ID A0A3A9K2H5_9THEO Unreviewed; 339 AA.
AC A0A3A9K2H5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=L-lactate oxidase {ECO:0000256|ARBA:ARBA00029513};
GN ORFNames=DXT63_01660 {ECO:0000313|EMBL:RKL64431.1};
OS Thermoanaerobacteraceae bacterium SP2.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae.
OX NCBI_TaxID=2292448 {ECO:0000313|EMBL:RKL64431.1, ECO:0000313|Proteomes:UP000271566};
RN [1] {ECO:0000313|Proteomes:UP000271566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|Proteomes:UP000271566};
RA Grouzdev D.S., Krutkina M.S., Patutina E.O.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + O2 = H2O2 + pyruvate; Xref=Rhea:RHEA:55868,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16651; Evidence={ECO:0000256|ARBA:ARBA00029324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55869;
CC Evidence={ECO:0000256|ARBA:ARBA00029324};
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:RKL64431.1}.
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DR EMBL; QSNL01000002; RKL64431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9K2H5; -.
DR OrthoDB; 9770452at2; -.
DR Proteomes; UP000271566; Unassembled WGS sequence.
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; 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 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 PIRSF; PIRSF000138; Al-hdrx_acd_dh; 2.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000271566}.
FT DOMAIN 37..339
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 236
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 110
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 151
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 212
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 234
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 236
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 239
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 267..271
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 290..291
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 339 AA; 35429 MW; 0D97A6ABD0573DAF CRC64;
MNMQELKKNA REKMKGYCRV CRVCDGVVCA GEVPGMGGTG TGASFKANVQ ALADVKLNLR
TFHDAKSPDI SCEIFGRKLS MPILAAPITG SEYNMGGAVP EAEFIQMVIS GSKQAGTMGM
CGDGGNPVFY SSGLSAIEKE GGHGIAVIKP RENHKVIEMV KRAQDIGAVA VGMDVDGAGL
VTMALMGQPV GPKNVKELKD IISHTKLPFI LKGIMTVDEA KLAVEAGARA IVVSNHGGRI
LDYTPGVAEV LPAIANTVKG KITIFADGGV RSGVDVLKYL ALGADAVLVG RPIIIGAFGG
GSEGVRLVLD TMAGELKQAM ILTGCSNLEE ITDRVIYRI
//