LOX_LENH9
ID LOX_LENH9 Reviewed; 369 AA.
AC C0XIJ3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, 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};
GN Name=haox {ECO:0000312|EMBL:EEI24763.1};
GN ORFNames=HMPREF0519_1054 {ECO:0000312|EMBL:EEI24763.1};
OS Lentilactobacillus hilgardii (strain ATCC 8290 / DSM 20176 / CCUG 30140 /
OS JCM 1155 / KCTC 3500 / NBRC 15886 / NCIMB 8040 / NRRL B-1843 / 9).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423757;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8290 / DSM 20176 / CCUG 30140 / JCM 1155 / KCTC 3500 / NBRC
RC 15886 / NCIMB 8040 / NRRL B-1843 / 9;
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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 (PubMed:34555022). May be
CC involved in the utilization of L-lactate as an energy source for growth
CC (By similarity). {ECO:0000250|UniProtKB:O33655,
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55869;
CC Evidence={ECO:0000305};
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; ACGP01000115; EEI24763.1; -; Genomic_DNA.
DR RefSeq; WP_003556662.1; NZ_GG669992.1.
DR EnsemblBacteria; EEI24763; EEI24763; HMPREF0519_1054.
DR PATRIC; fig|1423757.3.peg.2304; -.
DR HOGENOM; CLU_020639_6_1_9; -.
DR OrthoDB; 1186741at2; -.
DR Proteomes; UP000003752; 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 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; Reference proteome.
FT CHAIN 1..369
FT /note="L-lactate oxidase"
FT /id="PRO_0000454871"
FT DOMAIN 13..369
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 39
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 92..94
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 121
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 143
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 145
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 171
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 180
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 240
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 262
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
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 267
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 295..299
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 319
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
SQ SEQUENCE 369 AA; 39362 MW; 2D36712A906BA5D7 CRC64;
MVVVNGYKQN ENEKKLNVLN LDQLEKQAKE IIPTGGFGYI SGGSEDEWTL RENRRAFTHK
QIVPRALTNI EKPELETNVF GIPLKTPLFM VPAAAQGLAH VKGEVDTAKG VAAVGGLMAQ
STYSSTSIAD TAASGTGAPQ FFQLYMSKDW DFNEALLDEA KRAGVKGIIL TVDATVDGYR
EADIINNFQF PIPMANLTKY SEDDGQGKGI AEIYASAAQK IGSDDVARIA NYTDLPVIVK
GIESPEDALY AIGAGASGIY VSNHGGRQLN GGPASFDVLE DVAKAVNGKV PVIFDSGIRR
GSDVFKALAS GADLVGIGRP VIYGLALGGA QGVQSVFEHL DHELEIIMQL AGTKTISDVK
NAKLLNIRY
