FUS7_GIBM7
ID FUS7_GIBM7 Reviewed; 461 AA.
AC W7MWX4; W7MMI5;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, 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:22652150};
GN Name=FUS7 {ECO:0000303|PubMed:22652150}; ORFNames=FVEG_11080;
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=22652150; DOI=10.1016/j.fgb.2012.05.010;
RA Brown D.W., Butchko R.A., Busman M., Proctor R.H.;
RT "Identification of gene clusters associated with fusaric acid, fusarin, and
RT perithecial pigment production in Fusarium verticillioides.";
RL Fungal Genet. Biol. 49:521-532(2012).
CC -!- FUNCTION: Putative aldehyde dehydrogenase; part of the gene cluster
CC that mediates the biosynthesis of the mycotoxin fusarin C
CC (PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are
CC sufficient for fusarin production (By similarity). The other FUS
CC cluster members are not essential for fusarin C biosynthesis (By
CC similarity). {ECO:0000250|UniProtKB:S0ENH1,
CC ECO:0000269|PubMed:22652150}.
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 -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EWG52300.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EWG52301.1; Type=Erroneous gene model prediction; Evidence={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; DS022257; EWG52299.1; -; Genomic_DNA.
DR EMBL; DS022257; EWG52300.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DS022257; EWG52301.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_018758490.1; XM_018900240.1.
DR RefSeq; XP_018758491.1; XM_018900241.1.
DR RefSeq; XP_018758492.1; XM_018900242.1.
DR AlphaFoldDB; W7MWX4; -.
DR SMR; W7MWX4; -.
DR STRING; 117187.FVEG_11080T0; -.
DR EnsemblFungi; FVEG_11080T0; FVEG_11080T0; FVEG_11080.
DR GeneID; 30068616; -.
DR KEGG; fvr:FVEG_11080; -.
DR VEuPathDB; FungiDB:FVEG_11080; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_0_1; -.
DR OMA; NVYINGP; -.
DR OrthoDB; 692580at2759; -.
DR Proteomes; UP000009096; 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 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..461
FT /note="Putative aldehyde dehydrogenase FUS7"
FT /id="PRO_0000437366"
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; 50109 MW; 12596520482AE6E3 CRC64;
MNFDTFHNII AGQHRSARET SSGVNPLDRS SLWPAPVATA NDVEEAVRSA QEAFPAWSQK
TYKQRTELLE KFADLYLAHA NEFCQLIATE CGRTAGNAAI EVYFAAQWLR YPSKYEISQE
ITEDDKKTSI VTQEPLGVVA AICPWNFPLM LALGKIAPAL ATGNCVILKP SPFTPYSSLK
LVELAQQVFP PSVLQVLHGH DDLGPMLVKH SRIQKITFTG STATGKQILR DAAETMKRVT
LETAGNNASI ILPDVNIKAV IPQLAGGLWF NAGQVCIATR RMYIHQDIFE EVVAQLAEAS
KDLTSSIEPI QNEMQLVRLK QALADANAAG YELLSLGKTE AAEGFFIRPT IIKNPPPDAH
AVQQENFGPI VSCIKFSSLD EAIFLANNSD TGLAASVWSG DISAAKRVAA KLEAGNVYIN
GPPQPDPYVP FGGQKQSGLG VEYGLPGLLS FCQTKSTYVY K
