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Database: UniProt
Entry: A0A428NKR8_9HYPO
LinkDB: A0A428NKR8_9HYPO
Original site: A0A428NKR8_9HYPO 
ID   A0A428NKR8_9HYPO        Unreviewed;       295 AA.
AC   A0A428NKR8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=FMN hydroxy acid dehydrogenase domain-containing protein {ECO:0000259|PROSITE:PS51349};
GN   ORFNames=CEP53_012845 {ECO:0000313|EMBL:RSL41289.1};
OS   Fusarium sp. AF-6.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL41289.1, ECO:0000313|Proteomes:UP000287544};
RN   [1] {ECO:0000313|EMBL:RSL41289.1, ECO:0000313|Proteomes:UP000287544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL41289.1,
RC   ECO:0000313|Proteomes:UP000287544};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00024042}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RSL41289.1}.
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DR   EMBL; NKCJ01000466; RSL41289.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428NKR8; -.
DR   STRING; 1325737.A0A428NKR8; -.
DR   Proteomes; UP000287544; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 3.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR008259; FMN_hydac_DH_AS.
DR   PANTHER; PTHR10578:SF107; FMN HYDROXY ACID DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR   Pfam; PF01070; FMN_dh; 2.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287544};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..295
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
SQ   SEQUENCE   295 AA;  32592 MW;  1DD29CC8DC2681AB CRC64;
     MHPSATIWFS PWNLELQTNL YSIAHLHLKS FISFFIPTED NMSVDHRLPD VDINVLTIND
     LKERGSKALP ASVKDYFNEG AMDLLTIRDN EAAFDRYKLR PRTLNDVSSL DTSTTILGTK
     GAAMNNIPMT LSTYTSKTLE DVIAQGKGNP YMMHICFFKD RRKTLEIVKR AEGCIEWLRS
     HTKMEIWLQG ILNPDDVALA IKHGVDGVLI SNHGGRQLDG VPATLDALRA CVPVAKNKIK
     LAVDGGIRRG SDIFKAIALG ADFCMAGRPP LWGLAASPIY VSTFGLLLTV ISPIV
//
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