ID A0A0B7K7G1_BIOOC Unreviewed; 391 AA.
AC A0A0B7K7G1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=FMN hydroxy acid dehydrogenase domain-containing protein {ECO:0000259|PROSITE:PS51349};
GN ORFNames=BN869_000006948_1 {ECO:0000313|EMBL:CEO50890.1}, IM811_000398
GN {ECO:0000313|EMBL:KAF9758704.1};
OS Bionectria ochroleuca (Gliocladium roseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Bionectriaceae; Clonostachys.
OX NCBI_TaxID=29856 {ECO:0000313|EMBL:CEO50890.1};
RN [1] {ECO:0000313|EMBL:CEO50890.1}
RP NUCLEOTIDE SEQUENCE.
RA Durling Mikael;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF9758704.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S41 {ECO:0000313|EMBL:KAF9758704.1};
RA Wang H.;
RT "High-Quality Genome Resource of Clonostachys rosea strain S41 by Oxford
RT Nanopore Long-Read Sequencing.";
RL Submitted (OCT-2020) 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}.
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DR EMBL; CDPU01000020; CEO50890.1; -; Genomic_DNA.
DR EMBL; JADCTT010000001; KAF9758704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7K7G1; -.
DR Proteomes; UP000616885; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProtKB-ARBA.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR FunFam; 3.20.20.70:FF:000029; L-lactate dehydrogenase; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
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; 2-HYDROXYACID OXIDASE 1; 1.
DR PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
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 Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR000138-
KW 2}; FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRSR:PIRSR000138-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..383
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 278
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 78..80
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 107
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 136
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 138
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 164
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 173
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 254
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 276
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 278
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 281
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 309..313
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 332..333
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 391 AA; 41892 MW; 6E9E5DE229D3FEA6 CRC64;
MADPLTLDEV EAAAKKSLPR KIYDFYASGA DGQRAVARNR YAFSRLFIRP RVLQDVSDVD
TTVELFGVRS ALPVGIAPSA MQRLAGGEGE IDVAKAAAGM GLNLTLSSQS TSSLEDVMQA
KIDIEKGLPG PPFWMQIYLH DDIQKSVPLI RRAEAAGYQA LVLTVDTPVL GNRLAERKEA
VVLPKGLSLP NLEKTTPGAK PQPSINRQFM NVRSAAEAKA LRAAFGSKMH SASLTWERTI
KELRKVTSMK IILKGIMTAE DAALSVQYGA DAIIVSNHGG RQLDETCSTI EALPEVSGAV
NGALPVIIDG GVRTGADVFK CLALGADFVL VGRPALWGLA YDGRRGVETV MHILERELSR
TMALAGVRSV KEISRGMLGV ANRNGFGVSK L
//
