ID   SAN2_FUSV7              Reviewed;         370 AA.
AC   C7ZBE5;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Aldo-keto reductase NECHADRAFT_45914 {ECO:0000303|PubMed:26936154};
DE            EC=1.1.1.- {ECO:0000305|PubMed:26936154};
DE   AltName: Full=Sansalvamide biosynthesis cluster protein NECHADRAFT_45914 {ECO:0000303|PubMed:26936154};
GN   ORFNames=NECHADRAFT_45914;
OS   Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS   45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex; Fusarium vanettenii.
OX   NCBI_TaxID=660122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX   PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA   Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA   Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA   Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA   Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA   Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA   Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA   Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA   VanEtten H.D.;
RT   "The genome of Nectria haematococca: contribution of supernumerary
RT   chromosomes to gene expansion.";
RL   PLoS Genet. 5:E1000618-E1000618(2009).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=26936154; DOI=10.1007/s00294-016-0584-4;
RA   Romans-Fuertes P., Sondergaard T.E., Sandmann M.I., Wollenberg R.D.,
RA   Nielsen K.F., Hansen F.T., Giese H., Brodersen D.E., Soerensen J.L.;
RT   "Identification of the non-ribosomal peptide synthetase responsible for
RT   biosynthesis of the potential anti-cancer drug sansalvamide in Fusarium
RT   solani.";
RL   Curr. Genet. 62:799-807(2016).
CC   -!- FUNCTION: Aldo-keto reductase; part of the gene cluster that mediates
CC       the biosynthesis of sansalvamide, a cyclic pentadepsipeptide that shows
CC       promising results as potential anti-cancer drug (PubMed:26936154). The
CC       nonribosmal peptide synthetase NRPS30 produces sansalvamide by
CC       incorporating successively one phenylalanine, one leucine, one alpha-
CC       hydroxyisocaproic acid (HICA), one valine and one leucine before
CC       sansalvamide is released from by cyclization by the terminal C domain
CC       of NRPS30 (PubMed:26936154). The HICA residue is probably provided by
CC       reduction of alpha-ketoisocaproate by the cluster-specific aldo-keto
CC       reductase (NECHADRAFT_45914) (Probable). {ECO:0000269|PubMed:26936154,
CC       ECO:0000305|PubMed:26936154}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:26936154}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; GG698914; EEU38724.1; -; Genomic_DNA.
DR   RefSeq; XP_003044437.1; XM_003044391.1.
DR   AlphaFoldDB; C7ZBE5; -.
DR   SMR; C7ZBE5; -.
DR   STRING; 660122.C7ZBE5; -.
DR   EnsemblFungi; NechaT45914; NechaP45914; NechaG45914.
DR   GeneID; 9670749; -.
DR   KEGG; nhe:NECHADRAFT_45914; -.
DR   eggNOG; KOG1575; Eukaryota.
DR   HOGENOM; CLU_023205_2_0_1; -.
DR   InParanoid; C7ZBE5; -.
DR   OMA; EREMIKY; -.
DR   OrthoDB; 1383971at2759; -.
DR   Proteomes; UP000005206; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   SUPFAM; SSF51430; SSF51430; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..370
FT                   /note="Aldo-keto reductase NECHADRAFT_45914"
FT                   /id="PRO_0000450717"
FT   ACT_SITE        83
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT   BINDING         78
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O43488"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT   BINDING         204..205
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O43488"
FT   BINDING         230
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O43488"
FT   BINDING         259..269
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O43488"
FT   BINDING         333..341
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O43488"
SQ   SEQUENCE   370 AA;  41890 MW;  03EC40A1EB31FB44 CRC64;
     MSKTSVDKLL RIPQSLRDSI SRTRVDYRHL GNCGLRVSNP ILGGLHIGNS RWLPWVLNEE
     DAMPILKAAY DRGINTWDTA NVYSNGESEK VIAKALRKYN IPRSKVILMT KCYRVVCDSE
     NFDPGSGVTM HHELADKSKD YVNQWGLSRA AIFNAVEASL ERLGTHYIDI FQIHRFDPTV
     PIAETMSALN DLVKAGMVRY LGASSMWTYQ FAAMQNLAHA KGWTKFVSMQ NHYNLIYREE
     EREMIRYCND TGVGLIPWAP LASGRLARRP SQQSVSIRAS NSRNGSIYEA DDSNTDKIVS
     RVEEIAVKRN WPMSHVALAW LNKRVTAPII GFSTVQRIEE ALAAVGKELS EDEERYLEEL
     YAPRPIQGHS