LOX_ALIDK
ID LOX_ALIDK Reviewed; 365 AA.
AC F4G5A4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
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=Glycolate oxidase {ECO:0000305|PubMed:34555022};
DE EC=1.1.3.15 {ECO:0000269|PubMed:34555022};
GN OrderedLocusNames=Alide2_0580 {ECO:0000312|EMBL:AEB82996.1};
OS Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Alicycliphilus.
OX NCBI_TaxID=596154;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601;
RX PubMed=21742888; DOI=10.1128/jb.00365-11;
RA Oosterkamp M.J., Veuskens T., Plugge C.M., Langenhoff A.A., Gerritse J.,
RA van Berkel W.J., Pieper D.H., Junca H., Goodwin L.A., Daligault H.E.,
RA Bruce D.C., Detter J.C., Tapia R., Han C.S., Land M.L., Hauser L.J.,
RA Smidt H., Stams A.J.;
RT "Genome Sequences of Alicycliphilus denitrificans Strains BC and K601T.";
RL J. Bacteriol. 193:5028-5029(2011).
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: Catalyzes the oxidation of (S)-lactate (L-lactate) to
CC pyruvate, with a reduction of O2 to H2O2. To a lesser extent is also
CC able to use glycolate as substrate. {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 -!- CATALYTIC ACTIVITY:
CC Reaction=glycolate + O2 = glyoxylate + H2O2; Xref=Rhea:RHEA:25311,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:36655; EC=1.1.3.15;
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; CP002657; AEB82996.1; -; Genomic_DNA.
DR RefSeq; WP_013517511.1; NC_015422.1.
DR STRING; 596154.Alide2_0580; -.
DR EnsemblBacteria; AEB82996; AEB82996; Alide2_0580.
DR KEGG; adk:Alide2_0580; -.
DR eggNOG; COG1304; Bacteria.
DR HOGENOM; CLU_020639_0_0_4; -.
DR OMA; AWSWEKI; -.
DR Proteomes; UP000007938; 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 CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
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 Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; Oxidoreductase; Reference proteome.
FT CHAIN 1..365
FT /note="L-lactate oxidase"
FT /id="PRO_0000454874"
FT DOMAIN 6..365
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT ACT_SITE 261
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 32
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 85..87
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 114
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 135
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 137
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 163
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 237
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 259
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 261
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 264
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 292..296
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 316
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
SQ SEQUENCE 365 AA; 38409 MW; B410189AAFF136DC CRC64;
MSPSDRIPPG VWNAIDYERL APQAMDAGRH AYVAGGCGWD ATVAANRAAF AGWAVLPRLL
RDVRAGHTRL QLAGMDLPHP LLLAPVAHQR LAHPDAEIAT ARAAQATGSC LVASTLSSCT
LEDIAAASGP ARWFQLYLQP EREHSLDLLR RAEAAGYRAI VLTLDASIQL ASRGALQAGF
AMPADCVSAN LARYPQPAPA QPAAGESRIF QGAMRHAPRW DDLRWLLAST RLPVWIKGVL
HPEDARELQA AGAAGLIVSN HGGRSLDGAP ASLRMLPALR TAVGAGYPLL LDGGVRSGQD
AFKALALGAD AVLVGRLQVY ALAVAGALGV AHMLQMLVEE LHACMAQAGC ARLSDITHDT
LTPSC
