ADH1_EUPLT
ID ADH1_EUPLT Reviewed; 288 AA.
AC A0A165U5V5;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Short chain aldehyde dehydrogenase 1 {ECO:0000303|PubMed:27506796};
DE Short=ElADH1 {ECO:0000303|PubMed:27506796};
DE EC=1.1.1.1 {ECO:0000255|PROSITE-ProRule:PRU10001};
DE AltName: Full=Jolkinol C synthase {ECO:0000305|PubMed:27506796};
DE EC=1.1.1.- {ECO:0000269|PubMed:27506796};
GN Name=ADH1 {ECO:0000303|PubMed:27506796};
OS Euphorbia lathyris (Caper spurge).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Euphorbioideae; Euphorbieae;
OC Euphorbia; Euphorbia subgen. Esula; Euphorbia sect. Lathyris.
OX NCBI_TaxID=212925;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Seed;
RX PubMed=27506796; DOI=10.1073/pnas.1607504113;
RA Luo D., Callari R., Hamberger B., Wubshet S.G., Nielsen M.T.,
RA Andersen-Ranberg J., Hallstroem B.M., Cozzi F., Heider H.,
RA Lindberg Moeller B., Staerk D., Hamberger B.;
RT "Oxidation and cyclization of casbene in the biosynthesis of Euphorbia
RT factors from mature seeds of Euphorbia lathyris L.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E5082-E5089(2016).
CC -!- FUNCTION: Involved in the biosynthesis of macrocyclic lathyrane type
CC diterpenoids (also called Euphorbia factors) natural products,
CC including the cyclization route from casbene to jolkinol C, a precursor
CC for ingenol mebutate that is used to treat actinic keratosis, a
CC precancerous skin condition (PubMed:27506796). Catalyzes the conversion
CC of 4,5,8-trihydroxycasbene into jolkinol C in presence of NAD
CC (PubMed:27506796). Mediates also the formation of casbene dione
CC derivative and 4-ketocasbene from 4-hydroxy-8-ketocasbene and 4-
CC hydroxycasbene, respectively (PubMed:27506796). Together with
CC CYP71D445, triggers the biosynthesis of 8-ketocasbene from 8-
CC hydroxycasbene (PubMed:27506796). {ECO:0000269|PubMed:27506796}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,5,8-trihydroxycasbene + 2 NAD(+) = 2 H(+) + jolkinol C + 2
CC NADH; Xref=Rhea:RHEA:65600, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:156580, ChEBI:CHEBI:157602;
CC Evidence={ECO:0000269|PubMed:27506796};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65601;
CC Evidence={ECO:0000269|PubMed:27506796};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10001};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10001};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:27506796}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P48814}.
CC -!- TISSUE SPECIFICITY: Expressed in mature seeds.
CC {ECO:0000269|PubMed:27506796}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; KR350665; AMY98415.1; -; mRNA.
DR SMR; A0A165U5V5; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase.
FT CHAIN 1..288
FT /note="Short chain aldehyde dehydrogenase 1"
FT /id="PRO_0000453169"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT ACT_SITE 170
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19337"
FT BINDING 26..28
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 47
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 72..73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 99..101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT BINDING 166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT BINDING 170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
SQ SEQUENCE 288 AA; 29980 MW; D6AD3CFD83763481 CRC64;
MNGCCSQDPT SKRLEGKVAV ITGGASGIGA CTVKLFVKHG AKVVIADVQD ELGHSLCKEI
GSEDVVTYVH CDVSSDSDVK NVVDSAVSKY GKLDIMFSNA GVSGGLDPRI LATENDEFKK
VFEVNVFGGF LAAKHAARVM IPEKKGCILF TSSNSAAIAI PGPHSYVVSK HALNGLMKNL
SAELGQHGIR VNCVSPFGVV TPMMATAFGM KDADPEVVKA TIEGLLASAA NLKEVTLGAE
DIANAALYLA SDEAKYVSGL NLVVDGGYSV TNPSFTATLQ KAFAVAHV
