HAOX1_HUMAN
ID HAOX1_HUMAN Reviewed; 370 AA.
AC Q9UJM8; Q14CQ0; Q9UPZ0; Q9Y3I7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=2-Hydroxyacid oxidase 1 {ECO:0000305|PubMed:10777549};
DE Short=HAOX1 {ECO:0000303|PubMed:10777549};
DE EC=1.1.3.15 {ECO:0000305|PubMed:10777549, ECO:0000305|PubMed:10978532, ECO:0000305|PubMed:17669354, ECO:0000305|PubMed:18215067};
DE AltName: Full=Glycolate oxidase {ECO:0000303|PubMed:10978532};
DE Short=GO {ECO:0000303|PubMed:18215067};
DE Short=GOX {ECO:0000303|PubMed:17669354};
DE AltName: Full=Glyoxylate oxidase {ECO:0000303|PubMed:17669354};
DE EC=1.2.3.5 {ECO:0000305|PubMed:10777549, ECO:0000305|PubMed:17669354, ECO:0000305|PubMed:18215067};
GN Name=HAO1 {ECO:0000303|PubMed:10978532, ECO:0000312|HGNC:HGNC:4809};
GN Synonyms=GOX1 {ECO:0000312|HGNC:HGNC:4809};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND PATHWAY.
RC TISSUE=Liver;
RX PubMed=10978532; DOI=10.1016/s0167-4781(00)00161-5;
RA Williams E.L., Cregeen D.P., Rumsby G.;
RT "Identification and expression of a cDNA for human glycolate oxidase.";
RL Biochim. Biophys. Acta 1493:246-248(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TOPOLOGY,
RP AND TISSUE SPECIFICITY.
RX PubMed=10777549; DOI=10.1074/jbc.275.17.12590;
RA Jones J.M., Morrell J.C., Gould S.J.;
RT "Identification and characterization of HAOX1, HAOX2, and HAOX3, three
RT human peroxisomal 2-hydroxy acid oxidases.";
RL J. Biol. Chem. 275:12590-12597(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Stavrides G.S., Huckle E.J., Deloukas P.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Watanabe T.;
RT "Isolation and characterization of a novel human liver-specific gene
RT homologous to the plant glycolate oxidase by the differential display
RT method.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=17669354; DOI=10.1016/j.abb.2007.06.021;
RA Vignaud C., Pietrancosta N., Williams E.L., Rumsby G., Lederer F.;
RT "Purification and characterization of recombinant human liver glycolate
RT oxidase.";
RL Arch. Biochem. Biophys. 465:410-416(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9] {ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH FMN; GLYOXYLATE AND
RP 4-CARBOXY-5-DODECYLSULFANYL-1,2,3-TRIAZOLE, FUNCTION, COFACTOR, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18215067; DOI=10.1021/bi701710r;
RA Murray M.S., Holmes R.P., Lowther W.T.;
RT "Active site and loop 4 movements within human glycolate oxidase:
RT implications for substrate specificity and drug design.";
RL Biochemistry 47:2439-2449(2008).
RN [10] {ECO:0007744|PDB:2W0U}
RP X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) IN COMPLEX WITH FMN AND THE
RP SYNTHETIC INHIBITOR CCPST.
RX PubMed=20054120; DOI=10.1107/s1744309109041670;
RA Bourhis J.M., Vignaud C., Pietrancosta N., Gueritte F., Guenard D.,
RA Lederer F., Lindqvist Y.;
RT "Structure of human glycolate oxidase in complex with the inhibitor 4-
RT carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole.";
RL Acta Crystallogr. F 65:1246-1253(2009).
