ALDH1_TANCI
ID ALDH1_TANCI Reviewed; 499 AA.
AC A0A2I7G3B0;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Aldehyde dehydrogenase 1 {ECO:0000303|PubMed:29122986};
DE Short=TcALDH1 {ECO:0000303|PubMed:29122986};
DE EC=1.2.1.5 {ECO:0000269|PubMed:29122986};
DE AltName: Full=Trans-chrysanthemic acid synthase {ECO:0000305};
DE EC=1.2.1.- {ECO:0000269|PubMed:29122986};
GN Name=ALDH1 {ECO:0000303|PubMed:29122986};
OS Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum
OS cinerariifolium).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Anthemidinae; Tanacetum.
OX NCBI_TaxID=118510;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RX PubMed=29122986; DOI=10.1104/pp.17.01330;
RA Xu H., Moghe G.D., Wiegert-Rininger K., Schilmiller A.L., Barry C.S.,
RA Last R.L., Pichersky E.;
RT "Coexpression analysis identifies two oxidoreductases involved in the
RT biosynthesis of the monoterpene acid moiety of natural pyrethrin
RT insecticides in Tanacetum cinerariifolium.";
RL Plant Physiol. 176:524-537(2018).
RN [2]
RP REVIEW.
RX PubMed=15964038; DOI=10.1016/j.phytochem.2005.05.005;
RA Matsuda K., Kikuta Y., Haba A., Nakayama K., Katsuda Y., Hatanaka A.,
RA Komai K.;
RT "Biosynthesis of pyrethrin I in seedlings of Chrysanthemum
RT cinerariaefolium.";
RL Phytochemistry 66:1529-1535(2005).
RN [3]
RP REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Component of the monoterpenoid pyrethrins biosynthesis;
CC pyrethrins are widely used plant-derived pesticide (PubMed:30468448).
CC Mediates the conversion of trans-chrysanthemal into trans-chrysanthemic
CC acid (PubMed:29122986). Can also use octanal, hept-2-enal, dodecanal,
CC citral, farnesal, citronellal and perillyl aldehyde as substrates
CC (PubMed:29122986). {ECO:0000269|PubMed:29122986,
CC ECO:0000303|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.5;
CC Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NADP(+) = a carboxylate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:11888, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.5;
CC Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11889;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + octanal = 2 H(+) + NADPH + octanoate;
CC Xref=Rhea:RHEA:59904, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59905;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,3R)-chrysanthemal + H2O + NAD(+) = (1R,3R)-chrysanthemate
CC + 2 H(+) + NADH; Xref=Rhea:RHEA:60708, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:143899, ChEBI:CHEBI:143900;
CC Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60709;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,3R)-chrysanthemal + H2O + NADP(+) = (1R,3R)-chrysanthemate
CC + 2 H(+) + NADPH; Xref=Rhea:RHEA:60716, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:143899, ChEBI:CHEBI:143900;
CC Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60717;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-hept-2-enal + H2O + NADP(+) = (E)-hept-2-enoate + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:60720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:143912,
CC ChEBI:CHEBI:143913; Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60721;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanal + H2O + NADP(+) = dodecanoate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:60724, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:27836, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60725;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citral + H2O + NADP(+) = 3,7-dimethylocta-2,6-dienoate + 2
CC H(+) + NADPH; Xref=Rhea:RHEA:60728, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:23316, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:142930;
CC Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60729;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + perillyl aldehyde = 2 H(+) + NADPH +
CC perillate; Xref=Rhea:RHEA:60732, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15421, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:62641;
CC Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60733;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesal + H2O + NADP(+) = (2E,6E)-farnesoate + 2 H(+)
CC + NADPH; Xref=Rhea:RHEA:60736, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15894, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83276; Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60737;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-(-)-citronellal + H2O + NADP(+) = (S)-(-)-citronellate + 2
CC H(+) + NADPH; Xref=Rhea:RHEA:60740, ChEBI:CHEBI:368,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:143914;
CC Evidence={ECO:0000269|PubMed:29122986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60741;
CC Evidence={ECO:0000269|PubMed:29122986};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.6 uM for trans-chrysanthemal (in the presence of NAD(+))
CC {ECO:0000269|PubMed:29122986};
CC KM=4.4 uM for trans-chrysanthemal (in the presence of NADP(+))
CC {ECO:0000269|PubMed:29122986};
CC KM=20.4 uM for NAD(+) {ECO:0000269|PubMed:29122986};
CC KM=68.6 uM for NADP(+) {ECO:0000269|PubMed:29122986};
CC Note=kcat is 0.11 sec(-1) with trans-chrysanthemal as substrate (in
CC the presence of NAD(+)) (PubMed:29122986). kcat is 0.096 sec(-1) with
CC trans-chrysanthemal as substrate (in the presence of NADP(+))
CC (PubMed:29122986). kcat is 0.09 sec(-1) with NAD(+) as substrate (in
CC the presence of trans-chrysanthemal) (PubMed:29122986). kcat is 0.086
CC sec(-1) with NADP(+) as substrate (in the presence of trans-
CC chrysanthemal) (PubMed:29122986). {ECO:0000269|PubMed:29122986};
CC -!- PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:29122986}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P51977}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and disk florets.
CC {ECO:0000269|PubMed:29122986}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; MF497445; AUQ44119.1; -; mRNA.
DR AlphaFoldDB; A0A2I7G3B0; -.
DR SMR; A0A2I7G3B0; -.
DR BioCyc; MetaCyc:MON-20953; -.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0033721; F:aldehyde dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase.
FT CHAIN 1..499
FT /note="Aldehyde dehydrogenase 1"
FT /id="PRO_0000447849"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 300
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P51977"
FT BINDING 164..167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P51977"
FT BINDING 164..166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT BINDING 190..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P51977"
FT BINDING 223..224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P51977"
FT BINDING 243..248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT BINDING 243..244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P51977"
FT BINDING 266..268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 346..350
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 397..399
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P51977"
FT SITE 167
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
SQ SEQUENCE 499 AA; 53988 MW; 834E841905168901 CRC64;
MSSGANGNSK SLAYDIKFTK LFINGEFVDS ISGSTFETID PATEEVLATV AEGREEDVDL
AVKAAREAFD NGPWPRLSGE ARRKILLKFA DLIEENADEI ATLEVIDTGK PFQIARYVEN
SWTSETFRYF AGAADKIRGA TLKMSSDFQA YTLREPIGVV GHIIPWNAPA YLFAMKVAPA
LAAGCTVVIK PAENTPLVGL FMAYLSKLAG VPDGVINVVN GFGSTAGAAV SSHMDIDAVT
FTGSTKVGRT IMQAAAASNL KPVSLELGGK SPFIVFDDAD IEKAAEIAVL GVLSNKGELC
VAGSRVFVHE GIYDAFVKKL EATVKNWATG DRFDAATRHG PQNNKQQYEK VLSYIELGKK
EGATLVTGGK PFGNKGYYIE PTLFTNVTDE MTIAKEEIFG PVIMVLKFKT IEEVIRRANA
TTYGLAAGIM TKNIDIANTV TRSIRAGSVW VNCYLALDRD TPFGGYKMSG FGREQGLEAL
EHYLQVKTVT TPIYNSPWL
