ID A0A426JY21_9PSEU Unreviewed; 386 AA.
AC A0A426JY21;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 02-APR-2025, entry version 20.
DE SubName: Full=Lactate 2-monooxygenase {ECO:0000313|EMBL:RRO18012.1};
GN ORFNames=EIL87_07015 {ECO:0000313|EMBL:RRO18012.1};
OS Saccharopolyspora rhizosphaerae.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=2492662 {ECO:0000313|EMBL:RRO18012.1, ECO:0000313|Proteomes:UP000274515};
RN [1] {ECO:0000313|EMBL:RRO18012.1, ECO:0000313|Proteomes:UP000274515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H219 {ECO:0000313|EMBL:RRO18012.1,
RC ECO:0000313|Proteomes:UP000274515};
RA Intra B., Euanorasetr J., Take A., Inahashi Y., Mori M., Panbangred W.,
RA Matsumoto A.;
RT "Saccharopolyspora rhizosphaerae sp. nov., an actinomycete isolated from
RT rhizosphere soil in Thailand.";
RL Submitted (NOV-2018) 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:RRO18012.1}.
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DR EMBL; RSAA01000007; RRO18012.1; -; Genomic_DNA.
DR RefSeq; WP_125089365.1; NZ_RSAA01000007.1.
DR AlphaFoldDB; A0A426JY21; -.
DR OrthoDB; 9770452at2; -.
DR Proteomes; UP000274515; 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 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; IPR037350; LMO_FMN.
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; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000138-2};
KW FMN {ECO:0000256|PIRSR:PIRSR000138-2};
KW Monooxygenase {ECO:0000313|EMBL:RRO18012.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000274515}.
FT DOMAIN 18..386
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 283
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 44
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 97..99
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 128
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 150
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 152
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 178
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 187
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 259
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 281
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 283
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 286
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 313..317
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 336..337
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 386 AA; 41386 MW; 8057310B4BB7BE6E CRC64;
MAYGDYQLEI YLNGLSGVLP DLPMEFEELE ERAEAAMSPS VWSYVHGGAG SERTQRANVT
AFDRWGVVPR MFVGATERDL EVDLFGLTLP SPVFMAPIGV LGICGQDGHG DLATARAAAQ
SGVPMVASTL SSDPLEDVAA EFGDTPGFFQ LYTPKDRDLA ESLVRRAEKA GYKGIVVTLD
TWIPGWRPRD LATSNFPQLR GHCLSNYFTD PVFRAGLDTS PEEDPQAAVL RWVSTFGNPL
TWNDLPWLRS LTDLPLIVKG LCHPDDVRRA KDGGVDGIYC STHGGRQADG GLPALEVLPE
VVEAADGMPV LFDSGVRSGA DVIKALALGA TAVGIGRPYA YGLALGGTAG VVHVVRSLLA
EADLIMAVDG YPTLSDLTRD ALRRLR
//