RN [11] {ECO:0007744|PDB:2NZL}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH FMN AND GLYOXYLATE.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human hydroxyacid oxidase 1.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Broad substrate specificity (S)-2-hydroxy-acid oxidase that
CC preferentially oxidizes glycolate (PubMed:10777549, PubMed:17669354,
CC PubMed:18215067, PubMed:10978532). The glyoxylate produced by the
CC oxidation of glycolate can then be utilized by alanine-glyoxylate
CC aminotransferase for the peroxisomal synthesis of glycine; this pathway
CC appears to be an important step for the detoxification of glyoxylate
CC which, if allowed to accumulate, may be metabolized to oxalate with
CC formation of kidney stones (PubMed:10978532, PubMed:17669354). Can also
CC catalyze the oxidation of glyoxylate, and long chain hydroxyacids such
CC as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate, albeit with much
CC lower catalytic efficiency (PubMed:10777549, PubMed:17669354,
CC PubMed:18215067). Active in vitro with the artificial electron acceptor
CC 2,6-dichlorophenolindophenol (DCIP), but O2 is believed to be the
CC physiological electron acceptor, leading to the production of H2O2
CC (PubMed:10777549, PubMed:17669354, PubMed:18215067, PubMed:10978532).
CC Is not active on L-lactate and 2-hydroxybutanoate (PubMed:10777549).
CC {ECO:0000269|PubMed:10777549, ECO:0000269|PubMed:10978532,
CC ECO:0000269|PubMed:17669354, ECO:0000269|PubMed:18215067,
CC ECO:0000303|PubMed:10978532, ECO:0000303|PubMed:17669354}.
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:0000305|PubMed:10777549, ECO:0000305|PubMed:17669354,
CC ECO:0000305|PubMed:18215067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16790;
CC Evidence={ECO:0000305|PubMed:10777549};
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:0000305|PubMed:10777549, ECO:0000305|PubMed:10978532,
CC ECO:0000305|PubMed:17669354, ECO:0000305|PubMed:18215067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312;
CC Evidence={ECO:0000305|PubMed:10978532, ECO:0000305|PubMed:17669354};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + H2O + O2 = H(+) + H2O2 + oxalate;
CC Xref=Rhea:RHEA:14837, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:30623,
CC ChEBI:CHEBI:36655; EC=1.2.3.5; Evidence={ECO:0000305|PubMed:10777549,
CC ECO:0000305|PubMed:17669354, ECO:0000305|PubMed:18215067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14838;
CC Evidence={ECO:0000305|PubMed:17669354};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyhexadecanoate + O2 = 2-oxohexadecanoate + H2O2;
CC Xref=Rhea:RHEA:67944, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:65097, ChEBI:CHEBI:176593;
CC Evidence={ECO:0000305|PubMed:10777549, ECO:0000305|PubMed:18215067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67945;
CC Evidence={ECO:0000305|PubMed:10777549};
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:0000305|PubMed:10777549, ECO:0000305|PubMed:18215067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67941;
CC Evidence={ECO:0000305|PubMed:10777549};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:17669354, ECO:0000269|PubMed:18215067};
CC -!- ACTIVITY REGULATION: Inhibited by its product oxalate
CC (PubMed:17669354). Inhibited by high concentrations of
CC dichlorophenolindophenol (DCIP) in vitro (PubMed:17669354).
