ABA1_MAGOY
ID ABA1_MAGOY Reviewed; 512 AA.
AC L7HYA8;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Cytochrome P450 monooxygenase ABA1 {ECO:0000303|PubMed:26648962};
DE EC=1.-.-.- {ECO:0000305|PubMed:26648962};
DE AltName: Full=Abscisic acid biosynthesis protein 1 {ECO:0000303|PubMed:26648962};
GN ORFNames=OOU_Y34scaffold00719g26;
OS Magnaporthe oryzae (strain Y34) (Rice blast fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=1143189;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y34;
RX PubMed=22876203; DOI=10.1371/journal.pgen.1002869;
RA Xue M., Yang J., Li Z., Hu S., Yao N., Dean R.A., Zhao W., Shen M.,
RA Zhang H., Li C., Liu L., Cao L., Xu X., Xing Y., Hsiang T., Zhang Z.,
RA Xu J.-R., Peng Y.-L.;
RT "Comparative analysis of the genomes of two field isolates of the rice
RT blast fungus Magnaporthe oryzae.";
RL PLoS Genet. 8:E1002869-E1002869(2012).
RN [2]
RP IDENTIFICATION, INDUCTION, FUNCTION, AND PATHWAY.
RX PubMed=26648962; DOI=10.3389/fpls.2015.01082;
RA Spence C.A., Lakshmanan V., Donofrio N., Bais H.P.;
RT "Crucial roles of abscisic acid biogenesis in virulence of rice blast
RT fungus Magnaporthe oryzae.";
RL Front. Plant Sci. 6:1082-1082(2015).
RN [3]
RP FUNCTION.
RX PubMed=28469630; DOI=10.3389/fpls.2017.00587;
RA Lievens L., Pollier J., Goossens A., Beyaert R., Staal J.;
RT "Abscisic acid as pathogen effector and immune regulator.";
RL Front. Plant Sci. 8:587-587(2017).
CC -!- FUNCTION: Cytochrome P450 monooxygenase involved in the biosynthesis of
CC abscisic acid (ABA), a phytohormone that acts antagonistically toward
CC salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling,
CC to impede plant defense responses (PubMed:26648962). During pathogen-
CC host interaction, ABA plays a dual role in disease severity by
CC increasing plant susceptibility and accelerating pathogenesis in the
CC fungus itself (PubMed:26648962). 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 (By similarity). The cytochrome P450
CC monooxygenase ABA1 might then be involved in the conversion of alpha-
CC ionylideneethane to alpha-ionylideneacetic acid (By similarity). 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 (By similarity). ABA2 is responsible for the hydroxylation of
CC carbon atom C-1' and ABA4 might be involved in the oxidation of the C-
CC 4' carbon atom (By similarity). {ECO:0000250|UniProtKB:Q6H9H9,
CC ECO:0000269|PubMed:26648962}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Hormone biosynthesis. {ECO:0000269|PubMed:26648962}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; JH793878; ELQ35262.1; -; Genomic_DNA.
DR AlphaFoldDB; L7HYA8; -.
DR SMR; L7HYA8; -.
DR Proteomes; UP000011086; Unassembled WGS sequence.
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; ISS:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..512
FT /note="Cytochrome P450 monooxygenase ABA1"
FT /id="PRO_0000448413"
FT TRANSMEM 13..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 458
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"
SQ SEQUENCE 512 AA; 57458 MW; C3A904DA864846C0 CRC64;
MMLQQVADAL ATHWLSGILA IATVYLATSY IIDYRRLRAF PGPPLGSFSY LWLAYNALQG
RQGSIFYEVM KRYRVPEHSF VRIGPNDLMT DSPEVVRHMS SARSTYLRSS WYRTSKLDPS
GDSLLSIMDT AHHDALKAKA GRGYAGRDNR NLESDIDDQL RRLIGLLERK YLSGGGDASS
FRPVDMATTM QYFTLDSITK LAYSSAFGFL DLDTDVYGYI KAIRDAAPPI IVCSEWPLAG
RIFFSPPFLK MFGPTPKDKS GVGKLMGTLR QVVASRFGPD AKDQPDMLGS FVRNGLSQHQ
CEQEVILQIV AGSDTTATAL RGTLLQLCST PMVYLKLQKE IDEAVRSGMV GEGVISQETA
RKLPYLQAVI YEGLRLNPPF TGALMKEVPP GGDEIDGVFI PAGVRIGVSA KGIQMRQDVY
GHDVDVFRPE RWTECDEQRR MRMAANTELV FGYGRWMCAG KNVAFMELNK VYFELLRRFD
FQVVDTKTPV KEESFNVMFS KDMFMKVTKR VL
