LOX_LYSSC
ID LOX_LYSSC Reviewed; 386 AA.
AC B1HZY7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=L-lactate oxidase {ECO:0000305};
DE Short=LOX {ECO:0000305};
DE EC=1.1.3.- {ECO:0000269|PubMed:34555022};
DE AltName: Full=(S)-2-hydroxy-acid oxidase {ECO:0000305|PubMed:34555022};
DE EC=1.1.3.15 {ECO:0000269|PubMed:34555022};
GN OrderedLocusNames=Bsph_0911 {ECO:0000312|EMBL:ACA38525.1};
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41;
RX PubMed=18296527; DOI=10.1128/jb.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=34555022; DOI=10.1371/journal.pcbi.1009446;
RA Rembeza E., Engqvist M.K.M.;
RT "Experimental and computational investigation of enzyme functional
RT annotations uncovers misannotation in the EC 1.1.3.15 enzyme class.";
RL PLoS Comput. Biol. 17:e1009446-e1009446(2021).
CC -!- FUNCTION: Oxidase that catalyzes the oxidation of a broad range of 2-
CC hydroxyacids in vitro, such as (S)-lactate, 2-hydroxyoctanoate,
CC mandelate, 2-hydroxyoctadecanoate and (S)-2-hydroxyglutarate, to the
CC corresponding 2-oxoacids, with a reduction of O2 to H2O2
CC (PubMed:34555022). May be involved in the utilization of L-lactate as
CC an energy source for growth (By similarity).
CC {ECO:0000250|UniProtKB:O33655, ECO:0000269|PubMed:34555022}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2;
CC Xref=Rhea:RHEA:16789, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:35179, ChEBI:CHEBI:58123; EC=1.1.3.15;
CC Evidence={ECO:0000269|PubMed:34555022};
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:0000269|PubMed:34555022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55869;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyoctanoate + O2 = 2-oxooctanoate + H2O2;
CC Xref=Rhea:RHEA:67940, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:133514, ChEBI:CHEBI:176689;
CC Evidence={ECO:0000269|PubMed:34555022};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=mandelate + O2 = H2O2 + phenylglyoxylate;
CC Xref=Rhea:RHEA:68968, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:25147, ChEBI:CHEBI:36656;
CC Evidence={ECO:0000269|PubMed:34555022};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyoctadecanoate + O2 = 2-oxooctadecanoate + H2O2;
CC Xref=Rhea:RHEA:68964, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17162, ChEBI:CHEBI:76724;
CC Evidence={ECO:0000269|PubMed:34555022};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2-hydroxyglutarate + O2 = 2-oxoglutarate + H2O2;
CC Xref=Rhea:RHEA:27662, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16782, ChEBI:CHEBI:16810;
CC Evidence={ECO:0000269|PubMed:34555022};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q44467};
CC Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:Q44467};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q44467}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; CP000817; ACA38525.1; -; Genomic_DNA.
DR RefSeq; WP_012292672.1; NC_010382.1.
DR EnsemblBacteria; ACA38525; ACA38525; Bsph_0911.
DR KEGG; lsp:Bsph_0911; -.
DR HOGENOM; CLU_020639_6_1_9; -.
DR OMA; FQYEIYL; -.
DR Proteomes; UP000002164; Chromosome.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR Gene3D; 3.20.20.70; -; 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; IPR008259; FMN_hydac_DH_AS.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; Oxidoreductase.
FT CHAIN 1..386
FT /note="L-lactate oxidase"
FT /id="PRO_0000454873"
FT DOMAIN 16..382
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT ACT_SITE 277
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 42
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 95..97
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 124
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 146
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 148
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 174
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 183
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 253
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 275
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 277
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 280
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 308..312
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 332
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
SQ SEQUENCE 386 AA; 41916 MW; 73B3D13F5924B0D2 CRC64;
MTNTTDGDLL LKNITAQAPF PICFADLEKA VAEKIPAGPF GYIRSGAGGE QTLRNNRSAF
EKYSIVPRFL NDVSNVHTSI NLFGKTYPTP LLFAPVGMNG MVHEEGELAA VRAAQQLNMP
YIQSTVSTYA LEDVAEAAPS ATKWFQLYWS TNEEIAFSMA ARAESAGFEA IVLTVDTVML
GWREEDVRNQ FSPLKLGYAK GNYINDPVFM ASLPNDSFES YVQGVLQNVF HPTLNWEHVR
ELKRRTNLPI LLKGILHPED AKLAIVNGVD GIIVSNHGGR QLDGVIGSLD ALPSIVSAVK
GQIPIILDSG VYRGMDALKA LALGADAVAI GRPFIYGLAL EGQQGVERVM TNIYDELKVS
IALAGTTSIE GLRTITLVKN DGMEVK
