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Database: UniProt
Entry: A0A3A9K2H5_9THEO
LinkDB: A0A3A9K2H5_9THEO
Original site: A0A3A9K2H5_9THEO 
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
//
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