CC {ECO:0000269|PubMed:17669354}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for glycolate (at pH 7.5, with DCIP as electron acceptor)
CC {ECO:0000269|PubMed:10777549};
CC KM=141 uM for glycolate (at pH 7.5 and 37 degrees Celsius, with DCIP
CC as electron acceptor) {ECO:0000269|PubMed:18215067};
CC KM=56 uM for glycolate (at pH 7.0 and 37 degrees Celsius, with DCIP
CC as electron acceptor) {ECO:0000269|PubMed:17669354};
CC KM=40 uM for 2-hydroxy octanoate (at pH 7.5 and 37 degrees Celsius,
CC with DCIP as electron acceptor) {ECO:0000269|PubMed:18215067};
CC KM=2200 uM for glyoxylate (at pH 7.5 and 37 degrees Celsius, with
CC DCIP as electron acceptor) {ECO:0000269|PubMed:18215067};
CC KM=3400 uM for glyoxylate (at pH 7.0 and 37 degrees Celsius, with
CC DCIP as electron acceptor) {ECO:0000269|PubMed:17669354};
CC KM=16.5 mM for L-lactate (at pH 7.0 and 37 degrees Celsius, with DCIP
CC as electron acceptor) {ECO:0000269|PubMed:17669354};
CC KM=1.5 mM for L-mandelate (at pH 7.0 and 37 degrees Celsius, with
CC DCIP as electron acceptor) {ECO:0000269|PubMed:17669354};
CC Note=kcat is 3.6 sec(-1) for the oxidation of glycolate with DCIP as
CC electron acceptor (at pH 7.0 and 37 degrees Celsius)
CC (PubMed:17669354). kcat is 4.1 sec(-1) for the oxidation of glycolate
CC with DCIP as electron acceptor (at pH 7.5 and 37 degrees Celsius)
CC (PubMed:18215067). kcat is 0.7 sec(-1) for the oxidation of
CC glyoxylate with DCIP as electron acceptor (at pH 7.5 and 37 degrees
CC Celsius) (PubMed:18215067). kcat is 0.83 sec(-1) for the oxidation of
CC glyoxylate with DCIP as electron acceptor (at pH 7.0 and 37 degrees
CC Celsius) (PubMed:17669354). kcat is 0.46 sec(-1) for the oxidation of
CC L-lactate with DCIP as electron acceptor (at pH 7.0 and 37 degrees
CC Celsius) (PubMed:17669354). kcat is 0.11 sec(-1) for the oxidation of
CC L-mandelate with DCIP as electron acceptor (at pH 7.0 and 37 degrees
CC Celsius) (PubMed:17669354). Shows a higher catalytic efficiency for
CC glycolate compared to glyoxylate (PubMed:17669354, PubMed:18215067).
CC {ECO:0000269|PubMed:17669354, ECO:0000269|PubMed:18215067};
CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis.
CC {ECO:0000303|PubMed:10978532}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17669354}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:10777549}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver.
CC {ECO:0000269|PubMed:10777549, ECO:0000269|PubMed:10978532}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
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DR EMBL; AF244134; AAF63219.1; -; mRNA.
DR EMBL; AF231916; AAF40199.1; -; mRNA.
DR EMBL; AL121739; CAB57329.1; -; mRNA.
DR EMBL; AB024079; BAA82872.1; -; mRNA.
DR EMBL; AL021879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113665; AAI13666.1; -; mRNA.
DR EMBL; BC113667; AAI13668.1; -; mRNA.
DR CCDS; CCDS13100.1; -.
DR RefSeq; NP_060015.1; NM_017545.2.
DR PDB; 2NZL; X-ray; 1.35 A; A=1-370.
DR PDB; 2RDT; X-ray; 1.95 A; A=1-370.
DR PDB; 2RDU; X-ray; 1.65 A; A=1-370.
DR PDB; 2RDW; X-ray; 1.95 A; A=1-370.
DR PDB; 2W0U; X-ray; 2.84 A; A/B/C/D=1-370.
DR PDB; 5QIB; X-ray; 1.48 A; A=1-368.
DR PDB; 5QIC; X-ray; 1.34 A; A=1-368.
DR PDB; 5QID; X-ray; 1.45 A; A=1-368.
DR PDB; 5QIE; X-ray; 1.34 A; A=1-368.
DR PDB; 5QIF; X-ray; 1.20 A; A=1-368.
DR PDB; 5QIG; X-ray; 1.42 A; A=1-368.
DR PDB; 5QIH; X-ray; 1.33 A; A=1-368.
DR PDB; 6GMB; X-ray; 1.35 A; A=1-362.
DR PDB; 6GMC; X-ray; 1.20 A; A=1-362.
DR PDB; 6W44; X-ray; 1.64 A; A=1-368.
DR PDB; 6W45; X-ray; 1.70 A; A=1-368.
DR PDB; 6W4C; X-ray; 1.75 A; A=1-368.
DR PDB; 7M2O; X-ray; 2.07 A; A=1-370.
DR PDB; 7R4N; X-ray; 1.70 A; A=1-362.
