ID A0A4T0WEC4_9PEZI Unreviewed; 412 AA.
AC A0A4T0WEC4;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 08-OCT-2025, entry version 19.
DE SubName: Full=Putative lactate 2-monooxygenase PB1A11.03 {ECO:0000313|EMBL:TID04449.1};
GN ORFNames=CH35J_002583 {ECO:0000313|EMBL:TID04449.1};
OS Colletotrichum higginsianum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=80884 {ECO:0000313|EMBL:TID04449.1, ECO:0000313|Proteomes:UP000305883};
RN [1] {ECO:0000313|EMBL:TID04449.1, ECO:0000313|Proteomes:UP000305883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF305635-RFP {ECO:0000313|EMBL:TID04449.1,
RC ECO:0000313|Proteomes:UP000305883};
RX PubMed=31028389; DOI=.1093/gbe/evz087;
RA Tsushima A., Gan P., Kumakura N., Narusaka M., Takano Y., Narusaka Y.,
RA Shirasu K.;
RT "Genomic Plasticity Mediated by Transposable Elements in the Plant
RT Pathogenic Fungus Colletotrichum higginsianum.";
RL Genome Biol. Evol. 11:1487-1500(2019).
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:TID04449.1}.
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DR EMBL; MWPZ01000002; TID04449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4T0WEC4; -.
DR OrthoDB; 25826at2759; -.
DR Proteomes; UP000305883; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR CDD; cd03332; LMO_FMN; 1.
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 InterPro; IPR037350; LMO_FMN.
DR PANTHER; PTHR10578:SF86; DEPENDENT DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G02720)-RELATED; 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 Monooxygenase {ECO:0000313|EMBL:TID04449.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 29..404
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 299
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 55
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 108..110
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 137
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 159
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 161
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 187
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 196
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 275
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 297
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 299
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 302
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 330..334
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 353..354
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 412 AA; 44347 MW; 709D0C907295873A CRC64;
MADSGDGDER APYSAYAVSI YQNGIISGKM PIVTTDPNGL QAQAKKALGP EAFGYVFGGA
GELSTMDANR LAFRQWKIVP RFLRPSNPRD LRTELFGVTY ESPVLMAPIG VQGIFHADKE
TGLAAACAEL RIPYTLSTAA TSTIEEVAEA CGDQHRWFQL YWPMDDEITG SILRRAKANS
YKVLVVTLDT VTLAWRPTDL DQAYLPMVTG TGNSVAFSDP VFRKKFAEQN DGDAIEDNLI
SASRYWISEA FPGDHHRWED LALLKKHWDG PIVLKGVLSV DDARLAVEHG MSGIIVSNHG
GRQLDGGVAS LEMLPDIVEA VGDKLTVMFD SGIRTGADIV KALALGAKAV FVGRPAIYGL
GIAGKEGAKA VIAGLLADLD LTMGLAGFKS ISDLKPPILR HVRYGGDVKA NL
//
