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Database: UniProt
Entry: R5AYS7_9FIRM
LinkDB: R5AYS7_9FIRM
Original site: R5AYS7_9FIRM 
ID   R5AYS7_9FIRM            Unreviewed;       340 AA.
AC   R5AYS7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=L-lactate oxidase {ECO:0000256|ARBA:ARBA00029513};
GN   ORFNames=BN455_00324 {ECO:0000313|EMBL:CCX47079.1};
OS   Firmicutes bacterium CAG:103.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262999 {ECO:0000313|EMBL:CCX47079.1, ECO:0000313|Proteomes:UP000018290};
RN   [1] {ECO:0000313|EMBL:CCX47079.1, ECO:0000313|Proteomes:UP000018290}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:103 {ECO:0000313|Proteomes:UP000018290};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCX47079.1}.
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DR   EMBL; CAWL010000217; CCX47079.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5AYS7; -.
DR   Proteomes; UP000018290; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:UP000018290}.
FT   DOMAIN          42..340
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         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"
SQ   SEQUENCE   340 AA;  35857 MW;  96FE56834BADA872 CRC64;
     MDYNEVLQRA RARMAPRCKV CPECNGLGCG NTMPGPGSKA PGNGANDNWR AWRRWCLNMD
     TIAPNTPVDT SLELLGRTFS LPVIAAPIGS LRAQFNPEDD IRDYNACCIA AAAQTGIAAS
     FGDGLDARVF PHGCTLSQQY GGIGLPVINP LSMDTIRANL DLANAARPFA VSVVIDSAGL
     PHLKAASPDA GSKTVAELRE LCGYAQMPMI LKGIMTVRGA EKAVEAGAAA IVVSNHGGRV
     LPGSAATADV LPEIADAVGD RVKILVDGGI RSGTDIFRAL ALGADAVMIC RPFLISYYGG
     GMEGIVAYVE KLRAELTDAM YMCGARCLSD ITRDMVREVR
//
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