DR PDBsum; 2NZL; -.
DR PDBsum; 2RDT; -.
DR PDBsum; 2RDU; -.
DR PDBsum; 2RDW; -.
DR PDBsum; 2W0U; -.
DR PDBsum; 5QIB; -.
DR PDBsum; 5QIC; -.
DR PDBsum; 5QID; -.
DR PDBsum; 5QIE; -.
DR PDBsum; 5QIF; -.
DR PDBsum; 5QIG; -.
DR PDBsum; 5QIH; -.
DR PDBsum; 6GMB; -.
DR PDBsum; 6GMC; -.
DR PDBsum; 6W44; -.
DR PDBsum; 6W45; -.
DR PDBsum; 6W4C; -.
DR PDBsum; 7M2O; -.
DR PDBsum; 7R4N; -.
DR AlphaFoldDB; Q9UJM8; -.
DR SMR; Q9UJM8; -.
DR BioGRID; 119941; 5.
DR IntAct; Q9UJM8; 3.
DR STRING; 9606.ENSP00000368066; -.
DR BindingDB; Q9UJM8; -.
DR ChEMBL; CHEMBL4229; -.
DR DrugBank; DB07907; (2S)-2-HYDROXYOCTANOIC ACID.
DR DrugBank; DB07060; 3-(INDOL-3-YL) LACTATE.
DR DrugBank; DB03064; 3-Decyl-2,5-Dioxo-4-Hydroxy-3-Pyrroline.
DR DrugBank; DB04374; 4-Carboxy-5-(1-Pentyl)Hexylsulfanyl-1,2,3-Triazole.
DR DrugBank; DB06979; 5-(dodecylthio)-1H-1,2,3-triazole-4-carboxylic acid.
DR DrugBank; DB02279; Benzoylformic Acid.
DR DrugBank; DB03247; Flavin mononucleotide.
DR DrugBank; DB15935; Lumasiran.
DR DrugBank; DB02164; N-sulfo-flavin mononucleotide.
DR DrugBank; DB03884; Phenylpyruvic acid.
DR iPTMnet; Q9UJM8; -.
DR PhosphoSitePlus; Q9UJM8; -.
DR BioMuta; HAO1; -.
DR DMDM; 13124294; -.
DR MassIVE; Q9UJM8; -.
DR PaxDb; Q9UJM8; -.
DR PeptideAtlas; Q9UJM8; -.
DR PRIDE; Q9UJM8; -.
DR ProteomicsDB; 84633; -.
DR Antibodypedia; 8448; 411 antibodies from 32 providers.
DR DNASU; 54363; -.
DR Ensembl; ENST00000378789.4; ENSP00000368066.3; ENSG00000101323.5.
DR GeneID; 54363; -.
DR KEGG; hsa:54363; -.
DR MANE-Select; ENST00000378789.4; ENSP00000368066.3; NM_017545.3; NP_060015.1.
DR UCSC; uc002wmw.2; human.
DR CTD; 54363; -.
DR DisGeNET; 54363; -.
DR GeneCards; HAO1; -.
DR HGNC; HGNC:4809; HAO1.
DR HPA; ENSG00000101323; Tissue enriched (liver).
DR MIM; 605023; gene.
DR neXtProt; NX_Q9UJM8; -.
DR OpenTargets; ENSG00000101323; -.
DR PharmGKB; PA29185; -.
DR VEuPathDB; HostDB:ENSG00000101323; -.
DR eggNOG; KOG0538; Eukaryota.
DR GeneTree; ENSGT00390000018717; -.
DR HOGENOM; CLU_020639_6_1_1; -.
DR InParanoid; Q9UJM8; -.
DR OMA; FTRLMQT; -.
DR OrthoDB; 879633at2759; -.
DR PhylomeDB; Q9UJM8; -.
DR TreeFam; TF313363; -.
DR BRENDA; 1.1.3.15; 2681.
DR PathwayCommons; Q9UJM8; -.
DR Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SABIO-RK; Q9UJM8; -.
DR SignaLink; Q9UJM8; -.
