ABL2_LEPMJ
ID ABL2_LEPMJ Reviewed; 555 AA.
AC E5A7D8;
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 abl2 {ECO:0000303|PubMed:31034868};
DE EC=1.-.-.- {ECO:0000305|PubMed:31034868};
DE AltName: Full=Abscisic acid biosynthesis cluster protein 2 {ECO:0000303|PubMed:31034868};
GN Name=abl2 {ECO:0000303|PubMed:31034868}; ORFNames=LEMA_P087720.1;
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, 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:Q5K0D9,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; FP929136; CBX99533.1; -; Genomic_DNA.
DR RefSeq; XP_003843012.1; XM_003842964.1.
DR AlphaFoldDB; E5A7D8; -.
DR SMR; E5A7D8; -.
DR EnsemblFungi; CBX99533; CBX99533; LEMA_P087720.1.
DR GeneID; 13289264; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_14_11_1; -.
DR InParanoid; E5A7D8; -.
DR OMA; WSTSVIN; -.
DR OrthoDB; 1247045at2759; -.
DR Proteomes; UP000002668; Genome.
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 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..555
FT /note="Cytochrome P450 monooxygenase abl2"
FT /id="PRO_0000448419"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 489
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 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 555 AA; 62787 MW; 1EE75443D11E6F0A CRC64;
MFGDTSEVLP VAEGKGSSWP TQRLTMTVAF ADGDRTWSFD LFSKLAGLAL LSFAALFIQR
RLFHPLRKYP GPWLNSLSEI PAAIALASGR QQAYYRRLHS RYATSSGTIV RVAPNELSFV
DPNAWQDIYN RKPPHMEKHP VFIGAVAKVG GAVGISMAPL ATKDHSRHRR ALGYSFATSA
LVEQQEIILK QVRNLISHLK VFARKEKAID MTDWYTYTTF DLMGDLVFGQ PFGCLDGEGP
TEWSRAIIHV FVSGAWEQAI RRVAGVNTWA ESVLKKILIP KKVALWRRLH FAKSRETTLK
RIKDGQRNHK DLMYFLLKNK EARQNLSDLE IMINMVLLVS AGSETTASTL TAWTYFVCTN
RSVHRRLLKE IRGNFKTAEH IVWENTQPDQ LPYLEATIHE ALRLVPPPAS SQQRVVPPGG
AVICGERIPE GYAVAVPPVA VTHLDINFAD PTGFHPERWL PRDDDDWDEK FAKDKLGASQ
PFSLGPRACL GKTLAYFELR LILASVLWNF DIDLAHAKET KDLWTMEDDM KYLKGYLTWV
KPPLPVRLQE VKREA
