Search Results

Overview

Uniprot IDQ9UJM8
Protein Name2-Hydroxyacid oxidase 1
Gene NameHAO1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
149 KLVRQAEKMGYKAIF
176 DDVRNRFKLPPQLRM
223 SISWEDIKWLRRLTS
236 TSLPIVAKGILRGDD
249 DDAREAVKHGLNGIL
302 RKGTDVLKALALGAK
309 KALALGAKAVFVGRP
353 LSGCQNVKVIDKTLV
357 QNVKVIDKTLVRKNP
362 IDKTLVRKNPLAVSK
369 KNPLAVSKI******

Function

Broad substrate specificity (S)-2-hydroxy-acid oxidase that preferentially oxidizes glycolate (PubMed:10777549, PubMed:10978532, PubMed:17669354, PubMed:18215067). The glyoxylate produced by the oxidation of glycolate can then be utilized by alanine-glyoxylate aminotransferase for the peroxisomal synthesis of glycine; this pathway appears to be an important step for the detoxification of glyoxylate which, if allowed to accumulate, may be metabolized to oxalate with formation of kidney stones (PubMed:10978532, PubMed:17669354). Can also catalyze the oxidation of glyoxylate, and long chain hydroxyacids such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate, albeit with much lower catalytic efficiency (PubMed:10777549, PubMed:17669354, PubMed:18215067). Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP), but O2 is believed to be the physiological electron acceptor, leading to the production of H2O2 (PubMed:10777549, PubMed:10978532, PubMed:17669354, PubMed:18215067). Is not active on L-lactate and 2-hydroxybutanoate (PubMed:10777549)

Protein Sequence

10 MLPRLICIND 20 YEQHAKSVLP 30 KSIYDYYRSG 40 ANDEETLADN 50 IAAFSRWKLY 60 PRMLRNVAET 70 DLSTSVLGQR 80 VSMPICVGAT 90 AMQRMAHVDG 100 ELATVRACQS 110 LGTGMMLSSW 120 ATSSIEEVAE 130 AGPEALRWLQ 140 LYIYKDREVT 150 KKLVRQAEKM 160 GYKAIFVTVD 170 TPYLGNRLDD 180 VRNRFKLPPQ 190 LRMKNFETST 200 LSFSPEENFG 210 DDSGLAAYVA 220 KAIDPSISWE 230 DIKWLRRLTS 240 LPIVAKGILR 250 GDDAREAVKH 260 GLNGILVSNH 270 GARQLDGVPA 280 TIDVLPEIVE 290 AVEGKVEVFL 300 DGGVRKGTDV 310 LKALALGAKA 320 VFVGRPIVWG 330 LAFQGEKGVQ 340 DVLEILKEEF 350 RLAMALSGCQ 360 NVKVIDKTLV 370 RKNPLAVSKI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005782 peroxisomal matrix
Molecular Function GO:0003973 (S)-2-hydroxy-acid oxidase activity
Molecular Function GO:0010181 FMN binding
Molecular Function GO:0047969 glyoxylate oxidase activity
Biological Process GO:0001561 fatty acid alpha-oxidation
Biological Process GO:0006545 glycine biosynthetic process
Biological Process GO:0046296 glycolate catabolic process
Biological Process GO:0006979 response to oxidative stress

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.