DR UniPathway; UPA00288; -.
DR BioGRID-ORCS; 54363; 8 hits in 1068 CRISPR screens.
DR EvolutionaryTrace; Q9UJM8; -.
DR GenomeRNAi; 54363; -.
DR Pharos; Q9UJM8; Tclin.
DR PRO; PR:Q9UJM8; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9UJM8; protein.
DR Bgee; ENSG00000101323; Expressed in right lobe of liver and 31 other tissues.
DR ExpressionAtlas; Q9UJM8; baseline and differential.
DR Genevisible; Q9UJM8; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0047969; F:glyoxylate oxidase activity; IDA:UniProtKB.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IDA:UniProtKB.
DR GO; GO:0006545; P:glycine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046296; P:glycolate catabolic process; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
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 3D-structure; Amino-acid biosynthesis; Flavoprotein; FMN; Oxidoreductase;
KW Peroxisome; Phosphoprotein; Reference proteome.
FT CHAIN 1..370
FT /note="2-Hydroxyacid oxidase 1"
FT /id="PRO_0000206318"
FT DOMAIN 1..365
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT MOTIF 368..370
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 26
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000269|PubMed:18215067,
FT ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU"
FT BINDING 79..81
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18215067,
FT ECO:0000269|PubMed:20054120, ECO:0007744|PDB:2RDT,
FT ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW,
FT ECO:0007744|PDB:2W0U"
FT BINDING 108
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683,
FT ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120,
FT ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL,
FT ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU,
FT ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U"
FT BINDING 130
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683,
FT ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120,
FT ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU,
FT ECO:0007744|PDB:2W0U"
FT BINDING 132
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000269|PubMed:18215067,
FT ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU"
FT BINDING 158
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683,
FT ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120,
FT ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL,
FT ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU,
FT ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U"
FT BINDING 167
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000269|PubMed:18215067, ECO:0000269|Ref.11,
FT ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU"
FT BINDING 236
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683,
FT ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120,
FT ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL,
FT ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU,
FT ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U"
FT BINDING 258
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18215067,
FT ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11,
FT ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT,
FT ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW,
FT ECO:0007744|PDB:2W0U"
FT BINDING 260
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000269|PubMed:18215067,
FT ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU"
FT BINDING 263
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000269|PubMed:18215067,
FT ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU"
FT BINDING 291..295
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18215067,
FT ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11,
FT ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT,
FT ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW,
FT ECO:0007744|PDB:2W0U"
FT BINDING 314..315
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18215067,
FT ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11,
FT ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT,
FT ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW,
FT ECO:0007744|PDB:2W0U"
FT MOD_RES 184
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU19"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU19"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:5QIF"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:5QIF"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:7M2O"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5QIF"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:5QIF"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:5QIF"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:5QIF"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6GMC"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:5QIF"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:5QIF"
FT TURN 189..193
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 204..212
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:5QIF"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:5QIF"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:5QIF"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:5QIF"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 315..347
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:5QIF"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:5QIF"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:6W45"
SQ SEQUENCE 370 AA; 40924 MW; C683C6F7CB5FD323 CRC64;
MLPRLICIND YEQHAKSVLP KSIYDYYRSG ANDEETLADN IAAFSRWKLY PRMLRNVAET
DLSTSVLGQR VSMPICVGAT AMQRMAHVDG ELATVRACQS LGTGMMLSSW ATSSIEEVAE
AGPEALRWLQ LYIYKDREVT KKLVRQAEKM GYKAIFVTVD TPYLGNRLDD VRNRFKLPPQ
LRMKNFETST LSFSPEENFG DDSGLAAYVA KAIDPSISWE DIKWLRRLTS LPIVAKGILR
GDDAREAVKH GLNGILVSNH GARQLDGVPA TIDVLPEIVE AVEGKVEVFL DGGVRKGTDV
LKALALGAKA VFVGRPIVWG LAFQGEKGVQ DVLEILKEEF RLAMALSGCQ NVKVIDKTLV
RKNPLAVSKI
