ABA2_BOTFB
ID ABA2_BOTFB Reviewed; 527 AA.
AC A0A384JQH2;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Cytochrome P450 monooxygenase aba2 {ECO:0000303|PubMed:16820452};
DE EC=1.-.-.- {ECO:0000305|PubMed:16820452};
DE AltName: Full=Abscisic acid biosynthesis cluster protein 2 {ECO:0000303|PubMed:16820452};
GN Name=aba2; ORFNames=BCIN_08g03840;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=23104368; DOI=10.1128/ec.00164-12;
RA Staats M., van Kan J.A.L.;
RT "Genome update of Botrytis cinerea strains B05.10 and T4.";
RL Eukaryot. Cell 11:1413-1414(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=26913498; DOI=10.1111/mpp.12384;
RA van Kan J.A.L., Stassen J.H.M., Mosbach A., van der Lee T.A.J., Faino L.,
RA Farmer A.D., Papasotiriou D.G., Zhou S., Seidl M.F., Cottam E., Edel D.,
RA Hahn M., Schwartz D.C., Dietrich R.A., Widdison S., Scalliet G.;
RT "A gapless genome sequence of the fungus Botrytis cinerea.";
RL Mol. Plant Pathol. 18:75-89(2017).
RN [4]
RP FUNCTION.
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 [5]
RP INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
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 [6]
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:16820452}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is persistently induced 60 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) and
CC leads to the accumulation of 1'-deoxy-ABA.
CC {ECO:0000269|PubMed:16820452}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009812; ATZ52741.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A384JQH2; -.
DR SMR; A0A384JQH2; -.
DR VEuPathDB; FungiDB:Bcin08g03840; -.
DR Proteomes; UP000001798; Chromosome bcin08.
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:0009688; P:abscisic acid biosynthetic process; IMP:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
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.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Virulence.
FT CHAIN 1..527
FT /note="Cytochrome P450 monooxygenase aba2"
FT /id="PRO_0000448416"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 460
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 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 527 AA; 59910 MW; 97E0C79AC4514619 CRC64;
MLLSIKDLSE KYIMLLDVKD LSTLKTTVAV LVTVALIAQV LWKIFFHPLS AFPGPWFNRI
SEIPGSWVIA TGKQHSYYRK LHEKYGPVVR VAPNELSFIG DRAWDDIYGV QKKGPNFEKS
PIFIGAVSPL DGQTGISLAP NEAHTRQRRA LAHVFSNTAL LQQEEIMRSH VDKLVGQLKK
TIAENRPINF SNWYTYTTFD MMGDLCFAEP FGCLDQGGAT EWSTSVINVF KSAAWDQSIR
RVAGVNTWLQ KLMVKLLIPS KAANWRKVHF QNSREKTLRR LADGNREHKD FIYHILKNKE
AKNSLSETEI ILNMVLLISA GTETTASLLT GWTYFICTHP EVYKRLTDEI RGRFNSEQDI
TWETVKDLPY LHATLSEALR LYSPAPANQQ RIVPPGGSVI DGHFVPGKTT VAVAPWAAIN
SSLNFKDPQK FIPERWLGDE RFVNDKLNAS QPFSLGPRGC IGKNLSFFEM RLITSRLLWN
FDVSLVTTGE HGETNKLWDM DGAGKYMKVY QTWNKPDMWV MLKEVPR
