LOX_ROSS0
ID LOX_ROSS0 Reviewed; 370 AA.
AC B7RR92;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 50.
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 ORFNames=RGAI101_4115 {ECO:0000312|EMBL:EEB82810.1};
OS Roseobacter sp. (strain GAI101).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=391589;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAI101;
RA Edwards R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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. Is also able to use glycolate
CC and to a lesser extent 2-hydroxyoctadecanoate as substrate.
CC {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=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=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 -!- 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 -!- 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; DS999214; EEB82810.1; -; Genomic_DNA.
DR STRING; 391589.RGAI101_4115; -.
DR EnsemblBacteria; EEB82810; EEB82810; RGAI101_4115.
DR eggNOG; COG1304; Bacteria.
DR HOGENOM; CLU_020639_0_0_5; -.
DR Proteomes; UP000002944; Unassembled WGS sequence.
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.
FT CHAIN 1..370
FT /note="L-lactate oxidase"
FT /id="PRO_0000454875"
FT DOMAIN 8..367
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT ACT_SITE 262
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 34
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 87..89
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 116
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 136
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 138
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 164
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 173
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 238
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 260
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 262
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 265
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 293..297
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 317
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
SQ SEQUENCE 370 AA; 38615 MW; 0F86BC492B4F8809 CRC64;
MESADLRDPD GMPVTLSDFE IDAAGRLSAD LLAYLEGGAE AGQSVTENRA AFGRIGLLPK
LLSPCAGGHT RTTILGKQAP HPIMVAPMAF QNLFHPQGES ATAMAAAAQD ATMVLSCQTS
TPPEDIATIP GRRWFQLYMQ ADHEATMALV TRAVDCGADA LVVTLDAPIN GLRDREVAAG
FTLPDDVRPV MLDVLPQPPR PHLRDGQSVV FDGMMVFAPT ADDLARLIAD SPVPVIVKGC
LRPADATRLI DLGAQGIIVS NHGGRVLDTV PAPITQLAAV VDAVAGAVPV YVDGGIRRGS
DVFKALALGA QAVLVGRPVM HGLIVDGPRG ASQVLRRLRD ELEVTMALCG CATVADITPD
LLTGFSGTGS
