ABL1_LEPMJ
ID ABL1_LEPMJ Reviewed; 569 AA.
AC E5A7E1;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Cytochrome P450 monooxygenase abl1 {ECO:0000303|PubMed:31034868};
DE EC=1.-.-.- {ECO:0000305|PubMed:31034868};
DE AltName: Full=Abscisic acid biosynthesis cluster protein 1 {ECO:0000303|PubMed:31034868};
GN Name=abl1 {ECO:0000303|PubMed:31034868}; ORFNames=LEMA_P087750.1;
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
RN [2]
RP IDENTIFICATION, INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=31034868; DOI=10.1016/j.fgb.2019.04.015;
RA Darma R., Lutz A., Elliott C.E., Idnurm A.;
RT "Identification of a gene cluster for the synthesis of the plant hormone
RT abscisic acid in the plant pathogen Leptosphaeria maculans.";
RL Fungal Genet. Biol. 130:62-71(2019).
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:31034868). The first step of the pathway catalyzes the reaction
CC from farnesyl diphosphate to alpha-ionylideneethane performed by the
CC alpha-ionylideneethane synthase abl3 via a three-step reaction
CC mechanism involving 2 neutral intermediates, beta-farnesene and
CC allofarnesene (By similarity). The cytochrome P450 monooxygenase abl1
CC might then be involved in the conversion of alpha-ionylideneethane to
CC alpha-ionylideneacetic acid (By similarity). Alpha-ionylideneacetic
CC acid is further converted to abscisic acid in 2 steps involving the
CC cytochrome P450 monooxygenase abl2 and the short-chain
CC dehydrogenase/reductase abl4, 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). Abl2 is responsible for the hydroxylation of
CC carbon atom C-1' and abl4 might be involved in the oxidation of the C-
CC 4' carbon atom (By similarity). {ECO:0000250|UniProtKB:Q6H9H9,
CC ECO:0000269|PubMed:31034868}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Hormone biosynthesis. {ECO:0000269|PubMed:31034868}.
CC -!- INDUCTION: Expression is induced during the early biotrophic stage of
CC development (PubMed:31034868). Expression is positively regulated by
CC the ABA cluster-specific transcription regulator abl7
CC (PubMed:31034868). {ECO:0000269|PubMed:31034868}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of abscisic acid (ABA)
CC (PubMed:31034868). Does not affect sporulation, pycnidiospore
CC germination nor fungal growth rates in vitro, and does not alter the
CC pathogenicity of L.maculans (PubMed:31034868).
CC {ECO:0000269|PubMed:31034868}.
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; FP929136; CBX99536.1; -; Genomic_DNA.
DR RefSeq; XP_003843015.1; XM_003842967.1.
DR AlphaFoldDB; E5A7E1; -.
DR SMR; E5A7E1; -.
DR EnsemblFungi; CBX99536; CBX99536; LEMA_P087750.1.
DR GeneID; 13289208; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_14_0_1; -.
DR InParanoid; E5A7E1; -.
DR OMA; CETEGLF; -.
DR OrthoDB; 467733at2759; -.
DR Proteomes; UP000002668; Genome.
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 Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Virulence.
FT CHAIN 1..569
FT /note="Cytochrome P450 monooxygenase abl1"
FT /id="PRO_0000448414"
FT BINDING 464
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 569 AA; 64607 MW; E2CB3735A3D78A22 CRC64;
MYCDSFFMSR LLSLAQLSGS SWSSICLVCV TSLVFWRIKI AVTQYIRLRH IPSPSIFAAV
SYIWLARTTY SGKQYWIHRD LHRQHGPLVR IGPNEITTDD PEILKKIASS GSTYSRGTWY
LTGRFNPYHD NLFTILDPFA HKKAKTRSMP AYLGRDTPGL EVIINDKVKQ LISILQRRYL
AVLPGQDPPL VDLGLISNYF TMDVITHLAF GHQVGYLQDE KDHYNFLGSV RKLWPQMSTS
ADVPWIRNIL FSRPVLRFLG PKHTDKKGFG ALMGAAKQHV DRRFDSGEER KHDMLESLMK
RGFTRQECEI EGLFLLLSGT ESTACAIRQI LVHVITAPSV YAKLKQEIDS TCQGRGISYP
IQLAEAKRLP YLQAVIYEGI RMRPPLLGLF PKVVPEPGET FHGQFIPAGT SICTNGSSLL
RSKSLFGADA DLYNPGRFME LSKERREEME RNVELAFGHG QWMCAGKTIA FMELNKVVFE
KHCQFFRAFD MQLHSPLKPC EVESYAGLIA KPPAKSSDLS MISRVTDMSR GINPCYRYPP
QYRTHLKTHM LNVPSGSNFI RMPIVLPST
