LOX_CHLRE
ID LOX_CHLRE Reviewed; 384 AA.
AC F8WQN2; A8IEL8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=L-lactate oxidase {ECO:0000303|PubMed:21828292};
DE Short=LOX {ECO:0000303|PubMed:21828292};
DE EC=1.1.3.- {ECO:0000269|PubMed:21828292};
DE AltName: Full=Cr-LOX {ECO:0000303|PubMed:21828292};
GN ORFNames=CHLRE_03g171300v5 {ECO:0000312|EMBL:PNW85092.1},
GN CHLREDRAFT_127775 {ECO:0000312|EMBL:EDP06163.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=137c mt+;
RX PubMed=21828292; DOI=10.1105/tpc.111.088070;
RA Hackenberg C., Kern R., Huge J., Stal L.J., Tsuji Y., Kopka J.,
RA Shiraiwa Y., Bauwe H., Hagemann M.;
RT "Cyanobacterial lactate oxidases serve as essential partners in N2 fixation
RT and evolved into photorespiratory glycolate oxidases in plants.";
RL Plant Cell 23:2978-2990(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RG Chlamydomonas Annotation Team;
RG JGI Annotation Team;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Grigoriev I.V., Rokhsar D.S.;
RT "WGS assembly of Chlamydomonas reinhardtii.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of (S)-lactate (L-lactate) to
CC pyruvate, with a reduction of O2 to H2O2. Also shows a low oxidase
CC activity with glycolate in vitro. The very low glycolate oxidase
CC activity indicates that this enzyme is unlikely to be involved in
CC photorespiratory glycolate metabolism, a pathway in which the oxidation
CC of glycolate is taken over by glycolate dehydrogenase (GlcD).
CC {ECO:0000269|PubMed:21828292}.
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:21828292};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55869;
CC Evidence={ECO:0000305|PubMed:21828292};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.081 mM for (S)-lactate {ECO:0000269|PubMed:21828292};
CC KM=1.244 mM for glycolate {ECO:0000269|PubMed:21828292};
CC KM=0.29 uM for O2 {ECO:0000269|PubMed:21828292};
CC Vmax=10.59 umol/min/mg enzyme with (S)-lactate as substrate
CC {ECO:0000269|PubMed:21828292};
CC Vmax=0.189 umol/min/mg enzyme with glycolate as substrate
CC {ECO:0000269|PubMed:21828292};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q44467}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP06163.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB610509; BAK61668.1; -; mRNA.
DR EMBL; DS496116; EDP06163.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM008964; PNW85092.1; -; Genomic_DNA.
DR RefSeq; XP_001703481.1; XM_001703429.1.
DR STRING; 3055.EDP06163; -.
DR PRIDE; F8WQN2; -.
DR EnsemblPlants; PNW85092; PNW85092; CHLRE_03g171300v5.
DR GeneID; 5728931; -.
DR Gramene; PNW85092; PNW85092; CHLRE_03g171300v5.
DR eggNOG; KOG0538; Eukaryota.
DR HOGENOM; CLU_020639_6_1_1; -.
DR OMA; FTRLMQT; -.
DR OrthoDB; 879633at2759; -.
DR BRENDA; 1.1.3.2; 1318.
DR Proteomes; UP000006906; Chromosome 3.
DR ExpressionAtlas; F8WQN2; baseline.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
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 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..384
FT /note="L-lactate oxidase"
FT /id="PRO_0000454867"
FT DOMAIN 1..369
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 27
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 80..82
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 109
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 130
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 132
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 158
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q44467"
FT BINDING 167
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
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 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 384 AA; 41308 MW; AF5614C041DE19CB CRC64;
MADLSFLNLE EVEEEAKKVM PKMAFDYYST GSDTCYTVGE NRSCFSRYLL LPRMLRNVSR
VDTSHELFGI RSSMPVWVAP MAMHGLAHPG REVATCRAAA AAGVPFTFST VATSSLQEIQ
ETGHDNRIFQ LYVIRNREVV RRWVTEAESR GFKALMVTVD AQRLGNREAD ARNKFTLPPG
LALRNLEYLS SASTVQARDS QDGSGLMKLF TSEVDDSLTW EFIPWLRGVT KLPIIVKGLL
SPADAELAVQ YGVDGIVVSN HGGRQLDYAP SGLHMLPAVV AAVRGCGSSI PVLVDGGVRR
GTDVIKALAL GASGVLLGRP VLYGLAVGGQ AGVERVLQLL RSEIELSMAL AGCSSVQQIG
PQLLLPAPSA GPAPPMPAAQ LCKL
