FDB92_GIBM7
ID FDB92_GIBM7 Reviewed; 471 AA.
AC W7MM11;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Transmembrane transporter FVEG_08292 {ECO:0000303|PubMed:26808652};
DE AltName: Full=Fusarium detoxification of benzoxazolinone cluster 1 protein FVEG_08292 {ECO:0000303|PubMed:26808652};
DE Short=FDB1 cluster protein FVEG_08292 {ECO:0000303|PubMed:26808652};
GN ORFNames=FVEG_08292;
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [2]
RP FUNCTION.
RX PubMed=11876429; DOI=10.1094/mpmi.2002.15.2.91;
RA Glenn A.E., Gold S.E., Bacon C.W.;
RT "Fdb1 and Fdb2, Fusarium verticillioides loci necessary for detoxification
RT of preformed antimicrobials from corn.";
RL Mol. Plant Microbe Interact. 15:91-101(2002).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26808652; DOI=10.1371/journal.pone.0147486;
RA Glenn A.E., Davis C.B., Gao M., Gold S.E., Mitchell T.R., Proctor R.H.,
RA Stewart J.E., Snook M.E.;
RT "Two horizontally transferred xenobiotic resistance gene clusters
RT associated with detoxification of benzoxazolinones by Fusarium species.";
RL PLoS ONE 11:e0147486-e0147486(2016).
CC -!- FUNCTION: Transmembrane transporter; part of the Fusarium
CC detoxification of benzoxazolinone cluster 1 (FDB1) involved in the
CC degradation of benzoxazolinones produced by the host plant
CC (PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone
CC phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA)
CC and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their
CC inherent instability once released, spontaneously degrade to the more
CC stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone
CC (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429).
CC Might be involved in the transport of metabolites of benzoxazolinone
CC degradation (Probable). {ECO:0000269|PubMed:11876429,
CC ECO:0000269|PubMed:26808652, ECO:0000305|PubMed:26808652}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced in response to 2-benzoxazolinone (BOA)
CC exposure. {ECO:0000269|PubMed:26808652}.
CC -!- DISRUPTION PHENOTYPE: Does not affect 2-benzoxazolinone (BOA)
CC degradation. {ECO:0000269|PubMed:26808652}.
CC -!- MISCELLANEOUS: Fusarium verticillioides possesses 2 unlinked loci, FDB1
CC and FDB2, necessary for detoxification of antimicrobial compounds
CC produced by maize, including 2-benzoxazolinone (BOA) (Probable). The
CC FDB2 cluster arose as a duplication of the FDB1 cluster with
CC rearrangement and expansion by incorporating additional genes
CC (Probable). {ECO:0000305|PubMed:26808652}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; DS022252; EWG48580.1; -; Genomic_DNA.
DR RefSeq; XP_018754771.1; XM_018897184.1.
DR EnsemblFungi; FVEG_08292T0; FVEG_08292T0; FVEG_08292.
DR GeneID; 30066034; -.
DR KEGG; fvr:FVEG_08292; -.
DR VEuPathDB; FungiDB:FVEG_08292; -.
DR eggNOG; ENOG502SHQ6; Eukaryota.
DR HOGENOM; CLU_027816_3_1_1; -.
DR OMA; ANLFICT; -.
DR OrthoDB; 570025at2759; -.
DR Proteomes; UP000009096; Chromosome 10.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..471
FT /note="Transmembrane transporter FVEG_08292"
FT /id="PRO_0000454608"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 471 AA; 50821 MW; 8BC2D0FCAED466FF CRC64;
MTIETMLSEE KSQSSDNRNN GSIKVGISSG EVDLESREVF RTGDDVLDFR TVSWQRATIM
FCKINFAMSI LAIPQAISTV GAVGGSLILV GFTSLNVYTA LILGDFRNRH PECHMLADMM
GLIWGMVGRE LVGVQIIVLQ ILITAGGVAT TAVGLNALSN HSQCTVIFGL ASAILVTACS
SVRTFSKLGW ITWFGMITFT VGVLVFTIAV TQQDRPAAAS PTGDFDLGWT AIANPGFVVG
MVSSANLFIC TSGSSMFLPV ISEMRRPQDY RKACLWAGLI VGMLYLVLSL VIYRYCGTWL
SVPAFGSAGP LFKKISYGIS LPGLIIGVGI YQHVAAKYAF VRLLRDSDHL QKNTFTHWGT
WLGINFAFGT AAFIVAEAVP ILNYLLGLAG ALCAAPFSLI FPCLLWMYDF KGYRSGTLIQ
RAQYTIHVLI ALIGLYMVAG TAYAVVVAIK MAFQSGTIAR VFDCADNSGS V
