LOX_STRIN
ID LOX_STRIN Reviewed; 403 AA.
AC O33655;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=L-lactate oxidase {ECO:0000303|PubMed:10508058};
DE Short=LOX;
DE EC=1.1.3.- {ECO:0000269|PubMed:10508058};
GN Name=lctO {ECO:0000303|PubMed:10508058};
OS Streptococcus iniae (Streptococcus shiloi).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1346;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION.
RC STRAIN=ATCC 29178 / DSM 20576 / CIP 102508 / KCTC 3657 / LMG 14520 / NCIMB
RC 702722 / PW;
RX PubMed=10508058; DOI=10.1128/aem.65.10.4346-4350.1999;
RA Gibello A., Collins M.D., Dominguez L., Fernandez-Garayzabal J.F.,
RA Richardson P.T.;
RT "Cloning and analysis of the L-lactate utilization genes from Streptococcus
RT iniae.";
RL Appl. Environ. Microbiol. 65:4346-4350(1999).
CC -!- FUNCTION: Catalyzes the oxidation of (S)-lactate (L-lactate) to
CC pyruvate, with a reduction of O2 to H2O2. Is likely involved in the L-
CC lactate aerobic metabolism of S.iniae that enables the bacterium to
CC utilize L-lactate as an energy source for growth under aerobic
CC conditions in the absence (or at low concentrations) of glucose.
CC {ECO:0000269|PubMed:10508058}.
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:10508058};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55869;
CC Evidence={ECO:0000305|PubMed:10508058};
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 -!- INDUCTION: Induced during growth on L-lactate. Repressed by glucose.
CC {ECO:0000269|PubMed:10508058}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
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DR EMBL; Y07622; CAA68903.1; -; Genomic_DNA.
DR AlphaFoldDB; O33655; -.
DR SMR; O33655; -.
DR STRING; 1346.DQ08_07070; -.
DR eggNOG; COG1304; Bacteria.
DR BRENDA; 1.1.3.2; 8080.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0050040; F:lactate 2-monooxygenase activity; IEA:UniProtKB-EC.
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; IPR014080; L_lactate_ox.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR TIGRFAMs; TIGR02708; L_lactate_ox; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; Oxidoreductase.
FT CHAIN 1..403
FT /note="L-lactate oxidase"
FT /id="PRO_0000428946"
FT DOMAIN 21..375
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 47
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 99..101
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 128
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 150
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 152
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 178
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 187
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 220
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 246
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 270
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 273
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 301..305
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 325
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
SQ SEQUENCE 403 AA; 44120 MW; B43B6ABCCD95F9EB CRC64;
MENKSEMINA TTIEFKTSSA EGSVDFVNVF DLEKMAQKVI PKGAFGYIAS GAGDTFTLHE
NIRSFNHKLI PHGLKGVENP STEITFIGDK LASPIILAPV AAHKLANEQG EIASAKGVKE
FGTIYTTSSY STTDLPEISQ TLGDSPHWFQ FYYSKDDGIN RHIMDRLKAE GVKSIVLTVD
ATVGGNREVD KRNGFVFPVG MPIVQEYLPN GAGKTMDYVY KATKQALSPK DVEYIAQYSG
LPVYVKGPQC AEDAFRALEA GASGIWVTNH GGRQLDGGPA AFDSLQEVAE SVDRRVPIVF
DSGVRRGQHV FKALASGADL VALGRPVIYG LAMGGSVGTR QVFEKINDEL KMVMQLAGTQ
TIDDVKHFKL RHNPYDSSIP FSPKCFKIRL IFRRPNQILG QFF
