FUS7_GIBF5
ID FUS7_GIBF5 Reviewed; 461 AA.
AC S0ENH1;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Putative aldehyde dehydrogenase FUS7 {ECO:0000250|UniProtKB:O34660};
DE EC=1.2.1.3 {ECO:0000250|UniProtKB:O34660};
DE AltName: Full=Fusarin biosynthesis protein 7 {ECO:0000303|PubMed:23932525};
GN Name=FUS7 {ECO:0000303|PubMed:23932525}; ORFNames=FFUJ_10052;
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
RN [2]
RP INDUCTION.
RX PubMed=20572938; DOI=10.1111/j.1365-2958.2010.07263.x;
RA Wiemann P., Brown D.W., Kleigrewe K., Bok J.W., Keller N.P., Humpf H.U.,
RA Tudzynski B.;
RT "FfVel1 and FfLae1, components of a velvet-like complex in Fusarium
RT fujikuroi, affect differentiation, secondary metabolism and virulence.";
RL Mol. Microbiol. 77:972-994(2010).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23932525; DOI=10.1016/j.chembiol.2013.07.004;
RA Niehaus E.M., Kleigrewe K., Wiemann P., Studt L., Sieber C.M.,
RA Connolly L.R., Freitag M., Gueldener U., Tudzynski B., Humpf H.U.;
RT "Genetic manipulation of the Fusarium fujikuroi fusarin gene cluster yields
RT insight into the complex regulation and fusarin biosynthetic pathway.";
RL Chem. Biol. 20:1055-1066(2013).
CC -!- FUNCTION: Putative aldehyde dehydrogenase; part of the gene cluster
CC that mediates the biosynthesis of the mycotoxin fusarin C
CC (PubMed:23932525). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are
CC sufficient for fusarin production (PubMed:23932525). The other FUS
CC cluster members are not essential for fusarin C biosynthesis
CC (PubMed:23932525). {ECO:0000269|PubMed:23932525}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:O34660};
CC -!- INDUCTION: Expressed under high amounts of nitrogen via regulation by
CC GLN1 (PubMed:23932525). Moreover, components of the fungal-specific
CC velvet complex VEL1, VEL2 and LAE1 act also as positive regulators of
CC expression (PubMed:20572938, PubMed:23932525). Finally, expression is
CC induced under acidic conditions in a PACC-independent manner
CC (PubMed:23932525). {ECO:0000269|PubMed:20572938,
CC ECO:0000269|PubMed:23932525}.
CC -!- DISRUPTION PHENOTYPE: Does not alter fusarin C production
CC (PubMed:23932525). {ECO:0000269|PubMed:23932525}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; HF679031; CCT74093.1; -; Genomic_DNA.
DR AlphaFoldDB; S0ENH1; -.
DR SMR; S0ENH1; -.
DR STRING; 1279085.S0ENH1; -.
DR EnsemblFungi; CCT74093; CCT74093; FFUJ_10052.
DR VEuPathDB; FungiDB:FFUJ_10052; -.
DR HOGENOM; CLU_005391_0_0_1; -.
DR Proteomes; UP000016800; Chromosome 9.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR CDD; cd07106; ALDH_AldA-AAD23400; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR044086; FUS7/LUC3-like.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
PE 2: Evidence at transcript level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..461
FT /note="Putative aldehyde dehydrogenase FUS7"
FT /id="PRO_0000437365"
FT ACT_SITE 242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT BINDING 220..225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O34660"
SQ SEQUENCE 461 AA; 49998 MW; 850F333C1B1BB1B8 CRC64;
MSFDTFYNII TGQPRSARET TSGVNPLDRS SLWPAPVATG NDVEEAVRSA QEAFPAWSEK
TYKQRTELLE KFADLYLVHA NEFCQLIATE CGRTAGNAAI EVYVAAQWLR YPSKYEIPEE
VTEDEKKTSI VTHEPLGVVA AICPWNFPLM LALGKIAPAL ATGNCVILKP SPFTPYSSLK
LVELAQQVFP PSVLQVLHGH DDLGPMLVKH PRIQKITFTG STTTGKQILR DAAETMKRVT
LETAGNNASI ILPDVNIEAV IPQLAGGLWF NAGQVCIATR RMYIHQDIFD EAVAQLAEAS
KDLASGMEPI QNEMQLVRLQ QALSDANAAG CELLSLGKTE AAEGFFIQPT ILKSPPPDAD
VVQQENFGPI VSCIKFSSLD EAISLANNSD TGLAASVWSS DVSAARRVAA KLEVGNVYIN
GPPQPDPYVP FGGHKQSGLG VEYGLPGLLS FCQTKSTYLY K
