ID A0A9P4L990_9PLEO Unreviewed; 430 AA.
AC A0A9P4L990;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE SubName: Full=FMN-dependent alpha-hydroxy acid dehydrogenase {ECO:0000313|EMBL:KAF1845974.1};
GN ORFNames=K460DRAFT_366821 {ECO:0000313|EMBL:KAF1845974.1};
OS Cucurbitaria berberidis CBS 394.84.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Cucurbitaria.
OX NCBI_TaxID=1168544 {ECO:0000313|EMBL:KAF1845974.1, ECO:0000313|Proteomes:UP000800039};
RN [1] {ECO:0000313|EMBL:KAF1845974.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 394.84 {ECO:0000313|EMBL:KAF1845974.1};
RG DOE Joint Genome Institute;
RA Haridas S., Albert R., Binder M., Bloem J., Labutti K., Salamov A.,
RA Andreopoulos B., Baker S.E., Barry K., Bills G., Bluhm B.H., Cannon C.,
RA Castanera R., Culley D.E., Daum C., Ezra D., Gonzalez J.B., Henrissat B.,
RA Kuo A., Liang C., Lipzen A., Lutzoni F., Magnuson J., Mondo S., Nolan M.,
RA Ohm R., Pangilinan J., Park H.-J., Ramirez L., Alfaro M., Sun H., Tritt A.,
RA Yoshinaga Y., Zwiers L.-H., Turgeon B.G., Goodwin S.B., Spatafora J.W.,
RA Crous P.W., Grigoriev I.V.;
RL Submitted (JAN-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}.
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:KAF1845974.1}.
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DR EMBL; ML976616; KAF1845974.1; -; Genomic_DNA.
DR RefSeq; XP_040788537.1; XM_040933462.1.
DR AlphaFoldDB; A0A9P4L990; -.
DR GeneID; 63850713; -.
DR OrthoDB; 25826at2759; -.
DR Proteomes; UP000800039; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR FunFam; 3.20.20.70:FF:000132; FMN dependent 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:SF143; FMN-DEPENDENT ALPHA-HYDROXY ACID DEHYDROGENASE PB1A11.03; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000800039}.
FT DOMAIN 37..417
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 312
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 63
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 117..119
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 146
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 169
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 171
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 199
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 208
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 288
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 310
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 312
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 315
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 366..367
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 430 AA; 47210 MW; 2DF3EEEE2594F52F CRC64;
MANEAATQHH PKYQAHKPEQ DAVDYELQTY TRGLDFERPP LTFQASKWEE LACSRLSADS
KGYVYGSAGV RETTDKNRAA FKKWSIVPRR LVKYDGFPDL KTEILGEQLS VPIAMAPVGV
LKIFNPDGEM AATRAAAQEA VPYILSTASS TSIEDVAQAN GVDGQRWYQL YWPSREHDDI
TISLLQRANK AGFTTLFVTL DTYILGWRPS DMDNGYNPFM RADRIGVELG MTDPVFRQQF
KERHGVDVEE KMNSAAPEWM RTIFPGTSKG WEDVEFLKSH WDGPIVLKGI QSIVDAKKAA
EVGVAGIVVS NHGGRQQDGG NSSLGVLPHI VDAVGDKLTI FFDSGIQSGA DIAKALALGA
DCVLVGRPYV YGLALGGEKG VEHVLKSLVG ELELTLHLAG IQSVKKEHLN REALVLEDDL
FNSVKGIGLH
//
