ID A0A2Y9C9T8_9FIRM Unreviewed; 338 AA.
AC A0A2Y9C9T8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=L-lactate oxidase {ECO:0000256|ARBA:ARBA00029513};
GN ORFNames=A8806_103264 {ECO:0000313|EMBL:PWJ30857.1},
GN SAMN05216536_103264 {ECO:0000313|EMBL:SSA55018.1};
OS Faecalicatena orotica.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Faecalicatena.
OX NCBI_TaxID=1544 {ECO:0000313|EMBL:SSA55018.1, ECO:0000313|Proteomes:UP000251306};
RN [1] {ECO:0000313|EMBL:SSA55018.1, ECO:0000313|Proteomes:UP000251306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NLAE-zl-C242 {ECO:0000313|EMBL:SSA55018.1,
RC ECO:0000313|Proteomes:UP000251306};
RA Cai Z.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWJ30857.1, ECO:0000313|Proteomes:UP000245845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NLAE-zl-C242 {ECO:0000313|EMBL:PWJ30857.1,
RC ECO:0000313|Proteomes:UP000245845};
RA Kelly W.;
RT "The Hungate 1000. A catalogue of reference genomes from the rumen
RT microbiome.";
RL Submitted (MAY-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}.
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DR EMBL; QGDL01000003; PWJ30857.1; -; Genomic_DNA.
DR EMBL; UETE01000003; SSA55018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Y9C9T8; -.
DR OrthoDB; 9770452at2; -.
DR Proteomes; UP000245845; Unassembled WGS sequence.
DR Proteomes; UP000251306; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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 Isomerase {ECO:0000313|EMBL:SSA55018.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000245845}.
FT DOMAIN 47..338
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 338 AA; 36244 MW; AC492F6808B1EEC8 CRC64;
MEYSEVIKNA RTCIGPYCKA CNVCNGAVCK NTMPGPGAKG VGDLAVRNYT KWQEVRINMD
TICEQKPVNT EITLFGKKFS SPFFAGPVGA VKLHYGDKYT DQEYNDILVS SCAQNGIAAF
TGDGTNYQVM IEATKAISNF DGMGIPTVKP WDLGTIREKM ELVKKSGAFA VAMDIDAAGL
PFLQNLNPPA GSKSVEELKE IVKMAEIPFI LKGIMTPKGA LKAKEAGVQG IVVSNHGGRV
LDQCPSTAEV LPFIVEAVGS DMKVFVDGGI RTGTDVFKAL ALGADAVLIA RPFVTAVYGG
QEEGVAAYVQ KIQAELKDTM AMCGAFSLDE IQKDMIWK
//
