ABL5_LEPMJ
ID ABL5_LEPMJ Reviewed; 551 AA.
AC E5A7D6;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Cytochrome P450 monooxygenase abl5 {ECO:0000303|PubMed:31034868};
DE EC=1.-.-.- {ECO:0000305|PubMed:31034868};
DE AltName: Full=Abscisic acid biosynthesis cluster protein 5 {ECO:0000303|PubMed:31034868};
GN Name=abl5 {ECO:0000303|PubMed:31034868}; ORFNames=LEMA_P087700.1;
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, AND FUNCTION.
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). The cytochrome monooxygenase abl5 seems
CC not essential for the biosynthesis of ABA and its function remains to
CC be identified (PubMed:31034868). {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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-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; CBX99531.1; -; Genomic_DNA.
DR RefSeq; XP_003843010.1; XM_003842962.1.
DR AlphaFoldDB; E5A7D6; -.
DR SMR; E5A7D6; -.
DR STRING; 985895.E5A7D6; -.
DR EnsemblFungi; CBX99531; CBX99531; LEMA_P087700.1.
DR GeneID; 13289207; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_5_11_1; -.
DR InParanoid; E5A7D6; -.
DR OMA; FINTIMD; -.
DR OrthoDB; 825914at2759; -.
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; 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; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..551
FT /note="Cytochrome P450 monooxygenase abl5"
FT /id="PRO_0000448420"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 495
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 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 551 AA; 61894 MW; 7D5BE4355B2230AB CRC64;
MDSVRTFEAC FLSTAAEITF FLKNITTTGN RAQSTKVVLN TLTAIVVVWI CYRAVIYPKF
ISSLRHLPTA KRKYPLIGYG PAQFANSRGE LFLEMAKAIP NEGLIRFHGF LETENLLLTS
PEAIQEVLVK NSYNFIKPRG AKALFDRFLG SEVLFASEGP NHRNSKKHMQ PPFNLSKVKI
LYSMFWDKAV KMSDDIGRSV IPSEKEILVT DVDMHAHNAT LDAVMRALFG EKIEKSPYKH
EILRLLDSVL GGSWDVTAYF MMTAFLPLWT LKLIPGGIND RVNFSSYRLR QSVRAFLNER
KDESGSNKSD DIAMEMANSD YFTDDELVAN LLGLMMAGIE PTAAGFVWIA WYLAIHPDWQ
TKVRNELKAN IAHRFFTDDP TSFDAASVLE SLPILNAVCN EGLRLKPPAP TSNRIAKFDT
TILGHPVKAG TRIFISPFVS NRSEEFWGLT AAMYDPSRWL GDQKSGRKEV YNSRGGAATS
THCGFLPFLH GPRKCIGSIY AQAEMRAFIA CLVGRFEFEM ADKEEEMISA GILTSKPKGG
LKLRLHKVKK W
