLAYTTLFGS QRLLLLDCDL IKQVFTAPSG RDPMRYPKHY VYLREVVGDG LVVVEGSEWS
RHRRIVQPAF QSAFLRDAIT TTVPTLVENL VDVWKKTAGT SINLNAHLSI ITLDVIGKVA
FSHEFNASKL LNEWAECPDK ELGEVDDPLI SSIGAAFSSS PLKLMLTVLK QPWLEKHLSP
AFRTSRNLLN KAADDIVQNA KNIDDPKRRS VLNLMMEAKD DESSKARNKL TDTELRDEVK
TFLVAGHETT STWAHWSLYV LATRPDIQEK VFADITKHSP DDKTILLEQA DQMEYLWAFM
NETLRLYSPL GLISRVTHKE ENFKGYTIPA GTNLRIPIHL IHRHPDHWKD PEDFKPERWF
DTEESSKRHK FAFIPFAAGG RNCIGQRFAS MEAKIIVANV AKNFEIHLAD SMKGKKITFS
NFISLKCKPE IEIYVTPRG
