ABA1_BOTFU
ID ABA1_BOTFU Reviewed; 509 AA.
AC Q6H9H9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Cytochrome P450 monooxygenase aba1 {ECO:0000303|PubMed:16820452};
DE EC=1.-.-.- {ECO:0000305|PubMed:15240257};
DE AltName: Full=Abscisic acid biosynthesis cluster protein 2 {ECO:0000303|PubMed:16820452};
DE Flags: Precursor;
GN Name=aba1 {ECO:0000303|PubMed:15240257};
OS Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=40559;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, DISRUPTION
RP PHENOTYPE, AND PATHWAY.
RC STRAIN=SAS56;
RX PubMed=15240257; DOI=10.1128/aem.70.7.3868-3876.2004;
RA Siewers V., Smedsgaard J., Tudzynski P.;
RT "The P450 monooxygenase BcABA1 is essential for abscisic acid biosynthesis
RT in Botrytis cinerea.";
RL Appl. Environ. Microbiol. 70:3868-3876(2004).
RN [2]
RP INDUCTION, AND FUNCTION.
RX PubMed=16820452; DOI=10.1128/aem.02919-05;
RA Siewers V., Kokkelink L., Smedsgaard J., Tudzynski P.;
RT "Identification of an abscisic acid gene cluster in the grey mold Botrytis
RT cinerea.";
RL Appl. Environ. Microbiol. 72:4619-4626(2006).
RN [3]
RP FUNCTION.
RX PubMed=30226766; DOI=10.1021/jacs.8b08925;
RA Takino J., Kozaki T., Sato Y., Liu C., Ozaki T., Minami A., Oikawa H.;
RT "Unveiling biosynthesis of the phytohormone abscisic acid in fungi:
RT unprecedented mechanism of core scaffold formation catalyzed by an unusual
RT sesquiterpene synthase.";
RL J. Am. Chem. Soc. 140:12392-12395(2018).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of abscisic acid (ABA), a phytohormone that
CC acts antagonistically toward salicylic acid (SA), jasmonic acid (JA)
CC and ethylene (ETH) signaling, to impede plant defense responses
CC (PubMed:15240257, PubMed:16820452). The first step of the pathway
CC catalyzes the reaction from farnesyl diphosphate to alpha-
CC ionylideneethane performed by the alpha-ionylideneethane synthase aba3
CC via a three-step reaction mechanism involving 2 neutral intermediates,
CC beta-farnesene and allofarnesene (PubMed:30226766). The cytochrome P450
CC monooxygenase aba1 might then be involved in the conversion of alpha-
CC ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-
CC ionylideneacetic acid is further converted to abscisic acid in 2 steps
CC involving the cytochrome P450 monooxygenase aba2 and the short-chain
CC dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or
CC 1',4'-trans-diol-ABA, depending on the order of action of these 2
CC enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon
CC atom C-1' and aba4 might be involved in the oxidation of the C-4'
CC carbon atom (PubMed:16820452). {ECO:0000269|PubMed:15240257,
CC ECO:0000269|PubMed:16820452, ECO:0000269|PubMed:30226766,
CC ECO:0000305|PubMed:16820452}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Hormone biosynthesis. {ECO:0000269|PubMed:15240257}.
CC -!- INDUCTION: Expression is persistently induced 90 min after the addition
CC of the ABA precursor mevalonic acid (MVA) to the medium.
CC {ECO:0000269|PubMed:16820452}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of abscisic acid (ABA).
CC {ECO:0000269|PubMed:15240257}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AJ609392; CAE76652.2; -; Genomic_DNA.
DR AlphaFoldDB; Q6H9H9; -.
DR SMR; Q6H9H9; -.
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:0009688; P:abscisic acid biosynthetic process; IMP:GO_Central.
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 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Signal; Virulence.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..509
FT /note="Cytochrome P450 monooxygenase aba1"
FT /id="PRO_0000448410"
FT BINDING 451
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:P04798"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 509 AA; 57218 MW; 1B9F09B92487CE07 CRC64;
MSNSILNLGS FACLLSLGSI VLWYTISAVL AWYPLRKIPA PSFLATFSYL WLAKTTYSGK
QYWIQRDLHK KYGPLVRIGP TDIITDDPEI IKKISSARSS HRRGDWYLTG RFNPYYDNMF
TMLEPGPHAK AKARTAAAYS GRDMPDLEVG VNAQLQTLIG LMRSKYASNT VKPHQPLLDL
GQVSCFFTMD VITRLAFGEE FGYLKEETDQ YGFLGEVREL WPRMSTSADT PWIRKFLFSP
PFLKVLGPKP TDKTGFGALM AVAEHHVGKR FAPDAKKKED MLGSFIRHGL NQQECEVEGL
FMIVAGTEST ASAIRSTLVH VMTCPRVYQK LKTEINLAVE EGKVSSPIKL EEAKLLPFLQ
AVIYEGIRMR PPLLGLFPKI VPDGGEEFHG MFIPAGTAIC MNTSSLLRST ALFGDDAEVY
RPERFMELEK SKRGEMERNV ELAFGYGQYM CVGKTVAFME LNKSIFEILR AFDLQLLSPA
KPCDVLSYGI FLESNMLVKV TESEGTEYK
