FDB28_GIBM7
ID FDB28_GIBM7 Reviewed; 322 AA.
AC W7MSH6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 23-FEB-2022, entry version 31.
DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase FVEG_12628 {ECO:0000303|PubMed:19302487};
DE EC=1.1.1.- {ECO:0000305|PubMed:19302487};
DE AltName: Full=Fusarium detoxification of benzoxazolinone cluster 2 protein FVEG_12628 {ECO:0000303|PubMed:19302487};
DE Short=FDB2 cluster protein FVEG_12628 {ECO:0000303|PubMed:19302487};
GN ORFNames=FVEG_12628;
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.
RX PubMed=12788712; DOI=10.1128/aem.69.6.3165-3169.2003;
RA Glenn A.E., Meredith F.I., Morrison W.H. III, Bacon C.W.;
RT "Identification of intermediate and branch metabolites resulting from
RT biotransformation of 2-benzoxazolinone by Fusarium verticillioides.";
RL Appl. Environ. Microbiol. 69:3165-3169(2003).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19302487; DOI=10.1111/j.1365-2672.2009.04246.x;
RA Glenn A.E., Bacon C.W.;
RT "FDB2 encodes a member of the arylamine N-acetyltransferase family and is
RT necessary for biotransformation of benzoxazolinones by Fusarium
RT verticillioides.";
RL J. Appl. Microbiol. 107:657-671(2009).
RN [5]
RP FUNCTION, AND INDUCTION.
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: 3-hydroxyacyl-CoA dehydrogenase; part of the Fusarium
CC detoxification of benzoxazolinone cluster 2 (FDB2) involved in the
CC degradation of benzoxazolinones produced by the host plant
CC (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2
CC benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-
CC 3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due
CC to their inherent instability once released, spontaneously degrade to
CC the more stable corresponding benzoxazolinones, 6-methoxy-2-
CC benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively
CC (PubMed:11876429). The first step in the detoxification of
CC benzoxazolinones involves the hydrolysis of the cyclic ester bond of
CC benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to
CC aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to
CC convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-
CC 2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2
CC cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols
CC via N-malonylation to non-toxic malonamic acids (PubMed:19302487,
CC PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl)
CC malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl)
CC malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The
CC duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant
CC function for hydrolyzing the lactone moiety in the BOA molecule
CC (Probable). The roles of the amidases an other enzymes encoded by the 2
CC FDB clusters have not been identified so far (Probable).
CC {ECO:0000269|PubMed:11876429, ECO:0000269|PubMed:12788712,
CC ECO:0000269|PubMed:19302487, ECO:0000269|PubMed:26808652,
CC ECO:0000305|PubMed:26808652}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced in response to 2-benzoxasolinone (BOA)
CC exposure. {ECO:0000269|PubMed:26808652}.
CC -!- DISRUPTION PHENOTYPE: Does not affect tolerance to 2-benzoxazolinone
CC (BOA). {ECO:0000269|PubMed:19302487}.
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 3-hydroxyacyl-CoA dehydrogenase family.
CC {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; DS022261; EWG54408.1; -; Genomic_DNA.
DR RefSeq; XP_018760599.1; XM_018901978.1.
DR STRING; 117187.FVEG_12628T0; -.
DR EnsemblFungi; FVEG_12628T0; FVEG_12628T0; FVEG_12628.
DR GeneID; 30070058; -.
DR KEGG; fvr:FVEG_12628; -.
DR VEuPathDB; FungiDB:FVEG_12628; -.
DR eggNOG; KOG2305; Eukaryota.
DR HOGENOM; CLU_009834_0_1_1; -.
DR OMA; VIGMGWA; -.
DR OrthoDB; 840631at2759; -.
DR Proteomes; UP000009096; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Membrane; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..322
FT /note="3-hydroxyacyl-CoA dehydrogenase FVEG_12628"
FT /id="PRO_0000454622"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 151
FT /note="For hydroxyacyl-coenzyme A dehydrogenase activity"
FT /evidence="ECO:0000250|UniProtKB:P40939"
FT SITE 139
FT /note="Important for hydroxyacyl-coenzyme A dehydrogenase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P40939"
SQ SEQUENCE 322 AA; 35108 MW; 6491F07B0B45C9B0 CRC64;
MTQEIRTVAI VGCGVIGMGW AVLFLSRGLK VIISDPMEGA ENALKGYFEQ SRSYLEGFGD
YDKLVSNYEF VHDIASRLAE ADLIQENGPE RLEFKRGLIA TLDKYARPGV VIASSSSGLP
SSEFIQQCKQ DSTRVLIGHP FNPPHLIPLV EVVPHPGTSS ESVNTALNFY RSVGKRPILL
HHEVPGFVSN RLQAAINNEA YSLISRGIVS AEDLDAAVTS GPGLRWALTG PIATNALGGG
GGPEGFSQRM ERLGPAIRGW EDDILKHRFD WSEQRMSALQ ESVNKSLGAV KWDQLVEERD
LVLLQLLAAK QKMASMSTPS GH
