LOX_LACJE
ID LOX_LACJE Reviewed; 408 AA.
AC A0A5N1I561;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 1.
DT 03-AUG-2022, entry version 11.
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=F6H94_08130 {ECO:0000312|EMBL:KAA9320359.1};
OS Lactobacillus jensenii.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=109790;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB246;
RA Mores C.R., Putonti C., Wolfe A.J.;
RT "Draft genome sequence assemblies of isolates from the urinary tract.";
RL Submitted (SEP-2019) 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: Oxidase that catalyzes the oxidation of a broad range of 2-
CC hydroxyacids in vitro, such as (S)-lactate, 2-hydroxyoctanoate, and to
CC a lesser extent glycolate, mandelate and 2-hydroxyoctadecanoate, 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=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=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 -!- 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; VYWW01000049; KAA9320359.1; -; Genomic_DNA.
DR RefSeq; WP_006588101.1; NZ_VYWW01000049.1.
DR STRING; 575605.ACQN01000032_gene25; -.
DR GeneID; 66541068; -.
DR KEGG; lje:BUE77_00875; -.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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..408
FT /note="L-lactate oxidase"
FT /id="PRO_0000454870"
FT DOMAIN 14..370
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 40
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 93..95
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 122
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 144
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 146
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 172
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 181
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 241
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 263
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
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 268
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 296..300
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 320
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
SQ SEQUENCE 408 AA; 44229 MW; A1344FE32BD9B5F0 CRC64;
MTVYYKGFPQ SDRNEAIKMV NVDELEDRVR KVMPEAAYYY IASGSENEWT WRNNTAAFNH
FQIVPRSLTN MDNPSTETQF MGMDLKTPIM ICPIACHGIA HKDAEVATAQ GAKAAGALFS
SSTYANRSVE DIATATGDSP KFFQLYLSKD WDFNKMVFDA VKSAGYKGIM LTVDALVSGY
REANLRTNFT FPVPLDFFTR YVGAEGEGMS VAQMYANSAQ KIGPADVAKI KEMSGLPVFV
KGVMNAEDAY MAIGAGADGI VVSNHGGREI DTAPATIDML PEIAAAVNGR VPIILDSGVR
RGSHVFKALA LGADLVGIGR PFLYGLALGG AKGVESVINQ INNEFKILMQ LTGCKTVEDV
KHADIRQINY TADNLPSNTD PSVRRAYPVT KENQMEGTQD AATGASKH
